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1,2-dipalmitoyl-sn-glycerol + GTP
GDP + 1,2-dipalmitoyl-sn-glycerol 3-phosphate
2'-deoxy-ATP + sn-1,2-dihexanoylglycerol
2'-deoxy-ADP + sn-1,2-dihexanoylglycerol 3-phosphate
-
-
-
-
?
ADP + sn-1,2-dihexanoylglycerol
AMP + sn-1,2-dihexanoylglycerol 3-phosphate
-
MgADP- is a very poor phosphoryl donor
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
ATP + 1,2-diarachidonoyl-glycerol
ADP + 1,2-diarachidonoyl-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diarachidonoyl-sn-glycerol
ADP + 1,2-diarachidonoyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-dicapryl-sn-glycerol
ADP + 1,2-dicapryl-sn-glycerol 3-phosphate
about 140% of the activity with sn-1,2-dioleoylglycerol
-
-
?
ATP + 1,2-didecanoylglycerol
ADP + 1,2-didecanoylglycerol 3-phosphate
-
enzyme type I: activity is 157% of the activity with rac-1,2-dioleoylglycerol, enzyme type II: activity is 141% of the activity with rac-1,2-dioleoylglycerol
-
-
?
ATP + 1,2-didodecanoylglycerol
ADP + 1,2-didodecanoylglycerol 3-phosphate
-
enzyme type I: activity is 107% of the activity with rac-1,2-dioleoylglycerol, enzyme type II: activity is 227% of the activity with rac-1,2-dioleoylglycerol
-
-
?
ATP + 1,2-dihexadecanoylglycerol
ADP + 1,2-dihexadecanoylglycerol 3-phosphate
-
enzyme type I: activity is 198% of the activity with rac-1,2-dioleoylglycerol, enzyme type II: activity is 231% of the activity with rac-1,2-dioleoylglycerol
-
-
?
ATP + 1,2-dihexanoyl-sn-glycerol
ADP + 1,2-dihexanoyl-sn-glycerol 3-phosphate
ATP + 1,2-dihexanoylglycerol
ADP + 1,2-dihexanoylglycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-dilauroyl-sn-glycerol
ADP + 1,2-dilauroyl-sn-glycerol 3-phosphate
high activity
-
-
?
ATP + 1,2-dilinoleoyl-sn-glycerol
ADP + 1,2-dilinoleoyl-sn-glycerol
-
-
-
?
ATP + 1,2-dioctanoyl-sn-glycerol
ADP + 1,2-dioctanoyl-sn-glycerol 3-phosphate
ATP + 1,2-dioctanoylglycerol
ADP + 1,2-dioctanoylglycerol 3-phosphate
ATP + 1,2-dioleolyl-sn-glycerol
ADP + 1,2-dioleolyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-dioleoyl-sn-glycerol
ADP + 1,2-dioleoyl-sn-glycerol 3-phosphate
ATP + 1,2-dioleoylglycerol
ADP + 1,2-dioleoylglycerol 3-phospate
ATP + 1,2-dipalmitoyl-sn-glycerol
ADP + 1,2-dipalmitoyl-sn-glycerol 3-phosphate
ATP + 1,2-distearoyl-sn-glycerol
ADP + 1,2-distearoyl-sn-glycerol 3-phosphate
high activity
-
-
?
ATP + 1,2-ditetradecanoylglycerol
ADP + 1,2-ditetradecanoylglycerol 3-phosphate
-
enzyme type I: activity is 200% of the activity with rac-1,2-dioleoylglycerol, enzyme type II: activity is 262% of the activity with rac-1,2-dioleoylglycerol
-
-
?
ATP + 1,3-dioleoyl-sn-glycerol
ADP + 1,3-dioleoyl-sn-glycerol 2-phosphate
-
low activity, about 4% of the activity with 1,2-dioleoyl-sn-glycerol
-
-
?
ATP + 1-arachidoyl-2-arachidonoyl-sn-glycerol
ADP + ?
isoform DGKepsilon shows about 70% activity with 0.38 mol% 1-arachidoyl-2-arachidonoyl-sn-glycerol compared to 1-stearoyl-2-arachidonoyl-sn-glycerol
-
-
?
ATP + 1-NBD-decanoyl-2-decanoyl-sn-glycerol
ADP + 1-NBD-decanoyl-2-decanoyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1-O-hexadecyl-2-oleoyl-sn-glycerol
ADP + 1-O-hexadecyl-2-oleoyl-sn-glycerol 3-phosphate
-
45.4% of the activity with 1-stearoyl-2-arachidonoyl-sn-glycerol
-
-
?
ATP + 1-O-hexadecyl-2-sn-acetyl glycerol
ADP + 1-O-hexadecyl-2-sn-acetyl glycerol 3-phosphate
-
about 12fold the rate of 1-O-hexadecyl-sn-glycerol phosphorylation, isoforms diacylglycerol kinase alpha, beta, gamma, delta1, delta1, zeta, jota, theta
-
-
?
ATP + 1-O-hexadecyl-sn-glycerol
ADP + 1-O-hexadecyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1-O-hexanoyl-2-arachidonoyl-sn-glycerol
ADP + 1-O-hexanoyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
preferred by isozyme DGKzeta and isozyme DGKalpha
-
-
?
ATP + 1-O-hexanoyl-2-oleoyl-sn-glycerol
ADP + 1-O-hexanoyl-2-oleoyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1-oleoyl-2-palmitoyl-sn-glycerol
ADP + 1-palmitoyl-2-oleoyl-sn-glycerol 3-phosphate
about 85% of the activity with sn-1,2-dioleoylglycerol, DGKksi
-
-
?
ATP + 1-palmitoyl-2-arachidonoyl-sn-glycerol
ADP + 1-palmitoyl-2-arachidonoyl-sn-glycerol 3-phosphate
ATP + 1-palmitoyl-2-linoleoyl-sn-glycerol
ADP + 1-palmitoyl-2-linoleoyl-sn-glycerol 3-phosphate
-
enzyme type I: activity is 116% of the activity with rac-1,2-dioleoylglycerol, enzyme type II: activity is 86% of the activity with rac-1,2-dioleoylglycerol
-
-
?
ATP + 1-palmitoyl-2-oleolyl-sn-glycerol
ADP + 1-palmitoyl-2-oleolyl-sn-glycerol 3-phosphate
high activity
-
-
?
ATP + 1-palmitoyl-2-oleoyl-sn-glycerol
ADP + 1-palmitoyl-2-oleoyl-sn-glycerol 3-phosphate
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
ATP + 1-stearoyl-2-arachidonoylglycerol
ADP + 1-stearoyl-2-arachidonoylglycerol 3-phosphate
-
preferred enzyme, 6fold higher activity compared to substrate 1,2-dioleoylglycerol
-
-
?
ATP + 1-stearoyl-2-docosahexaenoyl-sn-glycerol
ADP + 1-stearoyl-2-docosahexaenoyl-sn-glycerol 3-phosphate
ATP + 1-stearoyl-2-eicosatetraenoyl-sn-glycerol
ADP + 1-stearoyl-2-eicosatetraenoyl-sn-glycerol 3-phosphate
high activity
-
-
?
ATP + 1-stearoyl-2-linoleoyl-sn-glycerol
ADP + 1-stearoyl-2-linoleoyl-sn-glycerol 3-phosphate
ATP + 1-stearoyl-2-oleoyl-sn-glycerol
ADP + 1-stearoyl-2-oleoyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 2,3-dioleoyl-sn-glycerol
ADP + 2,3-diacyl-sn-glycerol 1-phosphate
ATP + 2-arachidonoyl-sn-glycerol
ADP + 2-arachidonoyl-sn-glycerol 3-phosphate
isoform DGKepsilon shows substrate specificity for sn-2 arachidonoyl-diacylglycerol
-
-
?
ATP + 2-monooleoyl-rac-glycerol
ADP + 2-monooleoyl-rac-glycerol 3-phosphate
-
10.7% of the activity with 1-stearoyl-2-arachidonoyl-sn-glycerol
-
-
?
ATP + ceramide
ADP + ceramide 3-phosphate
ATP + rac-1,2-dioleoylglycerol
ADP + rac-1,2-dioleoylglycerol 3-phosphate
-
-
-
-
?
ATP + sn-1,2-dihexanoylglycerol
ADP + sn-1,2-dihexanoylglycerol 3-phosphate
-
-
-
-
?
ATP + sn-1,2-dioctanoylglycerol
ADP + sn-1,2-dioctanoylglycerol 3-phosphate
-
-
-
-
?
ATP + sn-1,2-dioleoylglycerol
ADP + sn-1,2-dioleoylglycerol 3-phosphate
ATP + sn-1,3-dioleoylglycerol
ADP + ?
about 10% of the activity with sn-1,2-dioleoylglycerol
-
-
?
GTP + 1,2-diacyl-sn-glycerol
GDP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
GTP + dioleoylglycerol
GDP + dioleoylglycerol 3-phosphate
-
-
-
-
?
GTP + sn-1,2-dihexanoylglycerol
GDP + sn-1,2-dihexanoylglycerol 3-phosphate
-
-
-
-
?
ITP + sn-1,2-dihexanoylglycerol
IDP + sn-1,2-dihexanoylglycerol 3-phosphate
-
-
-
-
?
additional information
?
-
1,2-dipalmitoyl-sn-glycerol + GTP
GDP + 1,2-dipalmitoyl-sn-glycerol 3-phosphate
-
-
-
-
?
1,2-dipalmitoyl-sn-glycerol + GTP
GDP + 1,2-dipalmitoyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
enzyme is more active toward long-chain diacylglycerol compared with short-chain diacylglycerol
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
nuclear DGK-theta is activated in response to alpha-thrombin
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
the enzyme may have an important function in the adult nervous system and muscle and during the development of the embryonic nervous system
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme functions to recycle diacylglycerol which is generated largely as a by-product of membrane-derived oligosaccharide biosynthesis
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
enzyme DgkA primarily recognizes diacylglycerol in the glycerol backbone and ester linkages but not the fatty acyl group
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
DGKiota may have important cellular functions in retina and brain
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
the expression of DGKeta2 is suppressed by glucocorticoid in contrast to the marked induction of DGKeta1
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
DGKgamma negatively regulates macrophage differentiation through its catalytic action operating on the cytoskeleton
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
the enzyme plays a role in cellular processes by regulating the intracellular concentration of the second messenger diacylglycerol. DGKeta may play a more general role in regulating cellular diacylglycerol levels
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
DAGKalpha is stimulated vby Src-like kinase-dependent phosphoinositide 3 kinase activation in lymphocytes. In vivo the increase in cellular levels of Src-like kinase-dependent phosphoinositide 3 kinase products is sufficient to induce DAGKalpha activation, allowing DAGKalpha relocation to the intact lymphocyte
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
high level expression of DGKalpha is induced following a signal transmitted through the pre-T-cell-receptor and the protein tyrosine kinase lck. Activity of DGKalpha contributes to survival in CD4+ 8+ double positive thymocytes as pharmacological inhibition of DGK activity results in death of this cell population both in cell suspension and thymic explants. DGKalpha promotes survival in theses thymocytes through a Bcl-regulated pathway
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme is involved in resynthesis of phosphatidylinositol by converting a second messenger diacylglycerol to phosphatidic acid
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme may regulate the intracellular concentration of diacylglycerol
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
DGK-Ialpha is involved in IL-2-mediated lymphocyte proliferation
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the 80000 Da and the 150000 Da enzyme form do not possess specificity towards diacylglycerol molecular species
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
i.e. phosphatidic acid
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
i.e. phosphatidic acid
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
1,2-diacyl-sn-glycerol 3-phosphate is phosphatidic acid
-
ir
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme binds and regulates signalling proteins which are activated by either diacylglycerol or phosphatidic acid
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
i.e. phosphatidic acid
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
1,2-diacyl-sn-glycerol 3-phosphate is phosphatidic acid
-
ir
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme binds and regulates signalling proteins which are activated by either diacylglycerol or phosphatidic acid, isozyme dgk-1 regulates diacylglycerol signalling required for acetylcholine release
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
i.e. phosphatidic acid
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
1,2-diacyl-sn-glycerol 3-phosphate is phosphatidic acid
-
ir
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme binds and regulates signalling proteins which are activated by either diacylglycerol or phosphatidic acid
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
r
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
i.e. phosphatidic acid
-
r
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
r
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
i.e. phosphatidic acid
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme binds and regulates signalling proteins which are activated by either diacylglycerol or phosphatidic acid
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
1,2-diacylglycerol is a second messenger
i.e. phosphatidic acid
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
i.e. phosphatidic acid
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme binds and regulates signalling proteins which are activated by either diacylglycerol or phosphatidic acid
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
1,2-diacyl-sn-glycerol 3-phosphate is phosphatidic acid
-
ir
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
DGKepsilon exhibits specificity for diacylglcerol substrates containing an arachidonoyl chain in the sn-2 position
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
i.e. phosphatidic acid
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
second messenger and intermediate in lipid synthesis
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
termination of diacylglycerol signaling, isozymes DGKalpha, DGKbeta, and DGKgamma play a pivotal role in development and metabolism of brain
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
1,2-diacyl-sn-glycerol 3-phosphate is phosphatidic acid
-
ir
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
reaction takes place during stimulated phosphatidylinositol turnover
-
-
?
ATP + 1,2-dihexanoyl-sn-glycerol
ADP + 1,2-dihexanoyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-dihexanoyl-sn-glycerol
ADP + 1,2-dihexanoyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-dioctanoyl-sn-glycerol
ADP + 1,2-dioctanoyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-dioctanoyl-sn-glycerol
ADP + 1,2-dioctanoyl-sn-glycerol 3-phosphate
-
preferred substrate
-
-
?
ATP + 1,2-dioctanoyl-sn-glycerol
ADP + 1,2-dioctanoyl-sn-glycerol 3-phosphate
-
preferred substrate
-
-
?
