Any feedback?
Information on EC 3.1.4.4 - phospholipase D and Organism(s) Rattus norvegicus and UniProt Accession P70496
for references in articles please use BRENDA:EC3.1.4.4Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.1.4.4 phospholipase DIUBMB Comments
Also acts on other phosphatidyl esters.
Specify your search results
Word Map
- 3.1.4.4
-
phosphatidic
- diacylglycerol
- pkc
-
liposomal
- doxorubicin
- agonist
-
pegylated
-
phorbol
- phospholipases
-
transphosphatidylation
- 12-myristate
-
adp-ribosylation
- 13-acetate
- pertussis
-
phosphohydrolase
-
arachidonic
- propranolol
- phosphoinositide
-
gtp-binding
- fmlp
-
prelabeled
- anandamide
- rhoa
- 1-butanol
-
endocannabinoids
- staurosporine
-
lysophosphatidic
- pc-plc
-
phosphatidylcholine-specific
-
latissimus
- diglyceride
- pkcalpha
-
phosphatidylinositol-specific
- pseudotuberculosis
- 1,2-diacylglycerol
- arf6
- cannabinoids
-
fmet-leu-phe
-
listening
-
fmlp-stimulated
-
platinum-resistant
- analysis
-
phosphoinositide-specific
- gtpgammas
- synthesis
-
3hcholine
-
hand-foot
-
platinum-sensitive
-
fmlp-induced
- lymphadenitis
- medicine
-
ptdins4,5p2
- molecular biology
- 5-kinase
- agriculture
- biotechnology
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
pld, phospholipase d, nape-pld, phospholipase d1, dermonecrotic toxin, phospholipase d2, pc-pld, pldalpha, rpld1, spo14, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AtPLDalpha1
-
-
-
-
AtPLDalpha2
-
-
-
-
AtPLDbeta1
-
-
-
-
AtPLDbeta2
-
-
-
-
AtPLDdelta
-
-
-
-
AtPLDepsilon
-
-
-
-
AtPLDgamma1
-
-
-
-
AtPLDgamma2
-
-
-
-
AtPLDgamma3
-
-
-
-
AtPLDp1
-
-
-
-
AtPLDp2
-
-
-
-
AtPLDzeta
-
-
-
-
choline phosphatase
-
-
-
-
hPLD1
-
-
-
-
hPLD2
-
-
-
-
lecithinase D
-
-
-
-
lipophosphodiesterase II
-
-
-
-
Meiosis-specific sporulation protein SPO14
-
-
-
-
mPLD1
-
-
-
-
mPLD2
-
-
-
-
Phosphatidylcholine-hydrolyzing phospholipase D1
-
-
-
-
Phosphatidylcholine-hydrolyzing phospholipase D2
-
-
-
-
phospholipase D
Phospholipase D1 PHOX and PX containing domain
-
-
-
-
Phospholipase D2 PHOX and PX containing domain
-
-
-
-
PLD
PLD delta
-
-
-
-
PLD epsilon
-
-
-
-
PLD zeta
-
-
-
-
PLD1
-
-
PLD1C
-
-
-
-
PLD2
PLDalpha
-
-
-
-
PLDalpha3
-
-
-
-
PLDbeta
-
-
-
-
PLDdelta1
-
-
-
-
PLDzeta1
-
-
-
-
PLDzeta2
-
-
-
-
rPLD1
-
-
-
-
rPLD2
-
-
-
-
PLD
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
phosphatidylcholine phosphatidohydrolase
Also acts on other phosphatidyl esters.
CAS REGISTRY NUMBER
COMMENTARY
9001-87-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-O-octadecyl-sn-glycero-3-phosphocholine + H2O
1-O-octadecyl-sn-glycero-3-phosphatidate + choline
-
-
-
-
?
dipalmitoylphosphatidylcholine + H2O
dipalmitoylglycerophosphate + choline
-
-
-
-
?
glycerophospho-(N-palmitoyl)ethanolamine + H2O
N-palmitoylethanolamine + ?
-
-
1% of the activity with N-palmitoyl-phosphatidylethanolamine
-
?
N-acyl-phosphatidylethanolamine + H2O
N-acylethanolamine + phosphatidate
-
high specificity for N-acyl-phosphatidylethanolamines without selectivity for long chain or medium chain N-acyl species
-
-
?
N-acylphosphatidylethanolamine + H2O
N-acylethanolamine + phosphatidate
-
-
-
-
?
N-arachidonoyl-phosphatidylethanolamine + H2O
phosphatidic acid + N-arachidonoylethanolamine
-
-
-
?
N-lauroyl-phosphatidylethanolamine + H2O
phosphatidic acid + N-lauroylethanolamine
-
-
-
-
?
N-palmitoyl-lyso-phosphatidylethanolamine + H2O
N-palmitoylethanolamine + sn-glycerol 3-phosphate
-
-
4% of the activity with N-palmitoyl-phosphatidylethanolamine
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
N-palmitoyl-phosphatidylethanolamine + H2O
phosphatidic acid + N-palmitoylethanolamine
-
-
-
?
N-palmitoyl-phosphatidylethanolamine + H2O
phosphatidic acid + N-palmitoylethanolamine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
both phosphatidylcholine and phosphatidylethanolamine are substrates for phospholipase D in UMR-106 osteoblastic cells and can therefore be sources of phospholipid hydrolysis products for downstream signaling in osteoblast
-
-
?
phosphatidylethanolamine + H2O
1,2-diacylglycerophosphate + ethanolamine
-
-
-
-
?
phosphatidylethanolamine + H2O
1,2-diacylglycerophosphate + ethanolamine
-
parathyroid hormone stimulates phosphatidylethanolamine hydrolysis by phospholipase D in osteoblastic cells. Both phosphatidylcholine and phosphatidylethanolamine are substrates for phospholipase D in UMR-106 osteoblastic cells and can therefore be sources of phospholipid hydrolysis products for downstream signaling in osteoblast
-
-
?
additional information
?
