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Information on EC 3.1.4.4 - phospholipase D and Organism(s) Mus musculus and UniProt Accession Q9Z280
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3.1.4.4 phospholipase DIUBMB Comments
Also acts on other phosphatidyl esters.
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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: Mus musculus
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 D1 PHOX and PX containing domain
-
-
-
-
Phospholipase D2 PHOX and PX containing domain
-
-
-
-
PLD
PLD delta
-
-
-
-
PLD epsilon
-
-
-
-
PLD zeta
-
-
-
-
PLD1C
-
-
-
-
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
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
hydrolysis of phosphatidylcholine by phospholipase D leads to the generation of phosphatidic acid, PA, which is itself a source of diacylglycerol. PLD2 emerges as an early player upstream of the Ras-MAPK-IL-2 pathway in T-cells via PA and DAG production
-
-
?
additional information
?
-
-
down-regulation of melanogenesis is mediated by phospholipase D2 but not by phospholipase D1 through turbiquitin proteasome-mediated degradation of tyrosinase. PLD2 may play an important role in regulating pigmentation in vivo
-
-
?
additional information
?
-
-
essential role for phospholipase D in activation of protein kinase C and degranulation in mast cells. Production of phosphatidic acid by PLD facilitates activation of protein kinase C and, in turn, degranulation, although additional PLD-dependent processes appear to be critical for antigen-mediated degranulation
-
-
?
additional information
?
-
-
mechanical stimuli activate mTOR (mammalian target of rapamycin) signaling through a phospholipase D-dependent increase in phosphatidic acid
-
-
?
additional information
?
-
-
PLD might be implicated in core protein-induced transformation
-
-
?
additional information
?
-
-
sphingosine significantly stimulates phospholipase D activity in mouse C2c12 myoblasts via phosphorylation to sphingosine 1-phosphate
-
-
?
additional information
?
-
-
survival signals generated by PLD attenuate expression of Egr-1 by activation of phosphatidylinositol 3-kinase signaling pathway and induction of PTEN by early growth response-1, which confers resistance to apoptosis
-
-
?
additional information
?
-
-
the PLD2 PX domain enables PLD1 to mediate signal transduction via ERK1/2 by providing a direct binding site for phosphatidylinositol 3,4,5-triphosphate and by activating PLD1
-
-
?
additional information
?
-
-
mechanical stimuli activate signaling by mTOR, i.e. mammalian target of rapamycin, in skeletal muscle through an enzyme-dependent increase in phosphatidic acid
-
-
?
additional information
?
-
-
PLD also performs transphosphatidylation using 1-butanol as phosphatidyl acceptor
-
-
?
additional information
?
-
-
PLD2 is regulated by phosphorylation-dephosphorylation, detailed overview
-
-
?
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 1-butanol as phosphatidyl acceptor leading to formation of phosphatidylbutan-1-ol
-
-
?
additional information
?
-
-
the catalytic activity of PLD is not required for PLD-mediated CKII inhibition, possible inhibition mechanism, overview
-
-
?
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
phospholipid + H2O
phosphatidic acid + alcohol
-
phosphoric ester hydrolysis
-
-
?
phosphatidylcholine + H2O
choline + phosphatidic acid
-
hydrolysis of phosphatidylcholine by phospholipase D leads to the generation of phosphatidic acid, PA, which is itself a source of diacylglycerol. PLD2 emerges as an early player upstream of the Ras-MAPK-IL-2 pathway in T-cells via PA and DAG production
-
-
?
additional information
?
-
-
down-regulation of melanogenesis is mediated by phospholipase D2 but not by phospholipase D1 through turbiquitin proteasome-mediated degradation of tyrosinase. PLD2 may play an important role in regulating pigmentation in vivo
-
-
?
additional information
?
-
-
essential role for phospholipase D in activation of protein kinase C and degranulation in mast cells. Production of phosphatidic acid by PLD facilitates activation of protein kinase C and, in turn, degranulation, although additional PLD-dependent processes appear to be critical for antigen-mediated degranulation
-
-
?
additional information
?
-
-
mechanical stimuli activate mTOR (mammalian target of rapamycin) signaling through a phospholipase D-dependent increase in phosphatidic acid
-
-
?
additional information
?
-
-
PLD might be implicated in core protein-induced transformation
-
-
?
additional information
?
-
-
sphingosine significantly stimulates phospholipase D activity in mouse C2c12 myoblasts via phosphorylation to sphingosine 1-phosphate
-
-
?
additional information
?