ATP + 1,2-dioctanoylglycerol
ADP + 1,2-dioctanoylglycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-dioctanoylglycerol
ADP + 1,2-dioctanoylglycerol 3-phosphate
-
enzyme type I: activity is 149% of the activity with rac-1,2-dioleoylglycerol, enzyme type II: activity is 114% of the activity with rac-1,2-dioleoylglycerol
-
-
?
ATP + 1,2-dioleoyl-sn-glycerol
ADP + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-dioleoyl-sn-glycerol
ADP + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-dioleoyl-sn-glycerol
ADP + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-dioleoyl-sn-glycerol
ADP + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-dioleoyl-sn-glycerol
ADP + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-dioleoyl-sn-glycerol
ADP + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-dioleoyl-sn-glycerol
ADP + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-dioleoyl-sn-glycerol
ADP + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-dioleoyl-sn-glycerol
ADP + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-dioleoyl-sn-glycerol
ADP + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-dioleoyl-sn-glycerol
ADP + 1,2-dioleoyl-sn-glycerol 3-phosphate
high activity
-
-
?
ATP + 1,2-dioleoyl-sn-glycerol
ADP + 1,2-dioleoyl-sn-glycerol 3-phosphate
isoform DGKepsilon shows about 7% activity with 0.38 mol% 1,2-dioleoyl-sn-glycerol compared to 1-stearoyl-2-arachidonoyl-sn-glycerol
-
-
?
ATP + 1,2-dioleoyl-sn-glycerol
ADP + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
about 15fold the rate of 1-O-hexadecyl-sn-glycerol phosphorylation, isoforms diacylglycerol kinase alpha, beta, gamma, delta1, delta1, zeta, jota, theta
-
-
?
ATP + 1,2-dioleoyl-sn-glycerol
ADP + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-dioleoylglycerol
ADP + 1,2-dioleoylglycerol 3-phospate
-
low activity
-
-
?
ATP + 1,2-dioleoylglycerol
ADP + 1,2-dioleoylglycerol 3-phospate
modeling of lipid substrate binding, involving residues Arg9, Ser17, Ser98 and Glu69, overview
-
-
?
ATP + 1,2-dipalmitoyl-sn-glycerol
ADP + 1,2-dipalmitoyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-dipalmitoyl-sn-glycerol
ADP + 1,2-dipalmitoyl-sn-glycerol 3-phosphate
highest activity
-
-
?
ATP + 1,2-dipalmitoyl-sn-glycerol
ADP + 1,2-dipalmitoyl-sn-glycerol 3-phosphate
-
15% of the activity with 1-stearoyl-2-arachidonoyl-sn-glycerol
-
-
?
ATP + 1,2-dipalmitoyl-sn-glycerol
ADP + 1,2-dipalmitoyl-sn-glycerol 3-phosphate
preferred substrate for isoform DGKzeta
-
-
?
ATP + 1-palmitoyl-2-arachidonoyl-sn-glycerol
ADP + 1-palmitoyl-2-arachidonoyl-sn-glycerol 3-phosphate
isoform DGKepsilon shows about 90% activity with 0.38 mol% 1-palmitoyl-2-arachidonoyl-sn-glycerol compared to 1-stearoyl-2-arachidonoyl-sn-glycerol
-
-
?
ATP + 1-palmitoyl-2-arachidonoyl-sn-glycerol
ADP + 1-palmitoyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
enzyme type I: activity is 181% of the activity with rac-1,2-dioleoylglycerol, enzyme type II: activity is 116% of the activity with rac-1,2-dioleoylglycerol
-
-
?
ATP + 1-palmitoyl-2-oleoyl-sn-glycerol
ADP + 1-palmitoyl-2-oleoyl-sn-glycerol 3-phosphate
-
96.5% of the activity with 1-stearoyl-2-arachidonoyl-sn-glycerol
-
-
?
ATP + 1-palmitoyl-2-oleoyl-sn-glycerol
ADP + 1-palmitoyl-2-oleoyl-sn-glycerol 3-phosphate
about 80% of the activity with sn-1,2-dioleoylglycerol
-
-
?
ATP + 1-palmitoyl-2-oleoyl-sn-glycerol
ADP + 1-palmitoyl-2-oleoyl-sn-glycerol 3-phosphate
about 80% of the activity with sn-1,2-dioleoylglycerol, DGKksi
-
-
?
ATP + 1-palmitoyl-2-oleoyl-sn-glycerol
ADP + 1-palmitoyl-2-oleoyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1-palmitoyl-2-oleoyl-sn-glycerol
ADP + 1-palmitoyl-2-oleoyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1-palmitoyl-2-oleoyl-sn-glycerol
ADP + 1-palmitoyl-2-oleoyl-sn-glycerol 3-phosphate
-
about 60% of the activity with 1-palmitoyl-2-arachidonoyl-sn-glycerol
-
-
?
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
about 110% of the activity with 1,2-dioleoyl-sn-glycerol
-
-
?
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
108% of the activity with sn-1,2-dioleoylglycerol
-
-
?
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
since diacylglycerol kinase is an enzyme of the phosphatidylinositol cycle, its natural substrate could be 1-stearoyl-2-arachidonoyl-sn-glycerol, thought to be the main diacylglycerol analog generated from phosphoinositide
-
-
?
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
preferred substrate of isoform diacylglycerol kinase epsilon
-
-
?
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
isoform DGKepsilon shows 100% activity with 0.38 mol% 1-stearoyl-2-arachidonoyl-sn-glycerol
-
-
?
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
in wild-type, ratio of enzymic activity of substrates 1-stearoyl-2-linoleoyl-sn-glycerol to 1-stearoyl-2-arachidonoyl-sn-glycerol is 0.109
-
-
?
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
specific substrate of isoform DGKepsilon
-
-
?
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
specific substrate of isoform DGKepsilon
-
-
?
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1-stearoyl-2-docosahexaenoyl-sn-glycerol
ADP + 1-stearoyl-2-docosahexaenoyl-sn-glycerol 3-phosphate
high activity
-
-
?
ATP + 1-stearoyl-2-docosahexaenoyl-sn-glycerol
ADP + 1-stearoyl-2-docosahexaenoyl-sn-glycerol 3-phosphate
no substrate for wild-type, but substrate for mutant R457Q
-
-
?
ATP + 1-stearoyl-2-linoleoyl-sn-glycerol
ADP + 1-stearoyl-2-linoleoyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1-stearoyl-2-linoleoyl-sn-glycerol
ADP + 1-stearoyl-2-linoleoyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1-stearoyl-2-linoleoyl-sn-glycerol
ADP + 1-stearoyl-2-linoleoyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1-stearoyl-2-linoleoyl-sn-glycerol
ADP + 1-stearoyl-2-linoleoyl-sn-glycerol 3-phosphate
in wild-type, ratio of enzymic activity of substrates 1-stearoyl-2-linoleoyl-sn-glycerol to 1-stearoyl-2-arachidonoyl-sn-glycerol is 0.109
-
-
?
ATP + 2,3-dioleoyl-sn-glycerol
ADP + 2,3-diacyl-sn-glycerol 1-phosphate
-
-
-
-
?
ATP + 2,3-dioleoyl-sn-glycerol
ADP + 2,3-diacyl-sn-glycerol 1-phosphate
-
-
isoform diacylglycerol kinase alpha 8.5%, zeta, 12%, epsilon 6% of the activity with 1,2-dioleoyl-sn-glycerol, respectively
-
?
ATP + ceramide
ADP + ceramide 3-phosphate
-
-
-
-
?
ATP + ceramide
ADP + ceramide 3-phosphate
-
no activity
-
-
?
ATP + ceramide
ADP + ceramide 3-phosphate
-
hardly utilized
-
-
?
ATP + sn-1,2-dioleoylglycerol
ADP + sn-1,2-dioleoylglycerol 3-phosphate
-
-
-
-
?
ATP + sn-1,2-dioleoylglycerol
ADP + sn-1,2-dioleoylglycerol 3-phosphate
-
-
-
-
?
ATP + sn-1,2-dioleoylglycerol
ADP + sn-1,2-dioleoylglycerol 3-phosphate
-
-
-
-
?
ATP + sn-1,2-dioleoylglycerol
ADP + sn-1,2-dioleoylglycerol 3-phosphate
recombinant DGKksi
-
-
?
ATP + sn-1,2-dioleoylglycerol
ADP + sn-1,2-dioleoylglycerol 3-phosphate
-
-
-
-
?
ATP + sn-1,2-dioleoylglycerol
ADP + sn-1,2-dioleoylglycerol 3-phosphate
-
enzyme type I: activity is 18% of the activity with rac-1,2-dioleoylglycerol, enzyme type II: activity is 19% of the activity with rac-1,2-dioleoylglycerol
-
-
?
ATP + sn-1,2-dioleoylglycerol
ADP + sn-1,2-dioleoylglycerol 3-phosphate
-
-
-
-
?
additional information
?
-
-
complex enzyme regulation, overview, the enzyme is involved in several processes such as cell growth, neuronal transmission, and cytoskeleton remodeling
-
-
?
additional information
?
-
the isozyme DGK2 is involved in cold signal transduction
-
-
?
additional information
?
-
-
the isozyme DGK2 is involved in cold signal transduction
-
-
?
additional information
?
-
isoform DGK4 has also guanylyl cyclase activity
-
-
-
additional information
?
-
-
the soluble diacylglycerol kinase DgkB is required for lipoteichoic acid production in Bacillus subtilis
-
-
?
additional information
?
-
the soluble diacylglycerol kinase DgkB is required for lipoteichoic acid production in Bacillus subtilis
-
-
?
additional information
?
-
-
no substrate: monoacylglycerol, ceramide, or undecaprenol
-
-
?
additional information
?
-
no substrate: monoacylglycerol, ceramide, or undecaprenol
-
-
?
additional information
?
-
-
enzyme assays with isolated rod outer segments prepared under room light from retinas obtained from dark-adapted bovine eyes
-
-
?
additional information
?
-
-
complex enzyme regulation, overview, the enzyme is involved in several processes such as cell growth, neuronal transmission, and cytoskeleton remodeling
-
-
?
additional information
?
-
-
the enzyme inhibits neurotransmission to control behaviour by terminating diacylglycerol signaling, probably independent of Galpha0 signaling
-
-
?
additional information
?
-
-
1-oleoyl-rac-glycerol is a poor substrate
-
-
?
additional information
?
-
-
DGK-3 affects the resetting of the thermal memory by altering plasticity in the temperature range of AFD synaptic output, without detectably affecting plasticity in the temperature range of AFD temperature sensitivity
-
-
?
additional information
?
-
-
diacylglycerol kinase gamma interacts with and activates beta2-chimaerin, a Rac-specific GAP, in response to epidermal growth factor
-
-
?
additional information
?
-
-
nuclear DGKgamma regulates cell cycle
-
-
?
additional information
?
-
-
complex enzyme regulation, overview, the enzyme is involved in several processes such as cell growth, neuronal transmission, and cytoskeleton remodeling
-
-
?
additional information
?
-
-
sn-1,3-dioleoylglycerol is not a substrate
-
-
?
additional information
?
-
-
no activity with ficaprenol
-
-
?
additional information
?
-
DgkA also has ATPase activity which is about 25% of its kinase activity
-
-
?
additional information
?
-
-
the isozyme zeta interacts with phosphoinositol phosphate 5-kinase activating it via phosphatidic acid, isozyme theta associates with RhoA, complex enzyme regulation involving alternative splicing, overview, the enzyme is involved in several processes such as cell growth, neuronal transmission, and cytoskeleton remodeling
-
-
?
additional information
?
-
-
diacylglycerol kinase alpha suppresses tumor necrosis factor-alpha-induced apoptosis of human melanoma cells through NF-kappaB activation
-
-
?
additional information
?
-
diacylglycerol kinase alpha suppresses tumor necrosis factor-alpha-induced apoptosis of human melanoma cells through NF-kappaB activation
-
-
?
additional information
?
-
-
diacylglycerol kinase zeta plays a role in modulation of membrane trafficking. DGKzeta depletion in JURKAT cells accelerates transferrin receptor exit from the endocytic recycling compartment
-
-
?
additional information
?
-
diacylglycerol kinase zeta plays a role in modulation of membrane trafficking. DGKzeta depletion in JURKAT cells accelerates transferrin receptor exit from the endocytic recycling compartment
-
-
?
additional information
?
-
-
the enzyme plays a role in the secretion of lethal exosomes bearing Fas ligand during activation-induced cell death of T lymphocytes
-
-
?
additional information
?
-
the enzyme plays a role in the secretion of lethal exosomes bearing Fas ligand during activation-induced cell death of T lymphocytes
-
-
?
additional information
?
-
-
diacylglycerol kinase alpha is involved in secretion of pro-apoptotic protein Fas ligand by T-lymphocytes via the regulation of the release of lethal exosomes by the exocytic pathway
-
-
?
additional information
?
-
diacylglycerol kinase alpha is involved in secretion of pro-apoptotic protein Fas ligand by T-lymphocytes via the regulation of the release of lethal exosomes by the exocytic pathway
-
-
?
additional information
?
-
diacylglycerol kinase gamma regulates beta2-chimaerin, a GTPase-activating protein for Rac
-
-
?
additional information
?
-
-
diacylglycerol kinase zeta is involved in control of vesicle trafficking
-
-
?
additional information
?
-
diacylglycerol kinase zeta is involved in control of vesicle trafficking
-
-
?
additional information
?
-
-
diacylglycerol kinases are required for anchorage-independent growth in MDA-MB-231 cells
-
-
?
additional information
?
-
2-arachidonoyl glycerol is a very poor substrate for the epsilon isoform of diacylglycerol kinases. 2-Oleoyl glycerol is also a poor substrate for this isoform of diacylglycerol kinases
-
-
?
additional information
?
-
2-arachidonoyl glycerol is a very poor substrate for the epsilon isoform of diacylglycerol kinases. 2-Oleoyl glycerol is also a poor substrate for this isoform of diacylglycerol kinases
-
-
?
additional information
?