-
-
5-[4-acridin-[9-ylamino]phenyl]-5-methyl-3-methylenedihydrofuran-2-one inhibits the formyl-Met-Leu-Phe-stimulated phospholipase D activity, mainly through the blockade of RhoA activation and degranulation
-
-
?
additional information
?
-
-
alpha-adrenoreceptor activation increases phospholipase D activity
-
-
?
additional information
?
-
-
dependency of activation of protein kinase D on phospholipase D, phospholipase D could be a key molecule that links Rho/protein kinase C signaling to diacylglycerol for protein kinase D activation
-
-
?
additional information
?
-
-
interaction of the PLD1 PX domain with phosphatidylinositol 3,4,5-trisphosphate and/or phosphatidic acid (or phosphatidylserine) may be an important factor in the spatiotemporal regulation and activation of PLD1
-
-
?
additional information
?
-
-
lysophosphatidic acid activates protein translation through the action of PLD1-generated phosphatidic acid on mTOR and the phosphoinositide 3-kinase/Akt pathway
-
-
?
additional information
?
-
-
Munc-18-1 is a potent negative regulator of basal PLD activity. EGF stimulation abolishes this interaction
-
-
?
additional information
?
-
-
phospholipase D elevates the level of MDM2 and suppresses DNA damage-induced increase in p53
-
-
?
additional information
?
-
-
phospholipase D plays an important role in the regulation of beta-hexosaminidase release in actively sensitized rat peritoneal mast cells
-
-
?
additional information
?
-
-
PLD1 is a signaling node, in which integration of convergent signals occurs within discrete locales of the cellular membrane
-
-
?
additional information
?
-
-
PLD2 may be involved in early developmental processes of some neuronal progenitors
-
-
?
additional information
?
-
-
prolonged elevation of PLD activity is required for myogenic differentiation
-
-
?
additional information
?
-
-
the enzyme participates in myogenesis through phosphatidic acid- and phosphatidylinositol bisphosphate-dependent actin fiber formation
-
-
?
additional information
?
-
-
thyrotrophin-releasing hormone increases phospholipase D activity through stimulation of protein kinase C in GH3 cells
-
-
?
additional information
?
-
-
no substrate: N-palmitoylethanolamine phosphate, phosphatidylcholine, phosphatidylserine, phosphatidylinositol
-
-
?
additional information
?
-
-
phospholipase D activates native TRPC3 cation channels after stimulation of G-protein-coupled type I glutamate receptors in the cerebellum. Small GTPases might be involved in the activation mechanism of TRPC3 in rat cerebellar Purkinje cells, overview
-
-
?
additional information
?
-
-
PLD catalyzes the hydrolysis of phospholipids resulting in the generation of phosphatidic acid and the release of the polar head group. The enzyme also catalyzes a transphosphatidylation reaction, in which the aliphatic chain of the primary alcohol is transferred to the phosphatidyl moiety of the phosphatidic acid product
-
-
?
additional information
?
-
-
PLD performs two different reactions: a hydrolytic reaction and a transphosphatidylation reaction, 1-butanol serves as acceptor in the transphosphatidylation reaction, while 2-butanol does not. PLD-catalysed PtdOH formation may be necessary for EGF-induced macropinocytosis
-
-
?
additional information
?
-
-
except for PLD2c, all PLD1 and PLD2 isozymes contain the catalytic core regions comprised of highly conserved domain I-IV. In domains II and IV, the enzymes contain two HxKxxxxD sequences designated HKD motifs, which are essential for enzymatic catalysis
-
-
?
additional information
?
-
-
PLD also performs transphosphatidylation using ethanol as phosphatidyl acceptor
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
both phosphatidylcholine and phosphatidylethanolamine are substrates for phospholipase D in UMR-106 osteoblastic cells and can therefore be sources of phospholipid hydrolysis products for downstream signaling in osteoblast
-
-
?
phosphatidylethanolamine + H2O
1,2-diacylglycerophosphate + ethanolamine
-
parathyroid hormone stimulates phosphatidylethanolamine hydrolysis by phospholipase D in osteoblastic cells. Both phosphatidylcholine and phosphatidylethanolamine are substrates for phospholipase D in UMR-106 osteoblastic cells and can therefore be sources of phospholipid hydrolysis products for downstream signaling in osteoblast
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
additional information
?
-
-
5-[4-acridin-[9-ylamino]phenyl]-5-methyl-3-methylenedihydrofuran-2-one inhibits the formyl-Met-Leu-Phe-stimulated phospholipase D activity, mainly through the blockade of RhoA activation and degranulation
-
-
?
additional information
?
-
-
alpha-adrenoreceptor activation increases phospholipase D activity
-
-
?
additional information
?
-
-
dependency of activation of protein kinase D on phospholipase D, phospholipase D could be a key molecule that links Rho/protein kinase C signaling to diacylglycerol for protein kinase D activation
-
-
?
additional information
?
-
-
interaction of the PLD1 PX domain with phosphatidylinositol 3,4,5-trisphosphate and/or phosphatidic acid (or phosphatidylserine) may be an important factor in the spatiotemporal regulation and activation of PLD1
-
-
?
additional information
?
-
-
lysophosphatidic acid activates protein translation through the action of PLD1-generated phosphatidic acid on mTOR and the phosphoinositide 3-kinase/Akt pathway
-
-
?
additional information
?
-
-
Munc-18-1 is a potent negative regulator of basal PLD activity. EGF stimulation abolishes this interaction
-
-
?
additional information
?
-
-
phospholipase D elevates the level of MDM2 and suppresses DNA damage-induced increase in p53
-
-
?
additional information
?