-
-
survival signals generated by PLD attenuate expression of Egr-1 by activation of phosphatidylinositol 3-kinase signaling pathway and induction of PTEN by early growth response-1, which confers resistance to apoptosis
-
-
?
additional information
?
-
-
the PLD2 PX domain enables PLD1 to mediate signal transduction via ERK1/2 by providing a direct binding site for phosphatidylinositol 3,4,5-triphosphate and by activating PLD1
-
-
?
additional information
?
-
-
mechanical stimuli activate signaling by mTOR, i.e. mammalian target of rapamycin, in skeletal muscle through an enzyme-dependent increase in phosphatidic acid
-
-
?
additional information
?
-
-
PLD also performs transphosphatidylation using 1-butanol as phosphatidyl acceptor
-
-
?
additional information
?
-
-
PLD2 is regulated by phosphorylation-dephosphorylation, detailed overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,2-bis(2-aminophenoxy)-ethane-N,N,N',N'-tetraacetic acid tetrakis(acetoxymethyl) ester
-
i.e. BAPTA-AM, chelator of intracellular free calcium, application results in reduction of extracellular pH-induced enzyme activity
neomycin
-
inhibits the mechanically induced increase in phosphatidic acid in skeletal muscle
resveratrol
-
a phytoalexin with antiinflammatory activity in C5 anaphylatoxin-stimulated primary neutrophils and in a mouse model of acute peritonitis, blocks PLD activity and membrane recruitment
1-butanol
-
inhibits the mechanically induced increase in phosphatidic acid in skeletal muscle and mechanical activation of signaling by mTOR, i.e. mammalian target of rapamycin
1-butanol
-
1-butanol inhibits PLD2 and is potent in cancelling ERK1/2 activation
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
Cdc42
-
in addition to interactions with Rac and Rho, PLD1 is regulated by Cdc42
-
dynamin
-
a large GTPase, can interact with PLD in a GTP dependent manner in vitro
-
phosphatidylinositol 3,4,5-triphosphate
-
specifically interacts with the phox homology domain of phospholipase D1 and stimulates activity
Rho GTPases
-
PLD1 and PLD2 activity is regulated by the Rho family of small GTPases
-
serotonin
-
i.e. 5-hydroxytryptamine, 5-HT, activates PLD via the 5-HT 2A receptor, leading to the generation of phosphatidic acid that promotes smooth muscle cell proliferation through activations of mammalian target of rapamycin, mTOR, S6K1 and MAPK but not the Rho or PI3-kinase/Akt signaling pathways, overview. Activation is completely blocked by ketanserin
additional information
-
acidic extracellular pH induces enzyme activity both via Ca2+ influx and acidic shingomyelinase
-
additional information
-
mechanical stimulation of skeletal muscle with intermittent passive stretch ex vivo induces phospholipase D activation, phosphatidic acid accumulation, and signaling by mTOR, i.e. mammalian target of rapamycin
-
additional information
-
epidermal growth factor triggers the activation of PLD in various cell types, such as mouse embryo fibroblasts, MEFs, a mouse myoblast cell line, C2C12, and a mouse embryo fibroblast cell line Swiss 3T3
-
additional information
-
in some physiological settings, the PLD2 activity appears to be regulated by the classical MAP kinase, extracellular signal-regulated kinase pathway
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
of dentate gyrus. Strong mRNA signal, and intense immunosignal in axons of granule cell
-
isozymes PLD1 and PLD2 during postnatal development: moderate basal level of PLD1 in the lungs at postnatal 1 week, with a gradual increase occurring until week 4. The pattern of PLD2 parallels that of PLD1, although the quantity of PLD2 is markedly less, immunohistochemic analysis, overview
-
phospholipase D activity is elevated in hepatitis C virus core protein-transformed NIH3T3 mouse fibroblast cells
-
L´PLD1 and PLD2 are localized to the Z-band in the skeletal muscle, a critical site of mechanical force transmission
-
isoforms PLD1 and PLD2 are localized to the z-band of skeletal muscle
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
phosphorylation of cofilin on Ser3 by LIM-kinase 1 correlates with a relocalisation of PLD1 from a predominantly intracellular localisation to the plasma membrane
-
phosphorylation of cofilin on Ser3 by LIM-kinase 1 correlates with a relocalisation of PLD1 from a predominantly intracellular localisation to the plasma membrane
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
pretreatment of mouse neutrophils with PLD inhibitor resveratrol significantly blocks oxidative burst, leukocyte migration, degranulation, and inflammatory cytokine production involving inhibition of sphingosine kinase activity and ERK1/2 phosphorylation
metabolism
physiological function
metabolism
-
phosphatidic acid is a source of diacylglycerol, the two versatile lipid second messengers are at the centre of a phospholipid signalling network and as such are involved in several cellular functions
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
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
-
importance and activating role of PLD2 for LPS-induced NO synthesis in Raw 264.7 cells with involvement of the S6K1-p42/44 MAPK-STAT3 pathway. Binding of transcription factor STAT3 to the iNOS promoter is mediated by PLD2
physiological function
-
phospholipase D signaling is involved in serotonin-induced mitogenesis of pulmonary artery smooth muscle cells. PLD activation participates in the cellular proliferation response to serotonin
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
-
PLD2 promotes an early and sustained increase in ERK1/2 phosphorylation in recombinant T-cell lines, which is inhibited by 1-butanol.