-
2-arachidonoyl glycerol is a very poor substrate for the zeta isoforms of diacylglycerol kinases. 2-Oleoyl glycerol is also a poor substrate for this isoform
-
-
?
additional information
?
-
2-arachidonoyl glycerol is a very poor substrate for the zeta isoforms of diacylglycerol kinases. 2-Oleoyl glycerol is also a poor substrate for this isoform
-
-
?
additional information
?
-
-
alkyl-lysophosphatidic acid can be produced in SKOV-3 cells by diacylglycerol kinase-mediated phosphorylation of 1-O-hexadecyl-sn-2-acetyl glycerol followed by deacetylation of 1-O-hexadecyl-sn-2-acetyl glycerol 3-phosphate. Production of alkyl-lysophosphatidic acid is stimulated by sphingosine and its analogues
-
-
?
additional information
?
-
the cholesterol recognition/interaction amino acid consensus domain adjacent to the lipoxygenase-like motif plays a role in acyl-chain selectivity. Despite the high degree of conservation of the amino acid sequence in this region of the protein, certain mutations result in proteins with higher activity than the wild-type protein. These mutations also result in a selective gain of acyl-chain preferences for diacylglycerols with different acyl-chain profiles. In addition to the lipoxygenase-like motif, adjacent residues also contribute to selectivity for diacylglycerols with specific acyl-chain compositions
-
-
?
additional information
?
-
water does not compete with diacylglycerol as an acceptor of the gamma-phosphate of ATP. Neither with the highly specific substrate, 1-stearoyl-2-arachidonoyl-sn-glycerol, nor with a less specific substrate, 1-stearoyl-2-linoleoyl-sn-glycerol, is there any evidence for ATP hydrolysis accompanying substrate phosphorylation
-
-
?
additional information
?
-
-
water does not compete with diacylglycerol as an acceptor of the gamma-phosphate of ATP. Neither with the highly specific substrate, 1-stearoyl-2-arachidonoyl-sn-glycerol, nor with a less specific substrate, 1-stearoyl-2-linoleoyl-sn-glycerol, is there any evidence for ATP hydrolysis accompanying substrate phosphorylation
-
-
?
additional information
?
-
the enzyme also shows 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows low 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows low 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows low 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows low 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows low 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows low 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows low 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows low 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows negligible 1-monoacylglycerol kinase (1-MGK) and 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows negligible 1-monoacylglycerol kinase (1-MGK) and 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows negligible 1-monoacylglycerol kinase (1-MGK) and 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows negligible 1-monoacylglycerol kinase (1-MGK) and 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows negligible 1-monoacylglycerol kinase (1-MGK) and 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows negligible 1-monoacylglycerol kinase (1-MGK) and 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows negligible 1-monoacylglycerol kinase (1-MGK) and 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows negligible 1-monoacylglycerol kinase (1-MGK) and 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows negligible 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows negligible 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows negligible 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows negligible 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows negligible 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows negligible 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows negligible 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
the enzyme also shows negligible 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
enzymatically active splice variant DGKeta3 lacks exon 26 encoding 31 amino acid residues. Splice variant DGKeta4 lacks the C-terminal half of variant DGKeta3 and has no enzymatic activity
-
-
-
additional information
?
-
isoform DGKepsilon is unable to phosphorylate 1-stearoyl-2-docosahexaenoyl-sn-glycerol and has essentially no activity in phosphorylating 1-monoacylglycerol substrates
-
-
-
additional information
?
-
-
isoform DGKepsilon is unable to phosphorylate 1-stearoyl-2-docosahexaenoyl-sn-glycerol and has essentially no activity in phosphorylating 1-monoacylglycerol substrates
-
-
-
additional information
?
-
isoform DGKzeta physically and functionally interacts with protein kinase Calpha. Diacylglycerol kinase control of protein kinase C facilitates cell-cell communication
-
-
-
additional information
?
-
-
complex enzyme regulation involving alternative splicing, overview, the enzyme is involved in several processes such as cell growth, neuronal transmission, and cytoskeleton remodeling
-
-
?
additional information
?
-
-
isozymes DGKzeta, DGKalpha, and DGKepsilon utilize 1-alkyl-2-acyl-glycerols as substrates, addition of cholesterol and/or phosphatidylethanolamine reduce the substrate specificity
-
-
?
additional information
?
-
-
diacylglycerol kinase delta regulates protein kinase C and epidermal growth factor receptor signaling
-
-
?
additional information
?
-
-
diacylglycerol kinase zeta regulates microbial recognition and host resistance to Toxoplasma gondii
-
-
?
additional information
?
-
diacylglycerol kinase zeta regulates microbial recognition and host resistance to Toxoplasma gondii
-
-
?
additional information
?
-
-
nuclear diacylglycerol kinase-zeta is a negative regulator of cell cycle progression in C2C12 mouse myoblasts
-
-
?
additional information
?
-
nuclear diacylglycerol kinase-zeta is a negative regulator of cell cycle progression in C2C12 mouse myoblasts
-
-
?
additional information
?
-
-
T cell anergy is reversed by active Ras and is regulated by diacylglycerol kinase-alpha
-
-
?
additional information
?
-
activation of a Ca2+-independent protein kinase C isozyme by 1,2-diacylglycerol, which is generated by phospholipase Cbeta and phospholipase D activation and inactivated by phosphorylation via diacylglycerol kinase, is responsible for the endothelin-1-induced decreases in Ca2+ transients and cell shortening
-
-
?
additional information
?
-
-
activation of a Ca2+-independent protein kinase C isozyme by 1,2-diacylglycerol, which is generated by phospholipase Cbeta and phospholipase D activation and inactivated by phosphorylation via diacylglycerol kinase, is responsible for the endothelin-1-induced decreases in Ca2+ transients and cell shortening
-
-
?
additional information
?
-
diacylglycerol kinase zeta and syntrophins play a role at multiple stages of the cell fusion process. Potential link between changes in the lipid content of the membranebilayer and reorganization of the actin cytoskeleton during myoblast fusion
-
-
?
additional information
?
-
-
diacylglycerol kinase zeta is a key determinant of cell cycle progression and differentiation of C2C12 cells
-
-
?
additional information
?
-
diacylglycerol kinase zeta is a key determinant of cell cycle progression and differentiation of C2C12 cells
-
-
?
additional information
?
-
-
diacylglycerol kinases alpha and zeta synergistically promote T cell maturation in the thymus
-
-
?
additional information
?
-
-
Rv2252 encodes a diacylglycerol kinase involved in the biosynthesis of phosphatidylinositol mannosides
-
-
?
additional information
?
-
-
phospholipase C/diacylglycerol kinase-mediated signalling is required for benzothiadiazole-induced oxidative burst and hypersensitive cell death in rice suspension-cultured cells
-
-
?
additional information
?
-
phospholipase C/diacylglycerol kinase-mediated signalling is required for benzothiadiazole-induced oxidative burst and hypersensitive cell death in rice suspension-cultured cells
-
-
?
additional information
?
-
-
enzyme form I and II show a preference for diacylglycerol substrates with saturated acyl chains of 10-12 carbon atoms
-
-
?
additional information
?
-
-
diacylglycerol emulsion
-
-
?
additional information
?
-
-
the enzyme is active in mixed micelles containing octyl glucoside and dioleoylglycerol
-
-
?
additional information
?
-
-
DGKzeta blocks cardiac hypertrophic programs in response to endothelin-1 in neonatal rat cardiomyocytes. DGKzeta blocks cardiac hypertrophy induced by G protein-coupled receptor agonists and pressure overload in vivo. DGKzeta attenuates ventricular remodeling and improves survival after myocardial infarction
-
-
?
additional information
?
-
-
diacylglycerol kinase is involved in the regulation of oxidative stress-induced intestinal cell injury
-
-
?
additional information
?
-
the enzyme also shows 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
additional information
?
-
1,2-diacylglycerol embedded in unilamellar dioleoyl-phosphatidylcholine vesicles is not a substrate for DgkB
-
-
?
additional information
?
-
the enzyme also shows 1-monoacylglycerol kinase (1-MGK) and low 2-monoacylglycerol kinase (2-MGK) activities, cf. EC 2.7.1.94
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
ATP + 1,2-dipalmitoyl-sn-glycerol
ADP + 1,2-dipalmitoyl-sn-glycerol 3-phosphate
preferred substrate for isoform DGKzeta
-
-
?
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
additional information
?
-
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
nuclear DGK-theta is activated in response to alpha-thrombin
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
the enzyme may have an important function in the adult nervous system and muscle and during the development of the embryonic nervous system
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme functions to recycle diacylglycerol which is generated largely as a by-product of membrane-derived oligosaccharide biosynthesis
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
DGKiota may have important cellular functions in retina and brain
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
the expression of DGKeta2 is suppressed by glucocorticoid in contrast to the marked induction of DGKeta1
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
DGKgamma negatively regulates macrophage differentiation through its catalytic action operating on the cytoskeleton
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
the enzyme plays a role in cellular processes by regulating the intracellular concentration of the second messenger diacylglycerol. DGKeta may play a more general role in regulating cellular diacylglycerol levels
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
DAGKalpha is stimulated vby Src-like kinase-dependent phosphoinositide 3 kinase activation in lymphocytes. In vivo the increase in cellular levels of Src-like kinase-dependent phosphoinositide 3 kinase products is sufficient to induce DAGKalpha activation, allowing DAGKalpha relocation to the intact lymphocyte
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
high level expression of DGKalpha is induced following a signal transmitted through the pre-T-cell-receptor and the protein tyrosine kinase lck. Activity of DGKalpha contributes to survival in CD4+ 8+ double positive thymocytes as pharmacological inhibition of DGK activity results in death of this cell population both in cell suspension and thymic explants. DGKalpha promotes survival in theses thymocytes through a Bcl-regulated pathway
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme is involved in resynthesis of phosphatidylinositol by converting a second messenger diacylglycerol to phosphatidic acid
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme may regulate the intracellular concentration of diacylglycerol
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
DGK-Ialpha is involved in IL-2-mediated lymphocyte proliferation
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the 80000 Da and the 150000 Da enzyme form do not possess specificity towards diacylglycerol molecular species
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme binds and regulates signalling proteins which are activated by either diacylglycerol or phosphatidic acid
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme binds and regulates signalling proteins which are activated by either diacylglycerol or phosphatidic acid, isozyme dgk-1 regulates diacylglycerol signalling required for acetylcholine release
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme binds and regulates signalling proteins which are activated by either diacylglycerol or phosphatidic acid
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
r
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
r
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme binds and regulates signalling proteins which are activated by either diacylglycerol or phosphatidic acid
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
the enzyme binds and regulates signalling proteins which are activated by either diacylglycerol or phosphatidic acid
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
second messenger and intermediate in lipid synthesis
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
termination of diacylglycerol signaling, isozymes DGKalpha, DGKbeta, and DGKgamma play a pivotal role in development and metabolism of brain
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
-
reaction takes place during stimulated phosphatidylinositol turnover
-
-
?
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
-
since diacylglycerol kinase is an enzyme of the phosphatidylinositol cycle, its natural substrate could be 1-stearoyl-2-arachidonoyl-sn-glycerol, thought to be the main diacylglycerol analog generated from phosphoinositide
-
-
?
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
specific substrate of isoform DGKepsilon
-
-
?
additional information
?
-
-
complex enzyme regulation, overview, the enzyme is involved in several processes such as cell growth, neuronal transmission, and cytoskeleton remodeling
-
-
?
additional information
?
-
the isozyme DGK2 is involved in cold signal transduction
-
-
?
additional information
?
-
-
the isozyme DGK2 is involved in cold signal transduction
-
-
?
additional information
?
-
-
the soluble diacylglycerol kinase DgkB is required for lipoteichoic acid production in Bacillus subtilis
-
-
?
additional information
?
-
the soluble diacylglycerol kinase DgkB is required for lipoteichoic acid production in Bacillus subtilis
-
-
?
additional information
?
-
-
complex enzyme regulation, overview, the enzyme is involved in several processes such as cell growth, neuronal transmission, and cytoskeleton remodeling
-
-
?
additional information
?
-
-
the enzyme inhibits neurotransmission to control behaviour by terminating diacylglycerol signaling, probably independent of Galpha0 signaling
-
-
?
additional information
?
-
-
DGK-3 affects the resetting of the thermal memory by altering plasticity in the temperature range of AFD synaptic output, without detectably affecting plasticity in the temperature range of AFD temperature sensitivity
-
-
?
additional information
?
-
-
diacylglycerol kinase gamma interacts with and activates beta2-chimaerin, a Rac-specific GAP, in response to epidermal growth factor
-
-
?
additional information
?
-
-
nuclear DGKgamma regulates cell cycle
-
-
?
additional information
?
-
-
complex enzyme regulation, overview, the enzyme is involved in several processes such as cell growth, neuronal transmission, and cytoskeleton remodeling
-
-
?
additional information
?
-
-
the isozyme zeta interacts with phosphoinositol phosphate 5-kinase activating it via phosphatidic acid, isozyme theta associates with RhoA, complex enzyme regulation involving alternative splicing, overview, the enzyme is involved in several processes such as cell growth, neuronal transmission, and cytoskeleton remodeling
-
-
?
additional information
?
-
-
diacylglycerol kinase alpha suppresses tumor necrosis factor-alpha-induced apoptosis of human melanoma cells through NF-kappaB activation
-
-
?
additional information
?
-
diacylglycerol kinase alpha suppresses tumor necrosis factor-alpha-induced apoptosis of human melanoma cells through NF-kappaB activation
-
-
?
additional information
?
-
-
diacylglycerol kinase zeta plays a role in modulation of membrane trafficking. DGKzeta depletion in JURKAT cells accelerates transferrin receptor exit from the endocytic recycling compartment
-
-
?
additional information
?