-
-
phospholipase D plays an important role in the regulation of beta-hexosaminidase release in actively sensitized rat peritoneal mast cells
-
-
?
additional information
?
-
-
PLD1 is a signaling node, in which integration of convergent signals occurs within discrete locales of the cellular membrane
-
-
?
additional information
?
-
-
PLD2 may be involved in early developmental processes of some neuronal progenitors
-
-
?
additional information
?
-
-
prolonged elevation of PLD activity is required for myogenic differentiation
-
-
?
additional information
?
-
-
the enzyme participates in myogenesis through phosphatidic acid- and phosphatidylinositol bisphosphate-dependent actin fiber formation
-
-
?
additional information
?
-
-
thyrotrophin-releasing hormone increases phospholipase D activity through stimulation of protein kinase C in GH3 cells
-
-
?
additional information
?
-
-
phospholipase D activates native TRPC3 cation channels after stimulation of G-protein-coupled type I glutamate receptors in the cerebellum. Small GTPases might be involved in the activation mechanism of TRPC3 in rat cerebellar Purkinje cells, overview
-
-
?
additional information
?
-
-
PLD catalyzes the hydrolysis of phospholipids resulting in the generation of phosphatidic acid and the release of the polar head group. The enzyme also catalyzes a transphosphatidylation reaction, in which the aliphatic chain of the primary alcohol is transferred to the phosphatidyl moiety of the phosphatidic acid product
-
-
?
additional information
?
-
-
PLD performs two different reactions: a hydrolytic reaction and a transphosphatidylation reaction, 1-butanol serves as acceptor in the transphosphatidylation reaction, while 2-butanol does not. PLD-catalysed PtdOH formation may be necessary for EGF-induced macropinocytosis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
n-butanol
n-butanol completely blocks the migration of NBT-II cells on collagen-coated substrates and disturbes the characteristic localization of actin along edge of lamellipodia
5,5'-dimethyl-1,2-bis-(2-aminophenoxy)-ethane-N,N,N',N'-tetraacetic acid
-
partial
5-[4-acridin-[9-ylamino]phenyl]-5-methyl-3-methylenedihydrofuran-2-one
-
inhibits the formyl-Met-Leu-Phe-stimulated phospholipase D activity, mainly through the blockade of RhoA activation and degranulation
Munc-18-1
-
inhibits phospholipase D activity by direct interaction in an epidermal growth factor-reversible manner
-
1-butanol
-
does not causes direct inhibition of TRPC3 channels, but causes blocking of phospholipase D which interferes with retrograde signaling, overview. Neither voltage-gated Ca2+-channels nor Ca2+-activated Cl channels are affected by 1-butanol
additional information
-
the silica-induced phospholipase D activity is partially attenuated by the pretreatment with U73122, genistein, PD 98056 and mepacrine
-
additional information
n-butanol completely blocks the migration of NBT-II cells on collagen-coated substrates and disturbes the characteristic localization of actin along edge of lamellipodia
-
additional information
n-butanol completely blocks the migration of NBT-II cells on collagen-coated substrates and disturbes the characteristic localization of actin along edge of lamellipodia
-
additional information
-
PLD activity is decreased in the presence of components required for the monooxygenase (MMO) activity (reducing system), including 100% phosphatidylcholine membranes, NADPH-cytochrome P450 reductase and NADPH. Lysophosphatidylserine recoveres the PLD activity in a concentration-dependent manner
-
additional information
-
dominant negative Rac1, N17Rac1, completely inhibits PLD activation by EGF, but not by PDGF. Dominant-negative RalA and Ras also abolish PLD activation by EGF
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
amyloid beta peptide
-
residues 1-42, i.e. Abeta1-42, a formyl-peptid-receptor-like 1 agonist, activates 3-4fold in microglia and astrocytes, respectively, at 0.001 mM. Endocytosis of Abeta1-42 in glial cells is PLD-dependent
-
Arf-1
-
the catalytic activator stimulates PLD1 by enhancing the catalytic constant kcat. Full-length enzyme and N-terminally truncated enzyme are strongly activated by Arf-1-GTPgammaS
-
ATP
-
extracellular application of nucleotides stimulates enzyme activity and shows a sustained activation of extracellular signal-regulated kinase. Effects on enzyme and extracellular signal-regulated kinase are not additive and not coupled to DNA synthesis. Best effects are with ATP and UTP at 0.01 mM and above
Carbachol
-
PLD1 is activated by cholinergic agonists. Atropine inhibits this PLD1 activation
CtBP1/BARS
-
a short splice variant of the CtBP1 gene and a physiological activator of PLD1 required in agonist-induced macropinocytosis. Stimulation of cells by serum or EGF results in the association of CtBP1/BARS with PLD1, which is specifically blocked by 1-butanol. CtBP1/BARS acts synergistically with ARF1 protein in activation of PLD, dependent on GTPgammaS or GTP but not on GDP, overview
-
dynamin
-
a large GTPase, can interact with PLD in a GTP dependent manner in vitro
-
formylmethionyl-leucyl-proline
-
i.e. fMLF, activates 4fold in microglia and astrocytes, respectively, at 0.001 mM, the activation is inhibited by WRW4, a formyl-peptid-receptor-like 1 antagonist
GTPgammaS
-
membrane fraction, 5fold increase in activity, membrane plus cytosolic fraction, 8fold increase in activity
lysophosphatidylserine
-
stimulates PLD activity in a concentration-dependent manner and approximately 5fold and 8fold increases in CYP1A2 and CYP2E1 activities, respectively, are shown in the presence of 2 mol% of the lysophosphatidylserine when compared to a 100% phosphatidylcholine matrix. LysoPS also accompanies conformational changes in both CYP1A2 and CYP2E1 when assayed by circular dichroism
phorbol 12-myristate 13-acetate
-
activates 13fold at 0.001 mM in microglia and astrocytes
