Phospholipase D1

From Wikipedia, the free encyclopedia

Phospholipase D1, phosphatidylcholine-specific

Identifiers

External IDs

OMIM: 602382 MGI: 109585 HomoloGene: 37651

Gene ontology
Molecular Function:	• phospholipase D activity • protein binding • hydrolase activity • phosphoinositide binding
Cellular Component:	• endosome • endoplasmic reticulum • Golgi apparatus • membrane
Biological Process:	• phospholipid metabolic process • chemotaxis • cell communication • Ras protein signal transduction • metabolic process • lipid catabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002662 (mRNA)
NP_002653 (protein)

NM_008875 (mRNA)
NP_032901 (protein)

Location

Chr 3: 172.8 - 173.01 Mb

Chr 3: 28.13 - 28.32 Mb

Pubmed search

[1]

[2]

Phospholipase D1, phosphatidylcholine-specific, also known as PLD1, is a human gene.

Phosphatidylcholine (PC)-specific phospholipases D (PLDs) EC 3.1.4.4 catalyze the hydrolysis of PC to produce phosphatidic acid and choline. A range of agonists acting through G protein-coupled receptors and receptor tyrosine kinases stimulate this hydrolysis. PC-specific PLD activity has been implicated in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis (Hammond et al., 1995).[supplied by OMIM]^[1]

[edit] References

^ Entrez Gene: PLD1 phospholipase D1, phosphatidylcholine-specific.

[edit] Further reading

Hammond SM, Altshuller YM, Sung TC, et al. (1996). "Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family.". J. Biol. Chem. 270 (50): 29640–3. PMID 8530346.
Hammond SM, Jenco JM, Nakashima S, et al. (1997). "Characterization of two alternately spliced forms of phospholipase D1. Activation of the purified enzymes by phosphatidylinositol 4,5-bisphosphate, ADP-ribosylation factor, and Rho family monomeric GTP-binding proteins and protein kinase C-alpha.". J. Biol. Chem. 272 (6): 3860–8. PMID 9013646.
Luo JQ, Liu X, Hammond SM, et al. (1997). "RalA interacts directly with the Arf-responsive, PIP2-dependent phospholipase D1.". Biochem. Biophys. Res. Commun. 235 (3): 854–9. doi:10.1006/bbrc.1997.6793. PMID 9207251.
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.
Bae CD, Min DS, Fleming IN, Exton JH (1998). "Determination of interaction sites on the small G protein RhoA for phospholipase D.". J. Biol. Chem. 273 (19): 11596–604. PMID 9565577.
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.
Kim JH, Lee SD, Han JM, et al. (1998). "Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA.". FEBS Lett. 430 (3): 231–5. PMID 9688545.
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.
Park SH, Chun YH, Ryu SH, et al. (1999). "Assignment of human PLD1 to human chromosome band 3q26 by fluorescence in situ hybridization.". Cytogenet. Cell Genet. 82 (3-4): 224. PMID 9858822.
Kim JH, Han JM, Lee S, et al. (1999). "Phospholipase D1 in caveolae: regulation by protein kinase Calpha and caveolin-1.". Biochemistry 38 (12): 3763–9. doi:10.1021/bi982478. PMID 10090765.
Kim Y, Han JM, Park JB, et al. (1999). "Phosphorylation and activation of phospholipase D1 by protein kinase C in vivo: determination of multiple phosphorylation sites.". Biochemistry 38 (32): 10344–51. doi:10.1021/bi990579h. PMID 10441128.
Walker SJ, Wu WJ, Cerione RA, Brown HA (2000). "Activation of phospholipase D1 by Cdc42 requires the Rho insert region.". J. Biol. Chem. 275 (21): 15665–8. doi:10.1074/jbc.M000076200. PMID 10747870.
Suzuki J, Yamazaki Y, Li G, et al. (2000). "Involvement of Ras and Ral in chemotactic migration of skeletal myoblasts.". Mol. Cell. Biol. 20 (13): 4658–65. PMID 10848592.
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.
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.
Oishi K, Takahashi M, Mukai H, et al. (2001). "PKN regulates phospholipase D1 through direct interaction.". J. Biol. Chem. 276 (21): 18096–101. doi:10.1074/jbc.M010646200. PMID 11259428.
Cai S, Exton JH (2001). "Determination of interaction sites of phospholipase D1 for RhoA.". Biochem. J. 355 (Pt 3): 779–85. PMID 11311142.
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.
Hughes WE, Parker PJ (2001). "Endosomal localization of phospholipase D 1a and 1b is defined by the C-termini of the proteins, and is independent of activity.". Biochem. J. 356 (Pt 3): 727–36. PMID 11389680.
Min DS, Ahn BH, Jo YH (2002). "Differential tyrosine phosphorylation of phospholipase D isozymes by hydrogen peroxide and the epidermal growth factor in A431 epidermoid carcinoma cells.". Mol. Cells 11 (3): 369–78. PMID 11459228.