-
diacylglycerol kinase zeta plays a role in modulation of membrane trafficking. DGKzeta depletion in JURKAT cells accelerates transferrin receptor exit from the endocytic recycling compartment
-
-
?
additional information
?
-
-
the enzyme plays a role in the secretion of lethal exosomes bearing Fas ligand during activation-induced cell death of T lymphocytes
-
-
?
additional information
?
-
the enzyme plays a role in the secretion of lethal exosomes bearing Fas ligand during activation-induced cell death of T lymphocytes
-
-
?
additional information
?
-
-
diacylglycerol kinase alpha is involved in secretion of pro-apoptotic protein Fas ligand by T-lymphocytes via the regulation of the release of lethal exosomes by the exocytic pathway
-
-
?
additional information
?
-
diacylglycerol kinase alpha is involved in secretion of pro-apoptotic protein Fas ligand by T-lymphocytes via the regulation of the release of lethal exosomes by the exocytic pathway
-
-
?
additional information
?
-
diacylglycerol kinase gamma regulates beta2-chimaerin, a GTPase-activating protein for Rac
-
-
?
additional information
?
-
-
diacylglycerol kinase zeta is involved in control of vesicle trafficking
-
-
?
additional information
?
-
diacylglycerol kinase zeta is involved in control of vesicle trafficking
-
-
?
additional information
?
-
-
diacylglycerol kinases are required for anchorage-independent growth in MDA-MB-231 cells
-
-
?
additional information
?
-
-
complex enzyme regulation involving alternative splicing, overview, the enzyme is involved in several processes such as cell growth, neuronal transmission, and cytoskeleton remodeling
-
-
?
additional information
?
-
-
diacylglycerol kinase delta regulates protein kinase C and epidermal growth factor receptor signaling
-
-
?
additional information
?
-
-
diacylglycerol kinase zeta regulates microbial recognition and host resistance to Toxoplasma gondii
-
-
?
additional information
?
-
diacylglycerol kinase zeta regulates microbial recognition and host resistance to Toxoplasma gondii
-
-
?
additional information
?
-
-
nuclear diacylglycerol kinase-zeta is a negative regulator of cell cycle progression in C2C12 mouse myoblasts
-
-
?
additional information
?
-
nuclear diacylglycerol kinase-zeta is a negative regulator of cell cycle progression in C2C12 mouse myoblasts
-
-
?
additional information
?
-
-
T cell anergy is reversed by active Ras and is regulated by diacylglycerol kinase-alpha
-
-
?
additional information
?
-
activation of a Ca2+-independent protein kinase C isozyme by 1,2-diacylglycerol, which is generated by phospholipase Cbeta and phospholipase D activation and inactivated by phosphorylation via diacylglycerol kinase, is responsible for the endothelin-1-induced decreases in Ca2+ transients and cell shortening
-
-
?
additional information
?
-
-
activation of a Ca2+-independent protein kinase C isozyme by 1,2-diacylglycerol, which is generated by phospholipase Cbeta and phospholipase D activation and inactivated by phosphorylation via diacylglycerol kinase, is responsible for the endothelin-1-induced decreases in Ca2+ transients and cell shortening
-
-
?
additional information
?
-
diacylglycerol kinase zeta and syntrophins play a role at multiple stages of the cell fusion process. Potential link between changes in the lipid content of the membranebilayer and reorganization of the actin cytoskeleton during myoblast fusion
-
-
?
additional information
?
-
-
diacylglycerol kinase zeta is a key determinant of cell cycle progression and differentiation of C2C12 cells
-
-
?
additional information
?
-
diacylglycerol kinase zeta is a key determinant of cell cycle progression and differentiation of C2C12 cells
-
-
?
additional information
?
-
-
diacylglycerol kinases alpha and zeta synergistically promote T cell maturation in the thymus
-
-
?
additional information
?
-
-
Rv2252 encodes a diacylglycerol kinase involved in the biosynthesis of phosphatidylinositol mannosides
-
-
?
additional information
?
-
-
phospholipase C/diacylglycerol kinase-mediated signalling is required for benzothiadiazole-induced oxidative burst and hypersensitive cell death in rice suspension-cultured cells
-
-
?
additional information
?
-
phospholipase C/diacylglycerol kinase-mediated signalling is required for benzothiadiazole-induced oxidative burst and hypersensitive cell death in rice suspension-cultured cells
-
-
?
additional information
?
-
-
DGKzeta blocks cardiac hypertrophic programs in response to endothelin-1 in neonatal rat cardiomyocytes. DGKzeta blocks cardiac hypertrophy induced by G protein-coupled receptor agonists and pressure overload in vivo. DGKzeta attenuates ventricular remodeling and improves survival after myocardial infarction
-
-
?
additional information
?
-
-
diacylglycerol kinase is involved in the regulation of oxidative stress-induced intestinal cell injury
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-2-amino-2-((S)-6-octyl-1,2,3,4-tetrahydronaphthalen-2-yl)propan-1-ol
-
analogue of FTY720, 0.01 mM increase phosphorylation of 1-O-hexadecyl-sn-2-acetyl glycerol by isoform diacylglycerol kinase alpha about 3.5fold.
1,3-dioleoylglycerol
-
activates
1-monooleoylglycerol
-
activates
1-O-alkylphosphatidylcholine
-
half-maximal activation at 21.9 mol%
1-palmitoyl-2-oleoylglycerophosphocholine
-
activates
4-(2,4-dimethylphenoxy)-N-hydroxybutanamide
0.1 mM KU-10 activates isoform DGKalpha by about 10%
-
4beta-phorbol-12-myristate-13-acetate
enhances voltage-dependent opening of wild-type and cAMP/H+-uncoupled hyperpolarization activated, cyclic nucleotide-regulated channels. 4beta-Phorbol-12-myristate-13-acetate exerts its effects on channel gating via sequential activation ofprotein kinase C and diacylglycerol kinase coupled with upregulation of mitogen-activated protein kinase and phospholipase A2
acidic phospholipids
-
activation in vitro
-
benzothiadiazole
activation of the expression of diacylglycerol kinase OsDAGK1
bis-phosphatidic acid
-
half-maximal activation at 3.9 mol%
-
cAMP
-
stimulates nuclear diacylglycerol kinase catalytic activity
cholesterol 3-sulfate
-
activates
D-glucose
-
exposure of L6 cell myotubes overexpressing human insulin receptors to 25 mM glucose for 5 min decreases the intracellular levels of diacylglycerol, paralleled by transient activation of diacylglycerol kinase and of insulin receptor signaling. Following 30-min exposure, both diacylglycerol levels and diacylglycerol kinase activity return close to basal levels. Glucose exposure redistributes diacylglycerol kinase isoforms alpha and delta, from the prevalent cytosolic localization to the plasma membrane fraction
detergent
-
no activity in absence of detergent
-
di-O-hexadecylphosphatidylcholine
-
half-maximal activation at 13.5 mol%
diacylglycerol 3-phosphate
-
the enzyme apoprotein is attributed to a novel feedback activation involving diacylglycerol 3-phosphate
dilauroyl-N,N-dimethylglycerophosphoethanolamine
-
activates
dilauroyl-N-methylglycerophosphoethanolamine
-
activates
dilauroylglycerophosphocholine
-
activates
dilauroylglycerophosphoethanolamine
-
activates
dilauroylphosphatidylcholine
-
half-maximal activation at 11.9 mol%
dimethylmyristamide
-
activates
dioleoyl ethylene glycol
-
activates
dioleoyl-phosphatidylglycerol
-
dioleoylphosphatidylcholine
-
half-maximal activation at 10.4 mol%
dioleoylphosphatidylglycerol
-
half-maximal activation at 6.3 mol%
dipalmitoylphosphatidic acid
-
activates only in presence of Triton X-100
endothelin-1
-
activates diacylglycerol kinase in caveolae/rafts and noncaveolae/rafts of mesenteric arteries. Activation does not depend on phosphatidylinositol 3-kinase. In response to norepinephrin, but not to epithelin-1, protein kinase PKB translocates to caveolae/rafts
epigallocatechin gallate
-
FTY720
-
in presence of 0.01 mM FTY720, phosphorylation of 1-O-hexadecyl-sn-2-acetyl glycerol by isoforms diacylglycerol kinase alpha, beta or gamma is 3fold increased
H2O2
-
endogenous nuclear diacylglycerol kinase zeta rapidly translocates to the cytoplasm following H2O2 treatment
hepatocyte growth factor
-
induces diaclyglycerol kinase activity, which is required for cell invasiveness
-
hexadecyl phosphorylcholine
-
half-maximal activation at 17.3 mol%
hexadecylphosphorylcholine
-
activates
lauryl maltoside
-
activates in presence of 11 mM Triton X-100
Lipid
-
purified enzyme is completely inactive unless a lipid is added to the assay buffer containing Triton X-100
lysophosphatidylcholine
-
activation of phospholipids in the order of decreasing efficiency: phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, sphingomyelin
lysophosphatidylethanolamine
-
activates
methyl myristate
-
activates
myristoylcholine chloride
-
activates
myristyl acetate
-
activates
n-hexyl beta-D-glucoside
-
activates in presence of 11 mM Triton X-100
N-[7-[cyclopropyl(hydroxy)methyl]-2,3-dihydro-1,4-benzodioxin-6-yl]cyclopropanecarboxamide
0.1 mM KU-8 activates isoform DGKalpha by 19%
-
nitrododecane
-
activates
norepinephrine
-
stimulates an increase in diacylglycerol kinase activity in caveolae/rafts of mesenteric arteries. Activation depends on phosphatidylinositol 3-kinase. In response to norepinephrin, but not to epithelin-1, protein kinase PKB translocates to caveolae/rafts
octyl acetate
-
activates
octyl beta-glucoside
-
activates in presence of 11 mM Triton X-100
oleic acid
-
activates only in presence of Triton X-100
oleoylcholine chloride
-
activates
palmitic acid
-
activates only in presence of Triton X-100
phorbol-12-myristate-13-acetate
diacylglycerol kinase zeta activity at the T cell receptor is enhanced by phorbol-12-myristate-13-acetate cotreatment
phosphatidyl glycerol
-
good activator
phosphatidylcholine plasmalogen
-
half-maximal activation at 7.3 mol%
-
phosphatidylglycerol
-
effective stimulation
phosphatidylinositol 4,5-bisphosphate
-
highly stimulating
platelet-activating factor
-
half-maximal activation at 22.4 mol%
rac-1,2-dioleoylglycero-3-sulfate
-
half-maximal activation at 2.7 mol%
sn-1,2-dioleoylglycerol
-
activates
sn-1,3-dioleoylglycerol
-
activates
sodium cholate
-
enhances activity of DGK I and DGK IV
sodium deoxycholate
-
enhances activity of DGK I and DGK IV
Sodium dodecyl sulfate
-
activates
sodium hexadecyl sulfate
-
half-maximal activation at 9.8 mol%
sphingomyelin
-
activation of phospholipids in the order of decreasing efficiency: phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, sphingomyelin
stearic acid
-
activates only in presence of Triton X-100
stearoyllysophosphatidylcholine
-
half-maximal activation at 15.8 mol%
cardiolipin
-
activates
cardiolipin
-
good activator
cardiolipin
-
mitochondrial, half-maximal activation at 2.3 mol%
cardiolipin
-
half-maximal activation by 1 mol%
cholesterol
DGKalpha can be activated in vitro in a Ca2+-independent manner by lipids such cholesterol
cholesterol
DGKalpha can be activated in vitro in a Ca2+-independent manner by lipids such cholesterol
deoxycholate
-
stimulation
deoxycholate
-
purified enzyme is completely devoid of activity without addition of phospholipid or deoxycholate
deoxycholate
-
enhances activity of enzyme form DGK-II and DGK-III, enzyme form DGK-I is not much affected
deoxycholate
-
the enzyme shows optimal activity in presence of phosphatidylserine or deoxycholate. Lower activity in presence of phosphatidylcholine. Diacylglycerol analogs containing an unsaturated fatty acid at the sn-2 position give optimal enzyme activity irrespective of the presence of deoxycholate
deoxycholate
-
enhances activity
P53
p53 activates DGKalpha in response to DNA damage
P53
p53 activates DGKalpha in response to DNA damage
phosphatidic acid
-
highly stimulating
phosphatidic acid
-
activates only in presence of Triton X-100
phosphatidic acid
-
more effective activator than phosphatidylserine. Phosphatidic acid decreases the apparent surface KM of DGKtheta for dioleoylglycerol and promotes binding to vesicles in a dose-dependent manner
phosphatidic acid
-
phosphatidic acid is more effective than phosphatidiylserine. Both decreases the apparent surface KM value for dioleoylglycerol and promote binding to vesicles, but through different mechanisms
phosphatidic acid
production of oxidative burst and hypersensitive cell death. Activation of the epxression of diacylglycerol kinase and transcritional factor gene OsBIERF3. Neomycin partially inhibits the poduction of oxidatve burst, hypersensitive cell death, and expression of both genes
phosphatidic acid
-
good activator of DGK IV, no effect on DGK I activity
phosphatidylcholine
-
-
phosphatidylcholine
-
activates
phosphatidylcholine
-
the enzyme shows optimal activity in presence of phosphatidylserine or deoxycholate. Lower activity in presence of phosphatidylcholine
phosphatidylcholine
-
moderate enhancement of DGK IV, no effect on DGK I activity
phosphatidylcholine
-
enzyme type II has a preference for phosphatidylcholine as cofactor, enzyme type I can utilize both phosphatidylserine and phosphatidylinositol, but has a lower preference for phosphatidylcholine
phosphatidylcholine
-
activation of phospholipids in the order of decreasing efficiency: phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, sphingomyelin
phosphatidylethanolamine
-
activates only in presence of Triton X-100
phosphatidylethanolamine
-
plus cardiolipin, activates
phosphatidylethanolamine
DGKalpha can be activated in vitro in a Ca2+-independent manner by lipids such as phosphatidylethanolamine
phosphatidylethanolamine
DGKalpha can be activated in vitro in a Ca2+-independent manner by lipids such as phosphatidylethanolamine
phosphatidylethanolamine
-
activation of phospholipids in the order of decreasing efficiency: phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, sphingomyelin
phosphatidylinositol
-
effective stimulation
phosphatidylinositol
-
enzyme type II has a preference for phosphatidylcholine as cofactor, enzyme type I can utilize both phosphatidylserine and phosphatidylinositol, but has a lower preference for phosphatidylcholine
phosphatidylinositol
-
enhances activity of DGK I and DGK IV
phosphatidylserine
-
strong activation
phosphatidylserine
-
activates
phosphatidylserine
-
good activator
phosphatidylserine
-
the enzyme shows optimal activity in presence of phosphatidylserine or deoxycholate. Lower activity in presence of phosphatidylcholine
phosphatidylserine
-
less effective activator than phosphatidic acid. Phosphatidylserine decreases the apparent surface KM of DGKtheta for dioleoylglycerol
phosphatidylserine
-
phosphatidic acid is more effective than phosphatidiylserine. Both decreases the apparent surface KM value for dioleoylglycerol and promote binding to vesicles, but through different mechanisms
phosphatidylserine
broadens the pH-dependent activity when the enzyme is assayed in cytosolic extracts. Phosphatidylserineconcentrates Mg2+ ions at the interface
phosphatidylserine
-
enzyme type II has a preference for phosphatidylcholine as cofactor, enzyme type I can utilize both phosphatidylserine and phosphatidylinositol, but has a lower preference for phosphatidylcholine
phosphatidylserine
-
enhances activity of DGK I and DGK IV
phosphatidylserine
-
activates
phosphatidylserine
-
activation of phospholipids in the order of decreasing efficiency: phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, sphingomyelin
phosphatidylserine
-
10-20 mol% result in 7.5-7.8fold activation of the recombinant wild-type enzyme, 3.8fold of the recombinant mutant DELTA196, and 6.5fold of the recombinant mutant DELTA332
Phospholipid
-
purified enzyme is completely devoid of activity without addition of phospholipid or deoxycholate
Phospholipid
-
a combination of diacylglycerol and phospholipid exclusively leads to full activation