phosphatidylinositol-4,5-bisphosphate
-
an essential cofactor for phospholipase D1 activity
protein kinase Calpha
-
activation of PLD1 involves N- and C-terminal PLD domains
-
Rho GTPases
-
PLD1 and PLD2 activity is regulated by the Rho family of small GTPases
-
Rho protein
-
small G proteins of the Rho and Arf families activate phospholipase D1. Small GTPases might be involved in the activation mechanism of TRPC3 in rat cerebellar Purkinje cells. Rho GTPases can activate phospholipase D1 through two mechanisms: direct binding to phospholipase D1 or activation of phosphatidylinositol-4,5-kinase, which triggers phosphatidylinositol-4,5-bisphosphate production, an essential cofactor for phospholipase D1 activity
-
thyrotropin
-
PLD-1, stimulation up to 2.3fold, accompanied by translocation of ADP-ribosylation factor and RhoA to the membrane fraction
-
UDP
-
extracellular application of nucleotides stimulates enzyme activity and shows a sustained activation of extracellular signal-regulated kinase. Effects on enzyme and extracellular signal-regulated kinase are not additive and not coupled to DNA synthesis. Best effects are with ATP and UTP at 0.01 mM and above
UTP
-
extracellular application of nucleotides stimulates enzyme activity and shows a sustained activation of extracellular signal-regulated kinase. Effects on enzyme and extracellular signal-regulated kinase are not additive and not coupled to DNA synthesis. Best effects are with ATP and UTP at 0.01 mM and above
ARF protein
-
ARF family small GTPases, which are composed of six isoforms, ARF1-6 act as PLD activators, they activates PLD1 and PLD2. ARFs are myristoylated at their N-terminal glycine residue and this lipid modification is required to fully activate PLD1 [11,12]. In the ARF-dependent activation of PLD1, phosphatidylinositol 4,5-disphosphate is an essential cofactor. Phosphatidylinositol 3,4,5-trisphosphate and phosphatidylinositol 4,5-disphosphate act as cofactors and bind to the PX domain, which is also responsible for protein-protein interactions. PLD2 directly interacts with the phosphatidylinositol 4-phosphate 5-kinase
-
ARF protein
-
small G proteins of the Rho and Arf families activate phospholipase D1
-
Arf1 protein
-
activates PLD, acts synergistically with CtBP1/BARS in activation of PLD, dependent on GTPgammaS or GTP but not on GDP, overview
-
Cdc42
-
stimulation of full-length enzyme and N-terminally truncated enzyme by GTPgammaS-loaded Cdc42
-
Cdc42
-
in addition to interactions with Rac and Rho, PLD1 is regulated by Cdc42
-
phosphatidylinositol 4,5-bisphosphate
-
stimulation of full-length enzyme and N-terminally truncated enzyme
Rac1
-
stimulation of full-length enzyme and N-terminally truncated enzyme by GTPgammaS-loaded Rac1
-
Rac1
-
PLD activation by EGF is dependent on Rac1, and not on PKC, in Rat1 fibroblasts
-
RhoA
-
small G proteins ARF3 and RhoA in the presence of guanosine 5'-3-O-(thio)triphosphate
RhoA
-
stimulation of full-length enzyme and N-terminally truncated enzyme by GTPgammaS-loaded RhoA
additional information
-
interaction of the PLD1 PX domain with phosphatidylinositol 3,4,5-trisphosphate and/or phosphatidic acid (or phosphatidylserine) may be an important factor in the spatiotemporal regulation and activation of PLD1
-
additional information
-
no activation of thymocyte enzyme by eicosapentaenoic acid. Negative correlation of enzyme activation and proliferative response of thymocytes to fatty acids
-
additional information
-
activation mechanism of PLD in macropinocytosis, overview
-
additional information
-
epidermal growth factor triggers the activation of PLD in various cell types, such as calvarial osteoblastic cells and 3Y1 rat fibroblasts
-
additional information
-
in some physiological settings, the PLD2 activity appears to be regulated by the classical MAP kinase, extracellular signal-regulated kinase pathway
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
KM-value for phosphatidylcholine (unstimulated) is 33mol%, full-length enzyme
-
0.0029
N-palmitoyl-phosphatidylethanolamine
-
mutant DELTAN55, 37°C, pH 7.4, presence of 10 mM MgCl2
0.0036
N-palmitoyl-phosphatidylethanolamine
-
mutant 387stop, 37°C, pH 7.4, presence of 10 mM MgCl2
0.0042
N-palmitoyl-phosphatidylethanolamine
-
mutant C237S, 37°C, pH 7.4, presence of 10 mM MgCl2
0.0043
N-palmitoyl-phosphatidylethanolamine
-
mutant C222S, 37°C, pH 7.4, presence of 10 mM MgCl2
0.0045
N-palmitoyl-phosphatidylethanolamine
-
mutant C288S, 37°C, pH 7.4, presence of 10 mM MgCl2
0.0047
N-palmitoyl-phosphatidylethanolamine
-
mutant C170S, 37°C, pH 7.4, presence of 10 mM MgCl2
0.0047
N-palmitoyl-phosphatidylethanolamine
-
wild-type, 37°C, pH 7.4, presence of 10 mM MgCl2
0.0061
N-palmitoyl-phosphatidylethanolamine
-
mutant C255S, 37°C, pH 7.4, presence of 10 mM MgCl2
0.008
N-palmitoyl-phosphatidylethanolamine
-
pH 7.5, 37°C, in presence of Cacl2
0.0143
N-palmitoyl-phosphatidylethanolamine
-
mutant C224S, 37°C, pH 7.4, presence of 10 mM MgCl2
0.0211
N-palmitoyl-phosphatidylethanolamine
-
mutant H331N, 37°C, pH 7.4, presence of 10 mM MgCl2
0.045
N-palmitoyl-phosphatidylethanolamine
-
pH 7.5, 37°C, in presence of Triton X-100
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.08
phosphatidylcholine
-
N-terminally truncated enzyme PLD1, stimulated by PKCalpha
0.1
phosphatidylcholine
-
N-terminally truncated enzyme PLD1, stimulated by Cdc42
0.1
phosphatidylcholine
-
N-terminally truncated enzyme PLD1, stimulated by PKCalpha + Rac1
0.1
phosphatidylcholine
-
N-terminally truncated enzyme PLD1, stimulated by PKCalpha + RhoA
0.117
phosphatidylcholine
-
N-terminally truncated enzyme PLD1, stimulated by PKCalpha + Cdc42
0.13
phosphatidylcholine
-
N-terminally truncated enzyme PLD1, stimulated by Rac1
0.17
phosphatidylcholine
-
N-terminally truncated enzyme PLD1, stimulated by RhoA
0.37
phosphatidylcholine
-
N-terminally truncated enzyme PLD1, stimulated by Arf-1
