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Phospholipase D2

PLD2, phospholipase D2
The protein encoded by this gene catalyzes the hydrolysis of phosphatidylcholine to phosphatidic acid and choline. The activity of the encoded enzyme is enhanced by phosphatidylinositol 4,5-bisphosphate and ADP-ribosylation factor-1. This protein localizes to the peripheral membrane and may be involved in cytoskeletal organization, cell cycle control, transcriptional regulation, and/or regulated secretion. Two transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Jul 2011] (from NCBI)
Top mentioned proteins: phospholipase D, ACID, V1a, CAN, Inactive
Papers using PLD2 antibodies
Microglia acquire distinct activation profiles depending on the degree of alpha-synuclein neuropathology in a rAAV based model of Parkinson's disease
Combs Colin K et al., In Journal of Neuroinflammation, 2009
... Anti-PLD1 and PLD2 antibodies were purchased from Abcam (Cambridge, MA) ...
Essential role of BCL9-2 in the switch between beta-catenin's adhesive and transcriptional functions.
Agarwal Sudha, In PLoS ONE, 2003
... PLD1 and PLD2 selective inhibitors were purchased from Cayman chemical ...
Papers on PLD2
Gomez-Cambronero et al., Boston, United States. In Mol Cell Biol, Feb 2016
We provide direct evidence for a feedback loop, where PLD induction upon starvation leads to PA, which induces expression of miRNAs that in turn inhibits PLD2 translation.
RhoA mediates the expression of acidic extracellular pH-induced matrix metalloproteinase-9 mRNA through phospholipase D1 in mouse metastatic B16-BL6 melanoma cells.
Kato et al., Kōriyama, Japan. In Int J Oncol, Feb 2016
In contrast, PLD2 inhibition or knockout had no effect on MMP-9 expression.
The transcription factors Slug (SNAI2) and Snail (SNAI1) regulate phospholipase D (PLD) promoter in opposite ways towards cancer cell invasion.
Gomez-Cambronero et al., Dayton, United States. In Mol Oncol, Jan 2016
We found that the activity of phospholipase D isoform 2 (PLD2) is highly increased in cancers with larger size and poor prognosis (MDA-MB-231 versus MCF-7 cells), so we determined if Snail or Slug were responsible for PLD2 gene transcription regulation.
Regulation of protein kinase CK2 catalytic activity by protein kinase C and phospholipase D2.
Bae et al., Taegu, South Korea. In Biochimie, Jan 2016
UNASSIGNED: We have previously demonstrated that phospholipase D2 (PLD2) overexpression antagonizes protein kinase CK2 (CK2) inhibition-mediated cellular senescence.
Accumulating insights into the role of phospholipase D2 in human diseases.
Ryu et al., South Korea. In Adv Biol Regul, Jan 2016
UNASSIGNED: Phospholipase D2 (PLD2) is a lipid-signaling enzyme that produces the signaling molecule phosphatidic acid (PA) by catalyzing the hydrolysis of phosphatidylcholine (PC).
MicroRNA-203 Modulates the Radiation Sensitivity of Human Malignant Glioma Cells.
Kim et al., Seoul, South Korea. In Int J Radiat Oncol Biol Phys, Nov 2015
Western blot analysis validated the fact that miR-203 downregulated ATM, RAD51, SRC, PLD2, PI3K-AKT, JAK-STAT3, VEGF, HIF-1α, and MMP2.
Syntenin and syndecan in the biogenesis of exosomes.
Zimmermann et al., Marseille, France. In Biol Cell, Oct 2015
SDC-syntenin-associated regulators include the endosomal sorting complex required for transport accessory component ALG-2-interacting protein X, the small GTPase adenosine 5'-diphosphate-ribosylation factor 6, the lipid-modifying enzyme phospholipase D2 and the endoglycosidase heparanase.
The phospholipase D superfamily as therapeutic targets.
Frohman, Stony Brook, United States. In Trends Pharmacol Sci, Mar 2015
With the advent of loss-of-function genetic mouse models that have revealed that PLD1 and PLD2 ablation is overtly tolerable, small-molecule PLD1/2 inhibitors that do not cause unacceptable clinical toxicity, a PLD2 polymorphism that has been linked to altered physiology, and growing delineation of processes that are subtly altered in mice lacking PLD1/2 activity, the stage is being set for assessment of PLD1/2 inhibition for therapeutic purposes.
Phospholipase D in cell signaling: from a myriad of cell functions to cancer growth and metastasis.