Phospholipid
-
activation by phospholipid is not stereospecific and is mimicked partially by fatty acids
Phospholipid
-
enhances activity. Activation of phospholipids in the order of decreasing efficiency: phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, sphingomyelin
sphingosine
-
in presence of 0.01 mM sphingosine, phosphorylation of 1-O-hexadecyl-sn-2-acetyl glycerol by isoforms diacylglycerol kinase alpha, beta or gamma is 7-9fold increased
sphingosine
-
potently activates the 80000 Da enzyme
additional information
the isozyme DGK2 is induced by exposure to low temperatures, e.g. 4°C
-
additional information
-
the isozyme DGK2 is induced by exposure to low temperatures, e.g. 4°C
-
additional information
-
serotonin signalling activates the enzyme
-
additional information
DGKzeta interacts with and is regulated by the retinoblastoma protein
-
additional information
isozyme DGK-teta is dependent on an activating accessory protein containing a poly-basic region, the broadening of the pH profile of DGK-theta is also dependent on a PBR-containing activator
-
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evolution
as the smallest kinase known, it shares no sequence homology with conventional kinases and possesses a distinct trimer structure. The phosphorylation reaction of diacylglycerol kinase features the same phosphoryl transfer mechanism as other kinases, despite its unique structural properties. DgkA appears to be an evolutionarily optimized enzyme and its chemical reaction rate approaches the substrate diffusion-controlled rate limit
evolution
comprehensive analysis on the 1-monoacylglycerol kinase (1-MGK) and 2-monoacylglycerol kinase (2-MGK) activities, EC 2.7.1.94, of ten diacylglyceol kinase (DGK) isozymes, EC 2.7.1.107, from different organisms. Type I (alpha, beta, and gamma), type II (delta, eta, and kappa) and type III (epsilon) DGKs have 7.9-19.2% 2-MGK activity compared to their DGK activities, whereas their 1-MGK activities are below 3.0%. Both the 1-MGK and 2-MGK activities of the type IV DGKs (zeta and iota) are below 1% relative to their DGK activities. Type V DGKtheta has approximately 6% 1-MGK activity and below 2% 2-MGK activity compared to its DGK activity. Purified DGKtheta exhibits the same results, indicating that its 1-MGK activity is intrinsic. DGK isozymes are categorized into three types with respect to their 1-MGK and 2-MGK activities: those having (1) 2-MGK activity relatively stronger than their 1-MGK activity (types I-III), (2) only negligible 1-MGK and 2-MGK activities (type IV), and (3) 1-MGK activity stronger than its 2-MGK activity (type V). The 1-MGK activity of DGKtheta and the 2-MGK activity of DGKalpha are stronger than those of the acylglycerol kinase reported as 1-MGK and 2-MGK to date
evolution
comprehensive analysis on the 1-monoacylglycerol kinase (1-MGK) and 2-monoacylglycerol kinase (2-MGK) activities, EC 2.7.1.94, of ten diacylglyceol kinase (DGK) isozymes, EC 2.7.1.107, from different organisms. Type I (alpha, beta, and gamma), type II (delta, eta, and kappa) and type III (epsilon) DGKs have 7.9-19.2% 2-MGK activity compared to their DGK activities, whereas their 1-MGK activities are below 3.0%. Both the 1-MGK and 2-MGK activities of the type IV DGKs (zeta and iota) are below 1% relative to their DGK activities. Type V DGKtheta has approximately 6% 1-MGK activity and below 2% 2-MGK activity compared to its DGK activity. Purified DGKtheta exhibits the same results, indicating that its 1-MGK activity is intrinsic. DGK isozymes are categorized into three types with respect to their 1-MGK and 2-MGK activities: those having (1) 2-MGK activity relatively stronger than their 1-MGK activity (types I-III), (2) only negligible 1-MGK and 2-MGK activities (type IV), and (3) 1-MGK activity stronger than its 2-MGK activity (type V). The 1-MGK activity of DGKtheta and the 2-MGK activity of DGKalpha are stronger than those of the acylglycerol kinase reported as 1-MGK and 2-MGK to date
evolution
comprehensive analysis on the 1-monoacylglycerol kinase (1-MGK) and 2-monoacylglycerol kinase (2-MGK) activities, EC 2.7.1.94, of ten diacylglyceol kinase (DGK) isozymes, EC 2.7.1.107, from different organisms. Type I (alpha, beta, and gamma), type II (delta, eta, and kappa) and type III (epsilon) DGKs have 7.9-19.2% 2-MGK activity compared to their DGK activities, whereas their 1-MGK activities are below 3.0%. Both the 1-MGK and 2-MGK activities of the type IV DGKs (zeta and iota) are below 1% relative to their DGK activities. Type V DGKtheta has approximately 6% 1-MGK activity and below 2% 2-MGK activity compared to its DGK activity. Purified DGKtheta exhibits the same results, indicating that its 1-MGK activity is intrinsic. DGK isozymes are categorized into three types with respect to their 1-MGK and 2-MGK activities: those having (1) 2-MGK activity relatively stronger than their 1-MGK activity (types I-III), (2) only negligible 1-MGK and 2-MGK activities (type IV), and (3) 1-MGK activity stronger than its 2-MGK activity (type V). The 1-MGK activity of DGKtheta and the 2-MGK activity of DGKalpha are stronger than those of the acylglycerol kinase reported as 1-MGK and 2-MGK to date
evolution
comprehensive analysis on the 1-monoacylglycerol kinase (1-MGK) and 2-monoacylglycerol kinase (2-MGK) activities, EC 2.7.1.94, of ten diacylglyceol kinase (DGK) isozymes, EC 2.7.1.107, from different organisms. Type I (alpha, beta, and gamma), type II (delta, eta, and kappa) and type III (epsilon) DGKs have 7.9-19.2% 2-MGK activity compared to their DGK activities, whereas their 1-MGK activities are below 3.0%. Both the 1-MGK and 2-MGK activities of the type IV DGKs (zeta and iota) are below 1% relative to their DGK activities. Type V DGKtheta has approximately 6% 1-MGK activity and below 2% 2-MGK activity compared to its DGK activity. Purified DGKtheta exhibits the same results, indicating that its 1-MGK activity is intrinsic. DGK isozymes are categorized into three types with respect to their 1-MGK and 2-MGK activities: those having (1) 2-MGK activity relatively stronger than their 1-MGK activity (types IIII), (2) only negligible 1-MGK and 2-MGK activities (type IV), and (3) 1-MGK activity stronger than its 2-MGK activity (type V). The 1-MGK activity of DGKtheta and the 2-MGK activity of DGKalpha are stronger than those of the acylglycerol kinase reported as 1-MGK and 2-MGK to date
evolution
DgkA is a unique kinase with a distinctive active site. It has no recognizable nucleotide sequence or structural binding motifs
malfunction
knockdown of DGKfzeta in cultured neurons decreases spine density
malfunction
knockdown of DGKfzeta in cultured neurons decreases spine density
malfunction
small interfering RNA-dependent knockdown of diacylglycerol kinase eta impairs the Ras/B-Raf/C-Raf/MEK/ERK pathway activated by epidermal growth factor in HeLa cells and inhibits cell proliferation
malfunction
presence or absence of 1-MGK and 2-MGK activities may be essential to the pathophysiological functions of each DGK isozyme
malfunction
presence or absence of 1-MGK and 2-MGK activities may be essential to the pathophysiological functions of each DGK isozyme
malfunction
presence or absence of 1-MGK and 2-MGK activities may be essential to the pathophysiological functions of each DGK isozyme
malfunction
-
transformed mouse embryo fibroblasts from mice that have a genetic deletion of DGKdelta exhibit decreased levels of many phospholipids and neutral lipids compared with wild-type mouse embryonic fibroblasts. DGKdelta knockout leads to down-regulation of enzymes responsible for fatty acid synthesis and lowers the amount of many lipid species within the cell
malfunction
disruption of isoform DGK4 does not impair male gametophytic development but reduces in vivo performance and alters pollen tube Youngs modulus and adhesion properties
malfunction
dysregulation of isoform DGKepsilon perturbs lipid signalling and biosynthesis, which has been linked to epilepsy, Huntington`s disease, and heart disease. Recessive loss-of-function mutations in the isoform DGKepsilon gene cause atypical haemolytic uremic syndrome
malfunction
isoform dgk2-deficient plants are gametophyte lethal, although parental single homozygous plants are viable. The dgk2/dgk4 double heterozygote shows defective pollen tube growth and seed development because of nonviable mutant gametes
malfunction
isoform dgk4-deficient plants are gametophyte lethal, although parental single homozygous plants are viable. The dgk2/dgk4 double heterozygote shows defective pollen tube growth and seed development because of nonviable mutant gametes
malfunction
isoform DGKdelta knockout mice exhibit serotonin transporter inhibitor-sensitive obsessive-compulsive disorder-like behaviors. Moreover, serotonin transporter protein levels are markedly increased in the DGKdelta-deficient brain
malfunction
recessive loss of function mutations in isoform DGKepsilon cause atypical hemolytic-uremic syndrome
malfunction
the suppression of DGKdelta expression increases the phosphorylation levels of conventional and novel protein kinase C (cnPKCs). Furthermore, DGKdelta suppression increases the levels of cyclin D1 and phospho-cnPKCs even at the first 24 h of myogenic differentiation
metabolism
1-stearoyl-2-arachidonoyl-sn-glycerol phosphorylation to phosphatidic acid catalyzed by isoform DGKepsilon is one of the key steps of the phosphoinositide cycle. Enhanced isoform DGKepsilon activity plays a role in Huntingtons disease pathogenesis
metabolism
isoform DGKdelta interacts with melanoma antigen gene-D1 adaptor protein and Praja-1 E3 ubiquitin-protein ligase, and enhances the ubiquitination of serotonin transporter through Praja-1. Isoform DGKdelta interacts with serotonin transporter and induces serotonin transporter degradation in an activity-dependent manner through the Praja-1 ubiquitin ligase-proteasome system
physiological function
DGKalpha has a central role in modulating T cell anergy through its ability to control DAG levels, which likely activates RasGRP1 and possibly other proteins
physiological function
DGKepsilon prevents cardiac hypertrophy and progression to heart failure under chronic pressure overload
physiological function
-
DGKs broadly regulate signaling events by virtue of their ability to provide 1,2-diacyl-sn-glycerol 3-phosphate (phosphatidic acid) for the synthesis of phosphatidylinositols
physiological function
-
DGKs broadly regulate signaling events by virtue of their ability to provide 1,2-diacyl-sn-glycerol 3-phosphate (phosphatidic acid) for the synthesis of phosphatidylinositols
physiological function
-
DGKs broadly regulate signaling events by virtue of their ability to provide 1,2-diacyl-sn-glycerol 3-phosphate (phosphatidic acid) for the synthesis of phosphatidylinositols
physiological function
-
DGKs broadly regulate signaling events by virtue of their ability to provide 1,2-diacyl-sn-glycerol 3-phosphate (phosphatidic acid) for the synthesis of phosphatidylinositols
physiological function
DGKs broadly regulate signaling events by virtue of their ability to provide 1,2-diacyl-sn-glycerol 3-phosphate (phosphatidic acid) for the synthesis of phosphatidylinositols, isoform DGKzeta activates phosphatidylinositol-4-phosphate 5-kinase type Ialpha, DGKzeta modulates Rac1 activation to influence neurite outgrowth, DGKzeta modulates mTor activation and immune cell signaling
physiological function
DGKzeta has an important biological function in the nucleus where it appears to modulate the cell cycle by metabolizing 1,2-diacylglycerol
physiological function
diacylglycerol kinase beta promotes dendritic outgrowth and spine maturation in developing hippocampal neurons
physiological function
diacylglycerol kinase zeta regulates actin cytoskeleton reorganization through dissociation of Rac1 from RhoGDI
physiological function
isoform DGKalpha positively regulates tumor nuclear factor-alpha-dependent necrosis factor-kappaB activation via the protein kinase Czeta-mediated Ser311 phosphorylation of p65/RelA, isoform DGKalpha does not affect phosphorylation of IkappaB, DGKalpha enhances phosphorylation of p65 at Ser311 but not at Ser468 or Ser536
physiological function
isoform DGKalpha positively regulates tumor nuclear factor-alpha-dependent necrosis factor-kappaB activation via the protein kinase Czeta-mediated Ser311 phosphorylation of p65/RelA, isoform DGKalpha does not affect phosphorylation of IkappaB, DGKalpha enhances phosphorylation of p65 at Ser311 but not at Ser468 or Ser536
physiological function
isoform DGKbeta is provided to perisynaptic sites of medium spiny neurons so that it can effectively produce 1,2-diacyl-sn-glycerol 3-phosphate upon activation of Gq protein-coupled receptors and modulate the cellular state of striatal output neurons
physiological function
-
isoform DGKepsilon interacts with actin stress fibers and is involved in their stability in vascular smooth muscle cells
physiological function
isoform DGKf appears to form a multi-protein complex with functionally related proteins to organize efficient 1,2-diacylglycerol and 1,2-diacyl-sn-glycerol 3-phosphate signaling pathways at excitatory synapses, the DGKzeta isoform at excitatory postsynaptic sites is critically involved in spine maintenance, DGKzeta promotes neurite outgrowth
physiological function
isoform DGKf appears to form a multi-protein complex with functionally related proteins to organize efficient 1,2-diacylglycerol and 1,2-diacyl-sn-glycerol 3-phosphate signaling pathways at excitatory synapses, the DGKzeta isoform at excitatory postsynaptic sites is critically involved in spine maintenance, DGKzeta promotes neurite outgrowth
physiological function
membrane localization of DGKalpha acts as a switch-off signal for Ras activation, mediated by localization to the membrane of Ras-GRP1, DGKalpha is a negative regulator of the T cell activation program, DGKalpha activity is required for optimal chemotactic response of neutrophils, whereas it halts their oxidative burst, DGKalpha is a negative modulator of diacylglycerol signaling, DGKalpha activity modulates the mTOR pathway to prevent cell cycle transition, DGKalpha is an indicator of cell quiescence, DGKalpha is a positive regulator of cell proliferation and migration
physiological function
membrane localization of DGKalpha acts as a switch-off signal for Ras activation, mediated by localization to the membrane of Ras-GRP1, DGKalpha is a negative regulator of the T cell activation program, DGKalpha activity is required for optimal chemotactic response of neutrophils, whereas it halts their oxidative burst, DGKalpha is a negative modulator of diacylglycerol signaling, DGKalpha activity modulates the mTOR pathway to prevent cell cycle transition, DGKalpha is an indicator of cell quiescence, DGKalpha is a positive regulator of cell proliferation and migration
physiological function
neither overexpression of wild type nor kinase-inactive DGKzeta affects cell cycle distribution
physiological function
nuclear DGK-zeta downregulates the expression of cyclin D1 and increased the expression of TIS21/BTG2/PC3
physiological function
overexpression of DGKeta1 can activate the Ras/B-Raf/C-Raf/MEK/ERK pathway in a DGK activity-independent manner, suggesting that DGKeta serves as a scaffold/adaptor protein, DGKeta activates C-Raf but not B-Raf
physiological function
endogenous isoform diacylglycerol kinase alpha is recruited to the T cell receptor complex following T cell receptor/CD28 engagement
physiological function