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
-
isoforms PLD1 and PLD2 regulate different steps in mast cell degranulation. PLD1 deficiency impairs FcepsilonRI-mediated mast cell degranulation while PLD2 deficiency enhances it. PLD deficiency affects activation of the phosphoinositide 3-kinase pathway and RhoA. Although PLD1 deficiency impairs F-actin disassembly, PLD2 deficiency enhances microtubule formation
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_MOUSE
1074
0
123969
Swiss-Prot
other Location (Reliability: 3)
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
phosphoprotein
-
the enzymatic activity of phospholipase D2, PLD2, is regulated by phosphorylation-dephosphorylation with existence of activator and inhibitory sites, overview. Epidermal growth factor receptor, i.e. EGFR, JAK3, and Src with JAK3 phosphorylate an inhibitory Y296, an activator Y415, and an ambivalent Y511 site, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K758R
R179A
-
mutation disrupts binding of the activator phosphatidylinositol 3,4,5-triphosphate
R179K
-
mutation disrupts binding of the activator phosphatidylinositol 3,4,5-triphosphate
additional information
additional information
-
interleukin-2 production evoked by PMA/ionomycin stimulation or CD3/CD28 engagement is enhanced in the two T-cell lines overexpressing PLD2
additional information
-
overexpression of phospholipase D isozymes, leads to downregulation of protein kinase CKII activity via proteasome-dependent CKIIbeta degradation in NIH3T3 cells. Co-localization of CKIIbeta and PLD isozymes in NIH3T3 cells
additional information
-
transfection of PLD1, PLD2, and their dominant negative forms into Raw 264.7 cells, only PLD2 overexpression, but not that of PLD1, increases NO synthesis and iNOS expression. LPS-induced NO synthesis and iNOS expression are blocked by PLD2 siRNA, suggesting that LPS upregulates NO synthesis through PLD2. Knockdown of PLD2 with siRNA also decreases phosphorylation of S6K1, p42/44 MAPK and STAT3 induced by LPS
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of PLD1, PLD2, and their dominant negative forms into Raw 264.7 cells
-
overexpression of PLD2 in MCF-7 cells, in MTLn3 cells, or in COS-7 cells. In COS-7, cells that show the highest level of PLD2 activity, the Y415 is a prominent phosphorylation site, and JAK3 compensates the negative modulation by EGFR on phosphorylation site Y296. In MCF-7, cells that show the lowest level of PLD2 activity, the converse is the case, with phosphorylation site Y296 unable to compensate the positive modulation by phosphorylation site Y415. PLD2 activity is low in the breast cancer cell line MCF-7 because it is kept downregulated by tyrosyl phosphorylation of Y296 by EGFR kinase, overview
-
overexpression of wild-type and inactive mutant PLD2 in bovine pulmonary artery smooth muscle cells
-
stable expression of PLD2 in T hybridoma 2B4 cell line. Overexpression of a dominant negative PLD2 attenuates the early and sustained increase in ERK1/2 phosphorylation induced by PLD2, overview
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Meacci, E.; Cencetti, F.; Donati, C.; Nuti, F.; Becciolini, L.; Bruni, P.
Sphingosine kinase activity is required for sphingosine-mediated phospholipase D activation in C2C12 myoblasts
Biochem. J.
381
655-663
2004
Mus musculus
Kim, J.; Lee, Y.H.; Kwon, T.K.; Chang, J.S.; Chung, K.C.; Min, D.S.
Phospholipase D prevents etoposide-induced apoptosis by inhibiting the expression of early growth response-1 and phosphatase and tensin homologue deleted on chromosome 10
Cancer Res.
66
784-793
2006
Mus musculus
Kim, J.; Choi, B.H.; Jang, K.L.; Min do, S.
Phospholipase D activity is elevated in hepatitis C virus core protein-transformed NIH3T3 mouse fibroblast cells
Exp. Mol. Med.