0.37
phosphatidylcholine
-
N-terminally truncated enzyme PLD1, stimulated by Arf-1 + Cdc42
0.37
phosphatidylcholine
-
N-terminally truncated enzyme PLD1, stimulated by Arf-1 + Rac1
0.43
phosphatidylcholine
-
N-terminally truncated enzyme PLD1, stimulated by Arf1 + PKCalpha
0.45
phosphatidylcholine
-
N-terminally truncated enzyme PLD1, stimulated by Arf1 + RhoA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.016
-
37°C, pH 7.4, presence of 10 mM MgCl2, substrate N-palmitoyl-phosphatidylethanolamine
2.4
-
37°C, pH 7.4, presence of 10 mM MgCl2, substrate N-lauroyl-phosphatidylethanolamine
additional information
-
quantification of transphosphatidylation activity of PLD in glial cells, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
stimulation of RBL-2H3 cells with ionimycin triggers phospholipase D2 translocation from plasma membrane to intracellular compartments and the release of exosomes
additional information
-
pattern of PLD1 amd PLD2 isozyme expression during development of the rat heart, overview
-
embryonic. PLD2 immunoreactivity is first observed in the chotoid plexus and in the most ventricular zone of the lateral and third ventricles at embryonic day 15, followed by gradual restriction to the limited zone of the ventricles at embryonic day 20. PLD2 expression is high in the developing cerebral cortex and hippocampus. In der cortex, PLD2 expression is observed in the marginal zone from the earliest stage and then declines and completely disappears by embryonic day 20
-
based on immunohistochemistry, PLD is detected in some neurons and glial cells in the cerebrum
-
the level of PLD2 in both the cerebrum and hindbrain is minimal compared to that of PLD1
-
Western blot analysis of PLD in the cerebrum shows that PLD1, a major PLD isoform in the brain, is detected weakly in the cerebrum at day 17 embryonic stage and its levels gradually increase until postnatal day 35 and remain unaltered thereafter
-
development of phospholipase D activity during ageing. Enzyme activity is identical in adult and aged nuclear fraction, increases by 25% from adult to aged cerebellum in mitochondrial-synaptosomal fraction, decreases by 18% from adult to aged cerebellum in the microsomal fraction and increases by 14% from adult to aged cerebellum in cytosolic fraction
-
PLD2 expression is observed in the marginal zone from the earliest stage and then declines and completely disappears by embryonic day 20
-
transient PLD1 expression during heart development in embryos, PLD1 levels increase at 0 and 3 days postpartum, and decline gradually beginning 7 days after birth, immunohistochemic analysis, overview
-
based on immunohistochemistry in the hindbrain PLD is found in some Purkinje cells and some cells of the molecular layer,as well as glial cells
-
in the hindbrain, comprising the cerebellum and pons, the peak level of PLD1 is detected at 21 days postnatally and declines progressively thereafter
-
the level of PLD2 in both the cerebrum and hindbrain is minimal compared to that of PLD1
-
myogenic cell. Prolonged elevation of PLD activity is required for myogenic differentiation. Low concentrations of the phorbol ester 12-O-tetradecanoylphorbol 13-acetate, cause a sustained increase in phospholipase D activity and bring myoblast to complete differentiation
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
using a GFP-PLD1 fusion protein PLD1 localizes intensely to intracellular vesicular compartments in the cell bodies and at zones along the edge of the large lamellipodia
-
stimulation of RBL-2H3 cells with ionimycin triggers phospholipase D2 translocation from plasma membrane to intracellular compartments and the release of exosomes. PLD2 is enriched on exosomes and its activity is correlated to the release of exosomes
-
-
phosphorylation of cofilin on Ser3 by LIM-kinase 1 correlates with a relocalisation of PLD1 from a predominantly intracellular localisation to the plasma membrane
using a GFP-PLD2 fusion protein PLD2 is localized to the protruding regions of lamellipodia in migrating cells
additional information
-
PLD-1, about 80% of total activity, PLD-2, about 20% of total acttivity
-
interaction of the PLD1 PX domain with phosphatidylinositol 3,4,5-trisphosphate and/or phosphatidic acid (or phosphatidylserine) may be an important factor in the spatiotemporal regulation and activation of PLD1
-
stimulation of RBL-2H3 cells with ionimycin triggers phospholipase D2 translocation from plasma membrane to intracellular compartments and the release of exosomes
-
phosphorylation of cofilin on Ser3 by LIM-kinase 1 correlates with a relocalisation of PLD1 from a predominantly intracellular localisation to the plasma membrane
additional information
-
immunochemicla study on intracellular localization
-
additional information
-
enzyme activity is identical in adult and aged nuclear fraction, increases by 25% from adult to aged cerebellum in mitochondrial-synaptosomal fraction, decreases by 18% from adult to aged cerebellum in the microsomal fraction and increases by 14% from adult to aged cerebellum in cytosolic fraction
-
additional information
-
ativation of mGluR1 leads to phospholipase D1 translocation in granule cells, activation of mGluR1 triggers migration and thus activation of PLD1 in a cell-specific manner in the cerebellum
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
-
the regulation of PLD activity by phosphoinositides, particularly by PtdIns(4,5)P2 provides a link with a number of proteins known to regulate cytoskeletal changes associated with adhesion and migration of cells, while this is also apparent when the additional PLD regulators, in particular the small GTPases, are considered
metabolism
-