endogenous isoform diacylglycerol kinase zeta is recruited to the T cell receptor complex following T cell receptor/CD28 engagement. Specific diacylglycerol kinase gene silencing shows that phosphatidic acid production at the activated complex depends mainly on diacylglycerol kinase zeta. At early stages of T cell immunological synapse formation, isoform zeta translocates rapidly to the plasma membrane, where rapid, sustained diacylglycerol accumulation is found
physiological function
-
in response to cold temperatures, there is a very fast accumulation of phosphatidic acid in Arabidopsis seedlings and leaf discs. Radiolabeling studies indicate a dominant role of diacylglycerol kinase under these conditions
physiological function
-
treating SKOV-3 ovarian cancer cell with a sphingosine analogue stimulates conversion of exogenous 1-alkyl-2-acetyl glycerol to alkyl-lysophosphatidic acid. Diacylglycerol kinase alpha may contribute significantly to the production of alkyl-lysophosphatidic acid in SKOV-3 cells, showing cross-talk between the sphingolipid and glycerol lipid pathways
physiological function
-
DGKdelta promotes de novo lipid synthesis is through signal transduction pathways, overview
physiological function
diacylglycerol kinase catalyzes the ATP-dependent phosphorylation of diacylglycerol to phosphatidic acid for use in shuttling water-soluble components to membrane-derived oligosaccharide and lipopolysaccharide in the cell envelope of Gram-negative bacteria
physiological function
light-dependent channel TRP in the light-sensitive microvilli of the photoreceptor's rhabdomere is opened by diacylglycerol and silenced by ATP, suggesting diacylglycerol kinase involvement. The ATP effect is abolished by inhibiting enzyme diacylglycerol kinase DGK and in the rdgA mutant, lacking functional DGK. Diacylglycerol activates TRP even in the presence of a DAG-lipase inhibitor, inconsistent with a requirement of polyunsaturated fatty acids in opening TRP. Diacylglycerol is the endogenous TRP agonist. ATP lowers the channel activity, the ATP effect is completely abolished by inhibition of the enzyme
physiological function
-
the enzyme is involved in a mechanism of light-regulated DAGK activity in the photoreceptors of the vertebrate species. Protein kinase C-dependent phosphorylation of retina rod outer segments (obtained from bovine retinas at room light) regulates DAGK activity
physiological function
-
the enzyme is involved in a mechanism of light-regulated DAGK activity in the photoreceptors of the vertebrate species. Protein kinase C-dependent phosphorylation of retina rod outer segments regulates DAGK activity
physiological function
the enzyme plays important roles is the nervous system
physiological function
enzyme isoforms control cancer cell survival, proliferation, and angiogenesis by regulating Akt/mTOR and MAPK/ERK pathways. In addition, some enzyme isoforms control cancer cell migration by regulating the activities of the Rho GTPases Rac1 and RhoA
physiological function
enzyme-deficient pollen tubes exhibit altered membrane recycling and phospholipid levels
physiological function
isoform DGK1 in Oryza sativa plays important roles in root growth and development. The enzyme suppresses lateral root number but promotes seminal root and crown root thickness and inhibits lateral root primordia formation and increases seminal root cell width
physiological function
-
isoform DGK2 expression is helpful to improve the drought resistance of transgenic Arabidopsis thaliana. Isoform DGK2 has effect on stomatal closure under water withholding condition. In addition, under stress conditions, isoform DGK2 significantly regulates the accumulation of hydrogen peroxide
physiological function
isoform DGK4 is crucial for gametogenesis and biosynthesis of phosphatidylglycerol and phosphatidylinositol in the endoplasmic reticulum
physiological function
isoform DGKalpha is involved in the vitamin E-induced amelioration of diabetic nephropathy in vivo
physiological function
isoform DGKalpha plays a crucial role in the amelioration of diabetic nephropathy and contributes to the effect of epigallocatechin gallate on diabetic nephropathy
physiological function
isoform DGKdelta regulates the early differentiation of C2C12 myoblasts via controlling the down-regulation of cyclin D1 expression
physiological function
isoform DGKeta3 plays specialized roles in spermatogenesis
physiological function
isoform DGKzeta modulates protein kinase C-dependent regulation of synapse plasticity. Isoform DGKzeta interaction with post-synaptic density 95/Discs-large/zona occludens-1-containing scaffolds restricts spatial activation of protein kinase Calpha. Isoform DGKzeta is a negative regulator of T-cell functions and a modulator of innate immunity
physiological function
isoforms DGK2 is crucial for gametogenesis and biosynthesis of phosphatidylglycerol and phosphatidylinositol in the endoplasmic reticulum
physiological function
nuclear isoform DGKalpha modulates cell cycle progression, and its activity or expression can lead to changes in the phosphorylated status of the retinoblastoma protein, thus, impairing G1/S transition and, subsequently, inducing cell cycle arrest, which is often uncoupled with apoptosis or autophagy induction. Nuclear enzyme activity drives K-562 cells through the G1/S transition during cell cycle progression
physiological function
-
the enzyme is involved in a mechanism of light-regulated DAGK activity in the photoreceptors of the vertebrate species. Protein kinase C-dependent phosphorylation of retina rod outer segments regulates DAGK activity
-
physiological function
-
light-dependent channel TRP in the light-sensitive microvilli of the photoreceptor's rhabdomere is opened by diacylglycerol and silenced by ATP, suggesting diacylglycerol kinase involvement. The ATP effect is abolished by inhibiting enzyme diacylglycerol kinase DGK and in the rdgA mutant, lacking functional DGK. Diacylglycerol activates TRP even in the presence of a DAG-lipase inhibitor, inconsistent with a requirement of polyunsaturated fatty acids in opening TRP. Diacylglycerol is the endogenous TRP agonist. ATP lowers the channel activity, the ATP effect is completely abolished by inhibition of the enzyme
-
additional information
1,2-dioctanoylglycerol is first docked into the active site of the crystal structure of DgkA, PDB ID 3ZE5, followed by construction of a ternary complex model by docking co-factor ATP and substrate 1,2-dioctanoylglycerol into the active site of DgkA. The complex of DgkA is optimized and equilibrated by molecular dynamics simulation in the lipid bilayer. The phosphotransfer reaction catalyzed by DgkA is then investigated through the hybrid density functional theory method B3LYP. Important role of the surface helix in the active site formation
additional information
Asn72 plays a key role in catalysis. Its side-chain amide bridges Glu69 and Glu76 both of which are essential, the gamma-phosphate of ATP is positioned for direct transfer to the primary hydroxyl of the lipid whose acyl chain is in the membrane, catalytic mechanism, overview. The putative catalytic site resides on the protein at the membrane/cytosol interface where the reactive moieties of the two substrates, with disparate polarities, come together for reaction. The ternary complex site, asBC, contains zinc-ACP and two lipid substrates. The gaamma-phosphate of the ATP analogue is positioned for direct transfer to the primary hydroxyl of the lipid whose acyl chain is in the membrane
additional information
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Asn72 plays a key role in catalysis. Its side-chain amide bridges Glu69 and Glu76 both of which are essential, the gamma-phosphate of ATP is positioned for direct transfer to the primary hydroxyl of the lipid whose acyl chain is in the membrane, catalytic mechanism, overview. The putative catalytic site resides on the protein at the membrane/cytosol interface where the reactive moieties of the two substrates, with disparate polarities, come together for reaction. The ternary complex site, asBC, contains zinc-ACP and two lipid substrates. The gaamma-phosphate of the ATP analogue is positioned for direct transfer to the primary hydroxyl of the lipid whose acyl chain is in the membrane
additional information
DgkA catalyzes phosphoryl transfer expected to take place at a polar/apolar interface
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A722V
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mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
C115Y
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mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
C184Y
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mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
G606E
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mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
G609E
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mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
G796R
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mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
N745I
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mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
P736S
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mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
Q246stop
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mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
Q422stop
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mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
R167stop
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mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
R180stop
-
mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
S880L
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mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
W646stop
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mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
W674stop
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mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
W767stop
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mutant isolated due to defects in DGK-1 controlled behaviour, altered behaviour compared to the wild-type enzyme, overview
G434D
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kinase-defective dominant-negative mutant , impairs hepatocyte growth factor- and v-Src-induced cell scatter and migration, without affecting the loss of intercellular adhesions, impairs hepatocyre growth factor-induced cell spreading, lamellipodia formation, membrane ruffling, and focal adhesions remodeling and impairs hepatocyte growth factor-induced Rac activation and membrane targeting
Y335F
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mutants is not tyrosine phosphorylated upon coexpression with activated Src mutant Y527F. Enzymatic activity is not stimulated by hepatocyte growth factor cell stimulation
A100L
site-directed mutagenesis, inactive mutant
A13K
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
A13R
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
A14Q
-
significantly impaired catalytic function, without evidence of gross structural alterations, subunit mixing experiments of mutant enzymes, subunit mixing experiments of mutant enzymes
A30L
site-directed mutagenesis, the mutant shows 93% reduced activity compared to the wild-type enzyme
C46A/C113A
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mutant lacking all Cys residues. Activity is slightly higher than wild-type
C46A/C113A/A29C
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introduction of Cys residue at transmembrane helix 1 into mutant lacking the native Cys residues. Low activity mutant, 64% trimer formation compared to wild-type
C46A/C113A/A30C
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introduction of Cys residue at transmembrane helix 1 into mutant lacking the native Cys residues. Low activity mutant, 79% trimer formation compared to wild-type
C46A/C113A/E28C
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introduction of Cys residue at transmembrane helix 1 into mutant lacking the native Cys residues. Low activity mutant, 93% trimer formation compared to wild-type
C46A/C113A/Q33C
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introduction of Cys residue at transmembrane helix 1 into mutant lacking the native Cys residues. Low activity mutant, 77% trimer formation compared to wild-type
C46A/C113A/R32C
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introduction of Cys residue at transmembrane helix 1 into mutant lacking the native Cys residues. Low activity mutant, 63% trimer formation compared to wild-type
C46A/C113AE34C
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introduction of Cys residue at transmembrane helix 1 into mutant lacking the native Cys residues. Low activity mutant, 100% trimer formation compared to wild-type
C46A/C113AF31C
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introduction of Cys residue at transmembrane helix 1 into mutant lacking the native Cys residues. Low activity mutant, 72% trimer formation compared to wild-type
D80A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D80E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D80N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D81A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D81K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D95A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D95E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E28A
site-directed mutagenesis, the mutation principally affects the binding of the Zn2+ ion, In the absence of the E28 side chain the zinc ions become purely coordinated by E76 and the ATP phosphates, the mutant shows highly reduced activity compared to the wild-type enzyme
E28D
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E28N
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E28Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E28R
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E34A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E34D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E34Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E69A
site-directed mutagenesis, inactive mutant, Asn72 plays a key role in catalysis. Its side-chain amide bridges Glu69 and Glu76
E69C
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mutant enzyme has an altered structure even in SDS
E69D
site-directed mutagenesis, inactive mutant, Asn72 plays a key role in catalysis. Its side-chain amide bridges Glu69 and Glu76
E69Q
site-directed mutagenesis, inactive mutant, Asn72 plays a key role in catalysis. Its side-chain amide bridges Glu69 and Glu76
E76D
site-directed mutagenesis, inactive mutant, Asn72 plays a key role in catalysis. Its side-chain amide bridges Glu69 and Glu76
E76L
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significantly impaired catalytic function, without evidence of gross structural alterations, subunit mixing experiments of mutant enzymes
E76Q
site-directed mutagenesis, inactive mutant, Asn72 plays a key role in catalysis. Its side-chain amide bridges Glu69 and Glu76
G20A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
G83P
site-directed mutagenesis, inactive mutant
G97P
site-directed mutagenesis, inactive mutant
I110P
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mutant enzyme can not be purified because its expression is toxic to the Escherichia coli host
I110R
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mutant enzyme can not be purified because its expression is toxic to the Escherichia coli host
I110W
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mutant is highly misfolding while at the same time being more stable than the wild-type protein
I110Y
