PLD2

From Wikipedia, the free encyclopedia

Phospholipase D2

Identifiers

External IDs

OMIM: 602384 MGI: 892877 HomoloGene: 55672

Gene ontology
Molecular Function:	• catalytic activity • phospholipase D activity • protein binding • hydrolase activity • phosphoinositide binding
Cellular Component:	• plasma membrane
Biological Process:	• G-protein coupled receptor internalization • receptor-mediated endocytosis • cytoskeleton organization and biogenesis • cell communication • small GTPase mediated signal transduction • metabolic process • lipid catabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002663 (mRNA)
NP_002654 (protein)

NM_008876 (mRNA)
NP_032902 (protein)

Location

Chr 17: 4.66 - 4.67 Mb

Chr 11: 70.36 - 70.37 Mb

Pubmed search

[1]

[2]

Phospholipase D2, also known as PLD2, is a human gene.

Phosphatidylcholine (PC)-specific phospholipases D (PLDs) catalyze the hydrolysis of PC to produce phosphatidic acid and choline. Activation of PC-specific PLDs occurs as a consequence of agonist stimulation of both tyrosine kinase and G protein-coupled receptors. PC-specific PLDs have been proposed to function in regulated secretion, cytoskeletal reorganization, transcriptional regulation, and cell cycle control.[supplied by OMIM]^[1]

[edit] References

^ Entrez Gene: PLD2 phospholipase D2.

[edit] Further reading

Sundaram M, Cook HW, Byers DM (2004). "The MARCKS family of phospholipid binding proteins: regulation of phospholipase D and other cellular components.". Biochem. Cell Biol. 82 (1): 191-200. doi:10.1139/o03-087. PMID 15052337.
McDermott M, Wakelam MJ, Morris AJ (2004). "Phospholipase D.". Biochem. Cell Biol. 82 (1): 225-53. doi:10.1139/o03-079. PMID 15052340.
Colley WC, Sung TC, Roll R, et al. (1997). "Phospholipase D2, a distinct phospholipase D isoform with novel regulatory properties that provokes cytoskeletal reorganization.". Curr. Biol. 7 (3): 191-201. PMID 9395408.
Lopez I, Arnold RS, Lambeth JD (1998). "Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2.". J. Biol. Chem. 273 (21): 12846-52. PMID 9582313.
Steed PM, Clark KL, Boyar WC, Lasala DJ (1998). "Characterization of human PLD2 and the analysis of PLD isoform splice variants.". FASEB J. 12 (13): 1309-17. PMID 9761774.
Slaaby R, Jensen T, Hansen HS, et al. (1999). "PLD2 complexes with the EGF receptor and undergoes tyrosine phosphorylation at a single site upon agonist stimulation.". J. Biol. Chem. 273 (50): 33722-7. PMID 9837959.
Park SH, Ryu SH, Suh PG, Kim H (1999). "Assignment of human PLD2 to chromosome band 17p13.1 by fluorescence in situ hybridization.". Cytogenet. Cell Genet. 82 (3-4): 225. PMID 9858823.
Czarny M, Fiucci G, Lavie Y, et al. (2000). "Phospholipase D2: functional interaction with caveolin in low-density membrane microdomains.". FEBS Lett. 467 (2-3): 326-32. PMID 10675563.
Lee C, Kim SR, Chung JK, et al. (2000). "Inhibition of phospholipase D by amphiphysins.". J. Biol. Chem. 275 (25): 18751-8. doi:10.1074/jbc.M001695200. PMID 10764771.
Park JB, Kim JH, Kim Y, et al. (2000). "Cardiac phospholipase D2 localizes to sarcolemmal membranes and is inhibited by alpha-actinin in an ADP-ribosylation factor-reversible manner.". J. Biol. Chem. 275 (28): 21295-301. doi:10.1074/jbc.M002463200. PMID 10801846.
Zhang Y, Redina O, Altshuller YM, et al. (2001). "Regulation of expression of phospholipase D1 and D2 by PEA-15, a novel protein that interacts with them.". J. Biol. Chem. 275 (45): 35224-32. doi:10.1074/jbc.M003329200. PMID 10926929.
Morash SC, Byers DM, Cook HW (2000). "Activation of phospholipase D by PKC and GTPgammaS in human neuroblastoma cells overexpressing MARCKS.". Biochim. Biophys. Acta 1487 (2-3): 177-89. PMID 11018470.
Divecha N, Roefs M, Halstead JR, et al. (2000). "Interaction of the type Ialpha PIPkinase with phospholipase D: a role for the local generation of phosphatidylinositol 4, 5-bisphosphate in the regulation of PLD2 activity.". EMBO J. 19 (20): 5440-9. doi:10.1093/emboj/19.20.5440. PMID 11032811.
Slaaby R, Du G, Altshuller YM, et al. (2001). "Insulin-induced phospholipase D1 and phospholipase D2 activity in human embryonic kidney-293 cells mediated by the phospholipase C gamma and protein kinase C alpha signalling cascade.". Biochem. J. 351 Pt 3: 613-9. PMID 11042115.
Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788-95. PMID 11076863.
Lee S, Park JB, Kim JH, et al. (2001). "Actin directly interacts with phospholipase D, inhibiting its activity.". J. Biol. Chem. 276 (30): 28252-60. doi:10.1074/jbc.M008521200. PMID 11373276.
Sarkar S, Miwa N, Kominami H, et al. (2001). "Regulation of mammalian phospholipase D2: interaction with and stimulation by G(M2) activator.". Biochem. J. 359 (Pt 3): 599-604. PMID 11672434.
Denmat-Ouisse LA, Phebidias C, Honkavaara P, et al. (2002). "Regulation of constitutive protein transit by phospholipase D in HT29-cl19A cells.". J. Biol. Chem. 276 (52): 48840-6. doi:10.1074/jbc.M104276200. PMID 11687572.
Lee S, Kim JH, Lee CS, et al. (2002). "Collapsin response mediator protein-2 inhibits neuronal phospholipase D(2) activity by direct interaction.". J. Biol. Chem. 277 (8): 6542-9. doi:10.1074/jbc.M108047200. PMID 11741937.
Han JM, Kim JH, Lee BD, et al. (2002). "Phosphorylation-dependent regulation of phospholipase D2 by protein kinase C delta in rat Pheochromocytoma PC12 cells.". J. Biol. Chem. 277 (10): 8290-7. doi:10.1074/jbc.M108343200. PMID 11744693.