36
454-460
2004
Mus musculus
Kageyama, A.; Oka, M.; Okada, T.; Nakamura, S.i.; Ueyama, T.; Saito, N.; Hearing, V.J.; Ichihashi, M.; Nishigori, C.
Down-regulation of melanogenesis by phospholipase D2 through ubiquitin proteasome-mediated degradation of tyrosinase
J. Biol. Chem.
279
27774-27780
2004
Mus musculus
Lee, J.S.; Kim, J.H.; Jang, I.H.; Kim, H.S.; Han, J.M.; Kazlauskas, A.; Yagisawa, H.; Suh, P.G.; Ryu, S.H.
Phosphatidylinositol (3,4,5)-triphosphate specifically interacts with the phox homology domain of phospholipase D1 and stimulates its activity
J. Cell Sci.
118
4405-4413
2005
Mus musculus
Peng, Z.; Beaven, M.A.
An essential role for phospholipase D in the activation of protein kinase C and degranulation in mast cells
J. Immunol.
174
5201-5208
2005
Mus musculus
Hornberger, T.A.; Chu, W.K.; mak, Y.W.; Hsiung, J.W.; Huang, S.A.; Chien, S.
The role of phospholipase D and phosphatidic acid in the mechanical activation of mTOR signaling in skeletal muscle
Proc. Natl. Acad. Sci. USA
103
4741-4746
2006
Mus musculus
Kim, H.; Lee, J.; Kim, S.; Shin, M.K.; Min, d.o.S.; Shin, T.
Differential expression of phospholipases D1 and D2 in mouse tissues
Cell Biol. Int.
31
148-155
2007
Mus musculus (P97813), Mus musculus (Q9Z280), Mus musculus
Kato, Y.; Ozawa, S.; Tsukuda, M.; Kubota, E.; Miyazaki, K.; St-Pierre, Y.; Hata, R.
Acidic extracellular pH increases calcium influx-triggered phospholipase D activity along with acidic sphingomyelinase activation to induce matrix metalloproteinase-9 expression in mouse metastatic melanoma
FEBS J.
274
3171-3183
2007
Mus musculus
Egertova, M.; Simon, G.M.; Cravatt, B.F.; Elphick, M.R.
Localization of N-acyl phosphatidylethanolamine phospholipase D (NAPE-PLD) expression in mouse brain: A new perspective on N-acylethanolamines as neural signaling molecules
J. Comp. Neurol.
506
604-615
2008
Mus musculus
Liu, Y.; Fanburg, B.L.
Phospholipase D signaling in serotonin-induced mitogenesis of pulmonary artery smooth muscle cells
Am. J. Physiol. Lung Cell Mol. Physiol.
295
L471-L478
2008
Homo sapiens, Mus musculus
Hamdi, S.M.; Cariven, C.; Coronas, S.; Malet, N.; Chap, H.; Perret, B.; Salles, J.P.; Record, M.
Potential role of phospholipase D2 in increasing interleukin-2 production by T-lymphocytes through activation of mitogen-activated protein kinases ERK1/ERK2
Biochim. Biophys. Acta
1781
263-269
2008
Homo sapiens, Mus musculus
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
Park, S.Y.; Cho, J.H.; Ma, W.; Choi, H.J.; Han, J.S.
Phospholipase D2 acts as an important regulator in LPS-induced nitric oxide synthesis in Raw 264.7 cells
Cell. Signal.
22
619-628
2010
Mus musculus
Issuree, P.D.; Pushparaj, P.N.; Pervaiz, S.; Melendez, A.J.
Resveratrol attenuates C5a-induced inflammatory responses in vitro and in vivo by inhibiting phospholipase D and sphingosine kinase activities
FASEB J.
23
2412-2424
2009
Homo sapiens, Mus musculus
Moon, C.; Jeong, J.; Shin, M.K.; Min, d.o..S.; Shin, T.
Expression of phospholipase D isozymes in mouse lungs during postnatal development
J. Vet. Med. Sci.
71
965-968
2009
Mus musculus
Henkels, K.M.; Peng, H.J.; Frondorf, K.; Gomez-Cambronero, J.
A comprehensive model that explains the regulation of phospholipase D2 activity by phosphorylation-dephosphorylation
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Mus musculus
Yoon, S.H.; Min, d.o..S.; Bae, Y.S.
Over-expression of phospholipase D isozymes down-regulates protein kinase CKII activity via proteasome-dependent CKIIbeta degradation in NIH3T3 cells
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Mus musculus
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