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mutant exhibits enhanced stability but folds with an efficiency similar to that of the wild type
K94A
K94 coordinates both alpha-phosphate and N7 of the adenine ring of ATP, the loss of the basic side-chain releases the adenine of ATP and the binding is lost, almost inactive mutant
K94L
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significantly impaired catalytic function, without evidence of gross structural alterations. Km-value for MgATP2- raises 13fold, subunit mixing experiments of mutant enzymes
K94M
K94 coordinates both alpha-phosphate and N7 of the adenine ring of ATP, the loss of the basic side-chain releases the adenine of ATP and the binding is lost, the mutant shows highly reduced activity compared to the wild-type enzyme
K94R
K94 coordinates both alpha-phosphate and N7 of the adenine ring of ATP, the loss of the basic side-chain releases the adenine of ATP and the binding is lost, almost inactive mutant
N72A
site-directed mutagenesis, inactive mutant, Asn72 plays a key role in catalysis. Its side-chain amide bridges Glu69 and Glu76
N72D
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
N72Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
N72S
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significantly impaired catalytic function, without evidence of gross structural alterations, subunit mixing experiments of mutant enzymes
R32A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R32K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R9A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R9E
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R9H
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R9K
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
S17A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S73A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S90P
site-directed mutagenesis, inactive mutant
S98A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
W112L
-
site-directed mutagenesis, inactive mutant
W117L
-
site-directed mutagenesis, inactive mutant
W18L
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
W18L/W25L
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
W18L/W25L/W112L/W117L
-
site-directed mutagenesis, inactive mutant
W18L/W25L/W47L
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site-directed mutagenesis, reduced activity compared to the wild-type enzyme
W18L/W25L/W47L/W112L
-
site-directed mutagenesis, inactive mutant
W18L/W25L/W47L/W117L
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
W18L/W47L/W112L/W117L
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site-directed mutagenesis, inactive mutant
W18L/W47L/W117L
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site-directed mutagenesis, reduced activity compared to the wild-type enzyme
W25L
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site-directed mutagenesis, reduced activity compared to the wild-type enzyme
W25L/W47L/W112L/W117L
-
site-directed mutagenesis, inactive mutant
Y86A
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
Y86F
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
C20A
-
mutant shows diminished Zn occupancy
C60A
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mutant shows diminished Zn occupancy
E134Q
the mutant shows impaired Ca2+ binding
E179Q
the mutant is not able to bind Ca2+
E35G
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mutant exhibits greatly reduced polymerization. Samples of the mutant incubated with an excess of zinc are shifted entirely to the insoluble fraction. In absence of zinc, most of the mutant protein sample is monomeric. In the presence of added zinc, the mutant organizes into large sheet structures
F369A/F372A
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significant decrease in diacylglycerol kinase activity. Mutant cells display reduced uptake of transferrin
F369A/F372A/F748A
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significant decrease in diacylglycerol kinase activity. Mutant cells display reduced uptake of transferrin
F748A
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diacylglycerol kinase activity similar to that of wild-type. Mutant cells display reduced uptake of transferrin
G236R
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site-directed mutagenesis, highly reduced activity compared to the wild-type isozyme theta
G392D
activity of the mutant is less than 1% of the wild type enzyme
H16A
-
mutant shows diminished Zn occupancy
H38A
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mutant shows diminished Zn occupancy
H3A
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mutant shows diminished Zn occupancy
H3A/C20A/H38A/C60A
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mutant shows a reduced zinc retention of 3%. Construct does not show any increase in turbidity after incubation with 50 microM zinc acetate. In the absence of zinc, short polymers are observed, much like the wild-type protein. When zinc is added, polymers increase in prevalence and length marginally but no large sheet structures are formed in 50 microM zinc. Mutant diminishes the formation of cytoplasmic puncta, shows partially impaired regulation of transport to the plasma membrane, and lacks the ability to inhibit the formation of CopII coated vesicles
L241V
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site-directed mutagenesis, slightly reduced activity compared to the wild-type isozyme theta
L447
residue is required for the cholesterol recognition/interaction amino acid consensus motif, mutation results in a loss of enzymatic activity
L447I
ratio of enzymic activity with substrates 1-stearoyl-2-linoleoyl-sn-glycerol to 1-stearoyl-2-arachidonoyl-sn-glycerol is 0.054
P244A
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site-directed mutagenesis, reduced activity compared to the wild-type isozyme theta
P244L
-
site-directed mutagenesis, reduced activity compared to the wild-type isozyme theta
P245L
-
site-directed mutagenesis, highly reduced activity compared to the wild-type isozyme theta
P32A
redcution of both Km and kcat value, while maintianing the ratio kcat/Km constant. Specificity of mutant for substrates with polyunsaturated acyl chains is retained. Mutant has a higher affinity for membranes
R457K
ratio of enzymic activity with substrates 1-stearoyl-2-linoleoyl-sn-glycerol to 1-stearoyl-2-arachidonoyl-sn-glycerol is 0.217
R457Q
mutation results in the loss of the cholesterol recognition/interaction amino acid consensus motif and the loss of a positively charged residue, resulting in a higher enzymatic activity than wild-type. Ratio of enzymic activity with substrates 1-stearoyl-2-linoleoyl-sn-glycerol to 1-stearoyl-2-arachidonoyl-sn-glycerol is 0.099. Mutant gains preference for substrate 1-stearoyl-2-docosahexaenoyl-sn-glycerol
S240T
-
site-directed mutagenesis, activity is unaltered compared to the wild-type isozyme theta
S258D/S265D/S270D/S271D
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mutation in diacylglycerol kinase zeta for mimicking of protein kinase C phosphorylation of serine residues within the MARCKS phosphorylation site domain. Mutations do prevent binding to retinoblastoma protein
S258N/S265N/S270N/S271N
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mutation in diacylglycerol kinase zeta for mimicking of protein kinase C phosphorylation of serine residues within the MARCKS phosphorylation site domain. Mutations do not prevent binding to retinoblastoma protein and subsequent stimulation of activity
V52E
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mutant exhibits greatly reduced polymerization, no polymers are visible in zinc-free conditions. After zinc addition, large sheet structures appear
Y335F
expression of wild-type diacylglycerol kinase alpha markedly reduces ERK phosphorylation, whereas the effect of expressing the nonphosphorylatableY335F mutant is much less pronounced
Y451F
mutation results in a loss of a hydroxyl group and an essential residue of the cholesterol recognition/interaction amino acid consensus motif, leading to a higher activity than the wild-type protein. Ratio of enzymic activity with substrates 1-stearoyl-2-linoleoyl-sn-glycerol to 1-stearoyl-2-arachidonoyl-sn-glycerol is 0.107. Mutant gains preference for substrate 1,2-diarachidonoyl-sn-glycerol, with activities comparable to 1-stearoyl-2-arachidonoyl-sn-glycerol
C20S
-
mutation in sterile alpha-motif, mutant forms an oligomer
D43G
-
mutation in sterile alpha-motif, mutant is largely monomeric in solution
E35G
-
mutation in sterile alpha-motif, mutant is largely monomeric in solution
G53D
-
mutation in sterile alpha-motif, mutant is largely monomeric in solution
K45E
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mutation in sterile alpha-motif, mutant forms an oligomer
K56E
-
mutation in sterile alpha-motif, mutant is largely monomeric in solution
T57P
-
mutant with reduced activity, used for construcution of fusion protein for genetic selection of soluble mutants
V52E
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mutation in sterile alpha-motif, mutant is largely monomeric in solution
G279D
inactive mutant of diacylglycerol kinase epsilon due to replacement of ATP-binding domain GxGxxG with GxDxxG. Similar subcellular localization as wild type
G356D
inactive mutant of diacylglycerol kinase zeta due to replacement of ATP-binding domain GxGxxG with GxDxxG. Similar subcellular localization as wild type
G428D
inactive mutant of diacylglycerol kinase alpha due to replacement of ATP-binding domain GxGxxG with GxDxxG. Similar subcellular localization as wild type
G491D
inactive mutant of diacylglycerol kinase gamma due to replacement of ATP-binding domain GxGxxG with GxDxxG. Similar subcellular localization as wild type
G495D
inactive mutant of diacylglycerol kinase beta due to replacement of ATP-binding domain GxGxxG with GxDxxG. In contrast to the filamentous image of the wild type, mutant is diffusely distributed throughout the cytoplasm
D216A
mutant shows strongly reduced activity
D97A
mutant shows strongly reduced activity
K15A
mutant shows reduced activity
K15A/K165A
mutant shows strongly reduced activity
K165A
mutant shows reduced activity
N96A
mutant shows strongly reduced activity
R100A
mutant shows reduced activity
R20A
mutant shows wild type activity
T94A
mutant shows strongly reduced activity
D434A
-
site-directed mutagenesis, inactive mutant
D434N
-
site-directed mutagenesis, inactive mutant
D465A
-
site-directed mutagenesis, inactive mutant
D465N
-
site-directed mutagenesis, 0.1% of wild-type activity
D497A
-
site-directed mutagenesis, inactive mutant
D497N
-
site-directed mutagenesis, 0.9% of wild-type activity, reduced stimulation by Ca2+ and phosphatidylserine compared to the wild-type enzyme
D529A
-
site-directed mutagenesis, 1.1% of wild-type activity
D529N
-
site-directed mutagenesis, 5.5% of wild-type activity, unaltered stimulation by Ca2+ and phosphatidylserine compared to the wild-type enzyme
D650A
-
site-directed mutagenesis, inactive mutant
D650N
-
site-directed mutagenesis, inactive mutant
D697A
-
site-directed mutagenesis, 1.4% of wild-type activity
D697N
-
site-directed mutagenesis, 4.0% of wild-type activity, reduced stimulation by Ca2+ and phosphatidylserine compared to the wild-type enzyme
D95N
-
significantly impaired catalytic function, without evidence of gross structural alterations. Km-value for MgATP2- raises 18fold, subunit mixing experiments of mutant enzymes
D95N
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
E76A
site-directed mutagenesis, inactive mutant, Asn72 plays a key role in catalysis. Its side-chain amide bridges Glu69 and Glu76
E76A
site-directed mutagenesis, the mutation principally affects the binding of the Zn2+ ion
D124A
residue involved in the Mg1-water network, no catalytic acitivity
D124A
mutant shows strongly reduced activity
D271A
mutant shows almost no activity
D271A
residue involved in the Mg1-water network, no catalytic acitivity
D68A
mutant shows almost no activity
D68A
no catalytic activity. Role of D68 in mediating the interaction of Mg2+ with the gamma-phosphate of ATP
E273A
no catalytic activity
E273A
mutant shows almost no activity
additional information
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expression of fusion constructs of Green Fluorescent Protein to truncated forms of diacylglycerol kinase 1 and diacylglycerol kinase 2 missing the catalytic and accessory domains. Fusion proteins are localized to the endoplasmic reticulum. Fusion constructs of N-terminal 50 amino acid residues of diacylglycerol kinase 1 and the 43 residues of diacylglycerol kinase 2 to the Yellow Fluorescent Protein alos localize to the endoplasmic reticulum
additional information
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functional complementation of Escherichia coli dgkA mutant. Conditional inactivation of gene expression leads to the accumulation of diacylglycerol and the cessation of lipoteichoic acid formation in Bacillus subtilis
additional information
functional complementation of Escherichia coli dgkA mutant. Conditional inactivation of gene expression leads to the accumulation of diacylglycerol and the cessation of lipoteichoic acid formation in Bacillus subtilis
additional information
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determination of mutational defects/molecular lesions affecting the enzyme activity and splice forms of the enzyme, overview
additional information
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deletion mutants lacking respectively the entire C-terminal half of diacylglycerol kinase alpha or the last 13 amino acids PPPRSTNFFGFLS. Contrary to wild-type, mutants are not pulled down by immobilized GST-Src-SH3 fusion protein
additional information
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downregulation of diacylglycerol kinase alpha by siRNA impairs hepatocyte growth factor- and v-Src-induced cell scatter and migration, without affecting the loss of intercellular adhesions, impairs hepatocyre growth factor-induced cell spreading, lamellipodia formation, membrane ruffling, and focal adhesions remodeling and impairs hepatocyte growth factor-induced Rac activation and membrane targeting
additional information
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the ATP binding sequence of isozyme DGK2in strain rdgA contains the mutant GXDXXG motif leading to rapid retinal degeneration after birth
additional information
generation of a mutant defective in the gene encoding DGK, rdgA
additional information
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generation of a mutant defective in the gene encoding DGK, rdgA
additional information
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generation of a mutant defective in the gene encoding DGK, rdgA
-
additional information
construction of a thermostabilized DELTA4 (4 changes relative to wild-type) form of DgkA using the DELTA7 structure, overview
additional information
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construction of deletion mutants, N- or C-terminal truncations inactivate the isozyme theta
additional information
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mutation of the second glycine in the binding sequence motif GXGXXG of the ATP-binding site to aspartate or alanine renders the mutant enzymes catalytically inactive
additional information