identification of a signaling pathway for PLD in the lacrimal gland with Rho and ROCK1 activating PLD1, but not PLD2, in response to cholinergic agonists causing their association with one another. Formation of this signaling complex results in the downstream activation of MEK and ERK, but the activation is independent of the signaling molecules Ras, Raf, Pyk2, and cSrc, which usually activate ERK. Activation of ERK then attenuates cholinergic agonist-stimulated protein secretion. The muscarinic activation of PLD1 attenuates protein secretion by activating ERK
physiological function
-
different PLD isozymes are likely to serve diverse functions in membrane trafficking, endocytosis, exocytosis, cell growth, differentiation and actin cytoskeletal organization. Regulatory function of PLD, detailed overview. Phospholipase D signalling is involved in neurite outgrowth
physiological function
-
key role for phospholipase D in the generation of the slow excitatory postsynaptic current in cerebellar Purkinje cells
physiological function
-
PLD mediates amyloid beta peptides endocytosis into glial cells, and ERK1/2 phosphorylation by a formyl-peptid-receptor-like 1, FPRL1, agonists in glial cells
physiological function
-
PLD2 plays the role of master regulator and in an ill-defined manner regulates Rho function, PLD1 activity is downstream of this activation, however the generated phosphatidic acid controls changes in cytoskeletal organisation through its regulation of phosphatidylinositol-4-phosphate-5-kinase activity, overview. Regulatory mechanisms of PLD1 and PLD2 cellular activities, overview
physiological function
-
roles of phospholipase D in epidermal growth factor receptor, EGFR, signaling, modelling, overview. Coordination of EGF signaling by the PX domain of PLD, detailed overview. PLD is a key mediator of EGFR function, and can be directly regulated by upstream binding partners in an EGF-dependent manner
physiological function
-
the PLD1 protein in the heart is strongly associated with the early postnatal development of the heart in rats. Isozyme PLD1, but not PLD2, is the major PLD isozyme involved in the natal and postnatal development of the rat heart
physiological function
-
vesicular trafficking such as macropinocytosis is a dynamic process that requires coordinated interactions between specialized proteins and lipids that involves PLD and its physiological activator, the fission protein CtBP1/BARS in agonist-induced macropinocytosis, overview. Molecular mechanisms of lipid remodelling regulation during macropinocytosis. PLD-catalysed PtdOH formation may be necessary for EGF-induced macropinocytosis
physiological function
-
phospholipase D is involved in myogenesis, process modelling with PLD requirement for cell differentiation. PLD is required for S6K1 phosphorylation both the long (p85) and short (p70) S6K1 isoforms are phosphorylated in a PLD1-dependent way, vasopressin stimulation also induces phosphorylation of Akt on Ser-473 through PLD1-dependent activation of mTORC2 complex. Under differentiating conditions, mTORC2 and Akt are activated in a PLD-dependent way. Regulation of mTOR by PLD and myogenic differentiation, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PLD1_RAT
1074
0
123814
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
except for PLD2c, all PLD1 and PLD2 isozymes contain the catalytic core regions comprised of highly conserved domain I-IV. In domains II and IV, the enzymes contain two HxKxxxxD sequences designated HKD motifs, which are essential for enzymatic catalysis
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
depletion of both PLD1 and PLD2 isoenzymes using shRNA reduces the velocity of the migration, but depletion of PLD2 inhibits motility more severly than that of PLD1
additional information
depletion of both PLD1 and PLD2 isoenzymes using shRNA reduces the velocity of the migration, but depletion of PLD2 inhibits motility more severly than that of PLD1
additional information
depletion of both PLD1 and PLD2 isoenzymes using shRNA reduces the velocity of the migration, but depletion of PLD2 inhibits motility more severly than that of PLD1
additional information
depletion of both PLD1 and PLD2 isoenzymes using shRNA reduces the velocity of the migration, but depletion of PLD2 inhibits motility more severly than that of PLD1
additional information
-
the inhibition of EGF-induced macropinocytosis caused either by PLD1 or PLD2 knockdown is rescued by the co-expression of the respective wild-type PLD isoforms, whereas the expression of a lipase inactive mutant, lipase-negative (LN)-PLD1 or LN-PLD2, does not restore macropinocytotic activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60 - 80
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable, one cycle of freezing and thawing causes loss of up to 50% of enzymic activity. Addition of 1% w/v octyl glucoside improves stability
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
full-length enzyme and N-terminally truncated enzyme PLD1 expressed as a maltose binding domain fusion protein
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expression of the respective wild-type PLD isoforms or lipase-negative (LN)-PLD1 or LN-PLD2inactive mutants in PLD1 or PLD2 KO mutant cells, respectively
-
full-length enzyme and N-terminally truncated enzyme PLD1 expressed as a maltose binding domain fusion protein
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
enzyme activity in thymocytes is negatively correlated to their proliferative response fatty acids
molecular biology
molecular biology
-
functional roles of CYP1A2 and CYP2E1 can be switched by interaction with a specific anionic lysophospholipid in vivo
molecular biology
-
PLD may differentially play a role in the course of early development of the brain, with special reference to the cerebrum and hindbrain, in rats
molecular biology
-
PLD may differentially play a role in the course of early development of the brain, with special reference to the cerebrum and hindbrain,in rats
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Taki, T.; Kanfer, J.N.