Gomez-Cambronero, Dayton, United States. In J Biol Chem, 2014
The particular involvement of PLD in cell migration is accomplished: (a) through the actions of its enzymatic product of reaction, phosphatidic acid, and its unique shape-binding role on membrane geometry; (b) through a particular guanine nucleotide exchange factor (GEF) activity (the first of its class assigned to a phospholipase) in the case of the mammalian isoform PLD2; and (c) through protein-protein interactions with a wide network of molecules: Wiskott-Aldrich syndrome protein (WASp), Grb2, ribosomal S6 kinase (S6K), and Rac2.
A Next generation PLD2 inhibitor with improved physiochemical properties and DMPK profile for translational in vivo
Lindsley et al., Bethesda, United States. In Unknown Journal, 2014
Further chemical optimization of our first generation phospholipase D2 (PLD2) probe (ML298) afforded ML395 (CID 73099363), a potent, >80-fold PLD2 selective allosteric inhibitor (cellular PLD1, IC50 >30,000 nM, cellular PLD2, IC50 = 360 nM).
Overexpression of phospholipase D enhances Bcl-2 expression by activating STAT3 through independent activation of ERK and p38MAPK in HeLa cells.
Han et al., Seoul, South Korea. In Biochim Biophys Acta, 2012
PLD acts as an important regulator in Bcl-2 expression by activating STAT3 involving the phosphorylation of Ser727 through the PLA(2)/G(i)/ERK1/2, RhoA/ROCK/p38 MAPK, and Rac1/p38 MAPK pathways.
Phospholipase D2: a pivotal player modulating RBL-2H3 mast cell structure.
Oliver et al., Ribeirão Preto, Brazil. In J Histochem Cytochem, 2012
Phosphatidic acid produced by PLD2 plays an important role in regulating cell morphology in mast cells.
Phospholipase D2 (PLD2) shortens the time required for myeloid leukemic cell differentiation: mechanism of action.
Gomez-Cambronero et al., Dayton, United States. In J Biol Chem, 2012
how PLD2 participates in cell differentiation
Phospholipase D2 (PLD2) is a guanine nucleotide exchange factor (GEF) for the GTPase Rac2.
Gomez-Cambronero et al., Dayton, United States. In Proc Natl Acad Sci U S A, 2012
Data show that the Phospholipase D2 (PLD2)-GTPase Rac2 protein-protein interaction is sufficient for the guanine nucleotide exchange factor (GEF) function.
The C-terminal domain of PLD2 participates in degradation of protein kinase CKII β subunit in human colorectal carcinoma cells.
Bae et al., Taegu, South Korea. In Bmb Rep, 2011
the C-terminal domain of PLD2 can regulate Casein Kinase II by accelerating Casein Kinase II beta degradation.
A new role for cyclic phosphatidic acid as a PPARgamma antagonist.
Glass et al., San Diego, United States. In Cell Metab, 2010
A recent study in Molecular Cell (Tsukahara et al., 2010) identifies cyclic phosphatidic acid (CPA) as a naturally occurring PPARgamma antagonist that can be generated from lysophospholipids by signal-dependent activation of phospholipase D2.
A role for phosphatidic acid in COPI vesicle fission yields insights into Golgi maintenance.
Hsu et al., Boston, United States. In Nat Cell Biol, 2008
This finding has allowed us to further delineate COPI vesicle fission into two sub-stages: 1) an earlier stage of bud-neck constriction, in which BARS and other COPI components are required, and 2) a later stage of bud-neck scission, in which phosphatidic acid generated by phospholipase D2 (PLD2) is also required.
The lymphocyte function-associated antigen-1 receptor costimulates plasma membrane Ras via phospholipase D2.
Philips et al., New York City, United States. In Nat Cell Biol, 2007
Thus, LFA-1 acts through PLD2 to reshape the pattern of Ras activation downstream of the TCR
Phospholipase D2-generated phosphatidic acid couples EGFR stimulation to Ras activation by Sos.
Bar-Sagi et al., Stony Brook, United States. In Nat Cell Biol, 2007
Our findings establish a crucial role for PLD2 in the coupling of extracellular signals to Sos-mediated Ras activation, and provide new insights into the spatial coordination of this activation event.
The phox homology domain of phospholipase D activates dynamin GTPase activity and accelerates EGFR endocytosis.
Ryu et al., South Korea. In Nat Cell Biol, 2006
PLD functions as a GTPase activating protein (GAP) through its phox homology domain (PX), which directly activates the GTPase domain of dynamin and increased epidermal growth factor receptor (EGFR) endocytosis at physiological EGF concentrations.
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