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truncated form of the protein (DGKDELTAepsilon) lacking the 40 N-terminal amino acids. Full-length FLAG-DGKepsilon and truncated FLAG-DGKepsilon are both more specific for 1-stearoyl-2-arachidonoyl-sn-glycerol than for 1,2-dioleoyl-sn-glycerol. 1-Stearoyl-2-linoleoyl-sn-glycerol exhibits intermediate specificity for both forms of the enzyme. The truncated form of the enzyme maintains substrate specificity for lipids with an arachidonoyl moiety present at the sn-2 position. The truncation increases the catalytic rate constant for all three substrates and may suggest a role in the negative regulation of this enzyme
additional information
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diacylglycerol kinase delta has alternative splicing variants, type 1 DGKdelta1 and type 2 DGKdelta2, with calculated molecular masses of 130 and 134 kDa, respectively. HeLa cells express both type 1 and 2 DGKdelta, and COS7 cells express only type 2 DGKdelta. In DGKdelta-knockdown cells uptake of transferrin is reduced. DGKdelta2 is partially co-localized with clathrin or adaptor protein AP2alpha in COS7 cells. Mutants lacking binding ability to AP2alpha as well as kinase-negative mutants cannot compensate for the uptake of transferrin inhibited by siRNA treatment. Overexpression of wild-type diacylglycerol kinase delta2 completely recovers the transferrin uptake
additional information
expression of a peptide corresponding to a putative transmembrane segment which comprises approximately residues 20-40 and is found in all forms of mammalian diacylglycerol kinase epsilon. Peptide KKKKLILWTLCSVLLPVFITFWKKKKK-NH2 has increased helical content and significant blue shifts in the presence of anionic but not zwitterionic bilayer membranes. Peptide dimerizes and preferentially interacts with cholesterol in lipid films comprised of homogeneous mixtures of cholesterol and phosphatidylcholine, yet the presence of cholesterol in hydrated vesicle bilayers decreases its helical content
additional information
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expression of truncated FLAG-tagged protein lacking the 40 N-terminal amino acids, which includes the hydrophobic segment. Truncated protein maintains substrate specificity and increases catalytic rate constant. Truncated protein may be extracted with 1.5 M KCl at neutral pH value, while wild-type protein remains fully membrane bound
additional information
heterologous expression of diacylglycerol kinase gamma in COS-7 cells. Upon stimulation with epidermal growth factor, enzyme specifically interacts and co-localizes at the plasma membrane with beta2-chimaerin. Enzyme enhances epidermal growth factor-dependent translocation of beta2-chimaerin to the plasma membrane and markedly augments epidermal growth factor-dependent GTPase-activating protein activity of beta2-chimaerin
additional information
in a female patient with a de novo balanced translocation, 46,X,t(X,2)(p11.2,q37)dn, who exhibits seizures, capillary abnormality, developmental delay, infantile hypotonia, and obesity, diacylglycerol kinase delta is disrupted at 2q37. Diacylglycerol kinase delta is involved in the etiology of seizures
additional information
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in a female patient with a de novo balanced translocation, 46,X,t(X,2)(p11.2,q37)dn, who exhibits seizures, capillary abnormality, developmental delay, infantile hypotonia, and obesity, diacylglycerol kinase delta is disrupted at 2q37. Diacylglycerol kinase delta is involved in the etiology of seizures
additional information
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overexpression of wild-type diacylglycerol kinase alpha, but not of its kinase-dead mutant, markedly suppresses tumor necrosis factor alpha-induced apoptosis of AKI human melanoma cells and enhances the tumor necrosis factor alpha-stimulated transcriptional activity of transcription factor NF-kappaB. siRNA-mediated knock-down of diacylglycerol kinase alpha enhances the apoptosis. Overexpression of isoforms beta and gamma has no detectable effect on apoptosis
additional information
overexpression of wild-type diacylglycerol kinase alpha, but not of its kinase-dead mutant, markedly suppresses tumor necrosis factor alpha-induced apoptosis of AKI human melanoma cells and enhances the tumor necrosis factor alpha-stimulated transcriptional activity of transcription factor NF-kappaB. siRNA-mediated knock-down of diacylglycerol kinase alpha enhances the apoptosis. Overexpression of isoforms beta and gamma has no detectable effect on apoptosis
additional information
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RNA interference-mediated knockdown of diacylglycerol kinase zeta leads to accelerated transferrin receptor exit from the lymphocyte endocytic recycling compartment back to the plasma membrane
additional information
RNA interference-mediated knockdown of diacylglycerol kinase zeta leads to accelerated transferrin receptor exit from the lymphocyte endocytic recycling compartment back to the plasma membrane
additional information
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silencing of diacylglycerol kinase theta by siRNA expression inhibits cAMP-dependent CYP17 transcription. LXXLL motifs in diacylglycerol kinase theta mediate a direct interaction of steroidogenic factor 1 with the kinase and may facilitate binding of phosphatidic acid to the receptor
additional information
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mutation of the second glycine in the binding sequence motif GXGXXG of the ATP-binding site to aspartate or alanine renders the mutant enzymes catalytically inactive
additional information
construction of mutant protein lacking the regulatory N-terminus and both C1 domains. Mutant is enzymatically active. deletion analysis reveals that the C1 domains are essential for plasma membrane targeting in intact cells but unnecessary for catalytic activity. The C-terminal sequence is required for membrane-binding in a phosphatidic acid-dependent manner. In the absence of the calcium binding domain, receptor-dependent translocation of the truncated protein is regulated by phosphorylation of residue Y335
additional information
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creation of thoracic transverse aortic constriction in transgenic mice with cardiac-specific overexpression of diacylglycerol kinase zeta and wild-type mice. Increases in heart weight at 4 weeks after thoracic transverse aortic constriction are attenuated in diacylglycerol kinase zeta transgenic mice compared with wild-type mice. Increases in interventricular septal thickness, dilatation of the left ventricular cavity, and decreases in left ventricular systolic function in wild-type mice are observed at 4 weeks after surgery and are attenuated in diacylglycerol kinase zetatransgenic mice. Contrary to wild-type, cardiac fibrosis and gene induction of type I and type III collagens, but not transforming growth factor are blocked in diacylglycerol kinase zeta transgenic mice
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deficiency for diacylglycerol kinase zeta results in impaired interleukin 12 and tumor necrosis factor alpha production following toll-like receptor stimulation in vitro and in vivo, increased resistance to endotoxin shock, and enhanced susceptibility to Toxoplasma gondii infection. Deficiency results in increased activation of the phosphatidylinositol 3-kinase-Akt pathway. Inhibition of phosphatidylinositol 3-kinase activity or treatment with phosphatidic acid can restore lipopolysaccharide-induced interleukin 12 production by diacylglycerol kinase zeta-deficient mice
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deficiency for diacylglycerol kinase zeta results in impaired interleukin 12 and tumor necrosis factor alpha production following toll-like receptor stimulation in vitro and in vivo, increased resistance to endotoxin shock, and enhanced susceptibility to Toxoplasma gondii infection. Deficiency results in increased activation of the phosphatidylinositol 3-kinase-Akt pathway. Inhibition of phosphatidylinositol 3-kinase activity or treatment with phosphatidic acid can restore lipopolysaccharide-induced interleukin 12 production by diacylglycerol kinase zeta-deficient mice
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diacylglycerol kinase delta knock-down mice reveal abnormal epiletic discharges and electrographic seizures in three out of six homozygotes
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expression of isolated His-tagged sterile alpha-motif domain of diacylglycerol kinase delta1, comprised of residues 1097-1164. The domain forms large aggregates with a molecular weight of 250000 Dalton or greater, while calculated monomer molecular weight is 9500 Dalton
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generation of double transgenic mice with cardiac-specific overexpression of both diacylglycerol kinase zeta and G-protein subunit alphaq. Diacylglycerol kinase zeta prevents cardiac dysfunction, determined by dilatation of left ventricular dimensions, reduction of left ventricular fractional shortening, and marked increases in left ventricular end-diastolic pressure in G-protein subunit alphaq transgenic mice. Translocation of protein kinase C isoforms, phosphorylation activity of c-jun N-terminal kinase and p38 mitogen-activated protein kinase in G-protein subunit alphaq transgenic mice are attenuated by diacylglycerol kinase zeta?. Diacylglycerol kinase zeta improves the survival rate of G-protein subunit alphaq transgenic mice
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generation of double transgenic mice with cardiac-specific overexpression of both diacylglycerol kinase zeta and G-protein subunit alphaq. Diacylglycerol kinase zeta prevents cardiac dysfunction, determined by dilatation of left ventricular dimensions, reduction of left ventricular fractional shortening, and marked increases in left ventricular end-diastolic pressure in G-protein subunit alphaq transgenic mice. Translocation of protein kinase C isoforms, phosphorylation activity of c-jun N-terminal kinase and p38 mitogen-activated protein kinase in G-protein subunit alphaq transgenic mice are attenuated by diacylglycerol kinase zeta?. Diacylglycerol kinase zeta improves the survival rate of G-protein subunit alphaq transgenic mice
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generation of heterozygous diacylglycerol kinase delta whole-body knockout mice. Diacylglycerol kinase delta haploinsufficiency increases diacylglycerol content, reduces peripheral insulin sensitivity, insulin signaling, and glucose transport, and leads to age-dependent obesity. Metabolic flexibility is impaired
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generation of mice lacking both diacylglycerol kinase alpha and zeat. Absence of both diacylglycerol kinases results in a severe decrease in the number of CD4+CD8- and CD4-CD8+ single-positive thymocytes correlating with increased diacylglycerol kinase-mediated signaling. Positive selection, but not negative selection, is impaired in diacylglycerol kinase alpha-/- zeta -/- mice. The developmental blockage in diacylglycerol kinase alpha-/- zeta -/- mice can be partially overcome by treatment with phosphatidic acid. Decreased diacylglycerol kinase activity also promotes thymic lymphomagenesis accompanying elevated Ras and Erk1/2 activation
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in mouse ventricular myocytes overexpressing diaclyglycerol kinase zeta, the effect induced by endothelin-1 on Ca2+ transients and cell shortening are abolished
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in mouse ventricular myocytes overexpressing diaclyglycerol kinase zeta, the effect induced by endothelin-1 on Ca2+ transients and cell shortening are abolished
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overexpression of diacylglycerol kinase zeta blocks cells in G1 phase of cell cycle. Cell cycle arrest is accompanied by decreased levels of retinoblastoma protein phosphorylated on Ser-807/811. Down-regulation by siRNA increases the number of cells in both the S and G2/M phases of the cell cycle and prevents the cell cycle block characterizing C2C12 cell myogenic differentiation
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overexpression of diacylglycerol kinase zeta blocks cells in G1 phase of cell cycle. Cell cycle arrest is accompanied by decreased levels of retinoblastoma protein phosphorylated on Ser-807/811. Down-regulation by siRNA increases the number of cells in both the S and G2/M phases of the cell cycle and prevents the cell cycle block characterizing C2C12 cell myogenic differentiation
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transgenic mice with cardiac-specific overexpression of diacylglycerol kinase zeta. Left ventricular chamber dilatation, reduction of left ventricular systolic function and increases in left ventricular weight and lung weight at 4 weeks after myocardial infarction are attenuated in transgenic mice compared with wild-type mice. In the noninfarct area, fibrosis fraction and upregulation of profibrotic genes, such as transforming growth factor-1, collagen type I, and collagen type III, are blocked in transgenic mice. Survival rate at 4 weeks after myocardial infarction is higher in transgenic mice than in wild-type
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transgenic mice with cardiac-specific overexpression of diacylglycerol kinase zeta. Left ventricular chamber dilatation, reduction of left ventricular systolic function and increases in left ventricular weight and lung weight at 4 weeks after myocardial infarction are attenuated in transgenic mice compared with wild-type mice. In the noninfarct area, fibrosis fraction and upregulation of profibrotic genes, such as transforming growth factor-1, collagen type I, and collagen type III, are blocked in transgenic mice. Survival rate at 4 weeks after myocardial infarction is higher in transgenic mice than in wild-type
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nuclear export signal mutant forms of DGK-zeta accumulate in the nucleus to a much greater extent than wild type DGK-zeta
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nuclear export signal mutant forms of DGK-zeta accumulate in the nucleus to a much greater extent than wild type DGK-zeta
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generation of enzyme-deficient DGKdelta-KO mouse embryonic fibroblasts
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generation of transgenic tobacco plants constitutively expressing rice diacylglycerol kinase. Overexpression results in enhanced resistance against infection by tobacco mosaic virus and Phytophthora parasitica var. nicotianae
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generation of transgenic tobacco plants constitutively expressing rice diacylglycerol kinase. Overexpression results in enhanced resistance against infection by tobacco mosaic virus and Phytophthora parasitica var. nicotianae
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antisense silencing of diacylglacerol kinase isoform delta, but not alpha, expression is sufficient to prevent the effect of high glucose on protein kinase alpha activity, insulin receptor signaling, and glucose uptake
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diacylglycerol kinase zeta siRNA tranfection decreases H2O2-induced apoptosis. Overexpression of kinase-dead diacylglycerol kinase zeta significantly increases protein kinase D phosphorylation
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construction of deletion mutants DELTA196, lacking the RVH motif and the EF hand, and DELTA332, lacking the RVH motif, the EF hand, and the C1 domain, mutant DELTA332 shows 50% of wild-type activity
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