Phospholipase D from rat brain
Methods Enzymol.
71
746-750
1981
Rattus norvegicus
Taki, T.; Kanfer, J.N.
Partial purification and properties of a rat brain phospholipase
J. Biol. Chem.
254
9761-9765
1979
Rattus norvegicus
Pappan, K.; Wang, X.
Molecular and biochemical properties and physiological roles of plant phospholipase D
Biochim. Biophys. Acta
1439
151-166
1999
Arabidopsis sp., Brassica oleracea, Saccharomyces cerevisiae, Ricinus communis, Catharanthus roseus, Homo sapiens, Mus musculus, Oryza sativa, Spuriopimpinella brachycarpa, Rattus norvegicus, Zea mays, Vigna unguiculata (O04865), Nicotiana tabacum (P93400)
Min, D.S.; Park, S.K.; Exton, J.H.
Characterization of a rat brain phospholipase D isozyme
J. Biol. Chem.
273
7044-7051
1998
Rattus norvegicus
Ueda, N.; Liu, Q.; Yamanaka, K.
Marked activation of the N-acylphosphatidylethanolamine-hydrolyzing phosphodiesterase by divalent cations
Biochim. Biophys. Acta
1532
121-127
2001
Rattus norvegicus
Freyberg, Z.; Bourgoin, S.; Shields, D.
Phospholipase D2 is localized to the rims of the Golgi apparatus in mammalian cells
Mol. Biol. Cell
13
3930-3942
2002
Rattus norvegicus
Devlin, M.A.; Das, S.; Singh, I.; Bourgoin, S.; Brindley, D.N.; Ginsberg, J.
The characterization of phospholipase D in FRTL-5 thyroid cells
Mol. Cell. Endocrinol.
167
107-115
2000
Rattus norvegicus
Lu, Y.B.; Wu, M.; Zhou, H.L.
Changes of phospholipase D activity of rat peritoneal mast cells in degranulation
Acta Pharmacol. Sin.
25
104-109
2004
Rattus norvegicus
Kam, Y.; Exton, J.H.
Role of phospholipase D in the activation of protein kinase D by lysophosphatidic acid
Biochem. Biophys. Res. Commun.
315
139-143
2004
Rattus norvegicus
Kuan, Y.H.; Lin, R.H.; Tsao, L.T.; Chen, Y.L.; Tzeng, C.C.; Wang, J.P.
Inhibition of phospholipase D activation by CYL-26z in formyl peptide-stimulated neutrophils involves the blockade of RhoA activation
Biochem. Pharmacol.
70
901-910
2005
Rattus norvegicus
Kim, D.S.; Yoon, M.S.; Kim, T.W.; Han, J.S.
Thyrotropin-releasing hormone increases phospholipase D activity through stimulation of protein kinase C in GH3 cells
Endocrine
23
33-38
2004
Rattus norvegicus
Kam, Y.; Exton, J.H.
Role of phospholipase D1 in the regulation of mTOR activity by lysophosphatidic acid
FASEB J.
18
311-319
2004
Rattus norvegicus
Laulagnier, K.; Grand, D.; Dujardin, A.; Hamdi, S.; Vincent-Schneider, H.; Lankar, D.; Salles, J.P.; Bonnerot, C.; Perret, B.; Record, M.
PLD2 is enriched on exosomes and its activity is correlated to the release of exosomes
FEBS Lett.
572
11-14
2004
Rattus norvegicus
Komati, H.; Minasi, A.; Naro, F.; Lagarde, M.; Prigent, A.F.; Adamo, S.; Nemoz, G.
Phorbol ester-induced differentiation of L6 myogenic cells involves phospholipase D activation
FEBS Lett.
577
409-414
2004
Rattus norvegicus
Lee, H.Y.; Park, J.B.; Jang, I.H.; Chae, Y.C.; Kim, J.H.; Kim, I.S.; Suh, P.G.; Ryu, S.H.
Munc-18-1 inhibits phospholipase D activity by direct interaction in an epidermal growth factor-reversible manner
J. Biol. Chem.
279
16339-16348
2004
Homo sapiens, Rattus norvegicus
Stahelin, R.V.; Ananthanarayanan, B.; Blatner, N.R.; Singh, S.; Bruzik, K.S.; Murray, D.; Cho, W.
Mechanism of membrane binding of the phospholipase D1 PX domain
J. Biol. Chem.
279
54918-54926
2004
Rattus norvegicus
Henage, L.G.; Exton, J.H.; Brown, H.A.
Kinetic analysis of a mammalian phospholipase D: Allosteric modulation by monomeric GTPases, protein kinase C, and polyphosphoinositides
J. Biol. Chem.
281
3408-3417
2006
Rattus norvegicus
Weismller, T.; Klein, J.; Lffelholz, K.
Effects of norepinephrine and cardiotrophin-1 on phospholipase D activity and incorporation of myristic acid into phosphatidylcholine in rat heart
J. Pharm. Sci.
95
335-340
2004
Rattus norvegicus
Ahn, E.K.; Lim, O.K.; Nam, H.Y.; Kim, H.J.; Chung, N.; Bae, G.N.; Lim, Y.
Silica induced phospholipase D (PLD) activation in Rat2 fibroblasts
J. Toxicol. Public Health
21
291-295
2005
Rattus norvegicus
-
Ueda, N.; Okamoto, Y.; Morishita, J.
N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: a novel enzyme of the beta-lactamase fold family releasing anandamide and other N-acylethanolamines
Life Sci.
77
1750-1758
2005
Rattus norvegicus
Pasquare, S.J.; Salvador, G.A.; Giusto, N.M.
Phospholipase D and phosphatidate phosphohydrolase activities in rat cerebellum during aging
Lipids
39
553-560
2004
Rattus norvegicus
Singh, A.T.K.; Frohman, M.A.; Stern, P.H.
Parathyroid hormone stimulates phosphatidylethanolamine hydrolysis by phospholipase D in osteoblastic cells
Lipids
40
1135-1140
2005
Rattus norvegicus
Mateos, M.V.; Uranga, R.M.; Salvador, G.A.; Giusto, N.M.
Coexistence of phosphatidylcholine-specific phospholipase C and phospholipase D activities in rat cerebral cortex synaptosomes
Lipids
41
273-280
2006
Rattus norvegicus
Komati, H.; Naro, F.; Mebarek, S.; de Arcangelis, V.; Adamo, S.; Lagarde, M.; Prigent, A.F.; Nemoz, G.
Phospholipase D is involved in myogenic differentiation though remodeling of actin cytoskeleton
Mol. Biol. Cell
16
1232-1244
2005
Rattus norvegicus
Hui, L.; Abbas, T.; Pielak, R.M.; Joseph, T.; bargonetti, J.; Foster, D.A.
Phospholipase D elevates the level of MDM2 and suppresses DNA damage-induced increase in p53
Mol. Cell. Biol.
24
5677-5686
2004
Rattus norvegicus
Choi, J.S.; Park, H.J.; Jo, Y.C.; Chun, M.H.; Chung, J.W.; Kim, J.M.; Min, D.S.; Lee, M.Y.
Immunohistochemical localization of phospholipase D2 in embryonic rat brain
Neurosci. Lett.
357
147-151
2004
Rattus norvegicus
Benitez-Rajal, J.; Lorite, M.J.; Burt, A.D.; Day, C.P.; Thompson, M.G.
Phospholipase D and extracellular signal-regulated kinase in hepatic stellate cells: effects of platelet-derived growth factor and extracellular nucleotides
Am. J. Physiol. Gastrointest. Liver Physiol.
291
G977-G986
2006
Rattus norvegicus
Wang, J.; Okamoto, Y.; Morishita, J.; Tsuboi, K.; Miyatake, A.; Ueda, N.
Functional analysis of the purified anandamide-generating phospholipase D as a member of the metallo-beta-lactamase family
J. Biol. Chem.
281
12325-12335
2006
Homo sapiens, Rattus norvegicus
Benzaria, A.; Meskini, N.; Dubois, M.; Nemoz, G.; Lagarde, M.; Prigent, A.F.
Phospholipase D as a potential target for the antiproliferative effects of polyunsaturated fatty acids in rat thymocytes
J. Nutr. Biochem.
18
228-235
2007
Rattus norvegicus
Kim, M.; Moon, C.; Kim, H.; Shin, M.K.; Min, D.S.; Shin, T.
Developmental levels of phospholipase D isozymes in the brain of developing rats
Acta Histochem.
112
81-91
2010
Rattus norvegicus
Cho, E.Y.; Yun, C.H.; Chae, H.Z.; Chae, H.J.; Ahn, T.
Lysophosphatidylserine-induced functional switch of human cytochrome P450 1A2 and 2E1 from monooxygenase to phospholipase D
Biochem. Biophys. Res. Commun.
376
584-589
2008
Homo sapiens, Rattus norvegicus
Nagasaki, A.; Inotsume, K.; Kanada, M.; Uyeda, T.Q.
Phospholipase D is essential for keratocyte-like migration of NBT-II cells
Cell Struct. Funct.
33
27-33
2008
Rattus norvegicus (P70496), Rattus norvegicus (P70498)
Rudge, S.A.; Wakelam, M.J.
Inter-regulatory dynamics of phospholipase D and the actin cytoskeleton
Biochim. Biophys. Acta
1791
856-861
2009
Homo sapiens, Mus musculus, Rattus norvegicus, Streptomyces chromofuscus
Lee, C.S.; Kim, K.L.; Jang, J.H.; Choi, Y.S.; Suh, P.G.; Ryu, S.H.
The roles of phospholipase D in EGFR signaling
Biochim. Biophys. Acta
1791
862-868
2009
Bos taurus, Cricetulus griseus, Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus
Kanaho, Y.; Funakoshi, Y.; Hasegawa, H.
Phospholipase D signalling and its involvement in neurite outgrowth
Biochim. Biophys. Acta
1791
898-904
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Haga, Y.; Miwa, N.; Jahangeer, S.; Okada, T.; Nakamura, S.
CtBP1/BARS is an activator of phospholipase D1 necessary for agonist-induced macropinocytosis
EMBO J.
28
1197-1207
2009
Rattus norvegicus
Glitsch, M.D.
Activation of native TRPC3 cation channels by phospholipase D
FASEB J.
24
318-325
2010
Rattus norvegicus
Moon, C.; Kim, H.; Kim, S.; Lee, Y.; Shin, M.K.; Min, d.o..S.; Shin, T.
Transient expression of phospholipase D1 during heart development in rats
J. Vet. Med. Sci.
70
411-413
2008
Rattus norvegicus
Brandenburg, L.O.; Konrad, M.; Wruck, C.; Koch, T.; Pufe, T.; Lucius, R.
Involvement of formyl-peptide-receptor-like-1 and phospholipase D in the internalization and signal transduction of amyloid beta 1-42 in glial cells
Neuroscience
156
266-276
2008
Rattus norvegicus
Hodges, R.R.; Guilbert, E.; Shatos, M.A.; Natarajan, V.; Dartt, D.A.
Phospholipase D1, but not D2, regulates protein secretion via Rho/ROCK in a Ras/Raf-independent, MEK-dependent manner in rat lacrimal gland
Invest. Ophthalmol. Vis. Sci.
52
2199-2210
2011
Rattus norvegicus
EXTERNAL LINKS (specific for EC-Number 3.1.4.4)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
