PLD2

PLD2
Identifiers
AliasesPLD2, phospholipase D2, PLD1C
External IDsMGI: 892877 HomoloGene: 55672 GeneCards: PLD2
Gene location (Human)
Chr.Chromosome 17 (human)[1]
BandNo data availableStart4,807,096 bp[1]
End4,823,434 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

5338

18806

Ensembl

ENSG00000129219

ENSMUSG00000020828

UniProt

O14939

P97813

RefSeq (mRNA)

NM_001243108
NM_002663

NM_008876
NM_001302475
NM_001302476

RefSeq (protein)

NP_001230037
NP_002654

NP_001289404
NP_001289405
NP_032902

Location (UCSC)Chr 17: 4.81 – 4.82 MbChr 17: 70.54 – 70.56 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Phospholipase D2 is an enzyme that in humans is encoded by the PLD2 gene.[5][6]

Function

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][7]

Interactions

PLD2 has been shown to interact with:

Inhibitors

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000129219 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020828 - Ensembl, May 2017
  3. "Human PubMed Reference:".
  4. "Mouse PubMed Reference:".
  5. Park SH, Ryu SH, Suh PG, Kim H (February 1999). "Assignment of human PLD2 to chromosome band 17p13.1 by fluorescence in situ hybridization". Cytogenet Cell Genet. 82 (3–4): 225. PMID 9858823. doi:10.1159/000015106.
  6. Lopez I, Arnold RS, Lambeth JD (June 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. doi:10.1074/jbc.273.21.12846.
  7. "Entrez Gene: PLD2 phospholipase D2".
  8. Lee S, Park JB, Kim JH, Kim Y, Kim JH, Shin KJ, Lee JS, Ha SH, Suh PG, Ryu SH (July 2001). "Actin directly interacts with phospholipase D, inhibiting its activity". J. Biol. Chem. 276 (30): 28252–60. PMID 11373276. doi:10.1074/jbc.M008521200.
  9. Park JB, Kim JH, Kim Y, Ha SH, Yoo JS, Du G, Frohman MA, Suh PG, Ryu SH (July 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. PMID 10801846. doi:10.1074/jbc.M002463200.
  10. Kim JH, Lee S, Kim JH, Lee TG, Hirata M, Suh PG, Ryu SH (March 2002). "Phospholipase D2 directly interacts with aldolase via Its PH domain". Biochemistry. 41 (10): 3414–21. PMID 11876650. doi:10.1021/bi015700a.
  11. 1 2 Lee C, Kim SR, Chung JK, Frohman MA, Kilimann MW, Rhee SG (June 2000). "Inhibition of phospholipase D by amphiphysins". J. Biol. Chem. 275 (25): 18751–8. PMID 10764771. doi:10.1074/jbc.M001695200.
  12. Zheng X, Bollinger Bollag W (December 2003). "Aquaporin 3 colocates with phospholipase d2 in caveolin-rich membrane microdomains and is downregulated upon keratinocyte differentiation". J. Invest. Dermatol. 121 (6): 1487–95. PMID 14675200. doi:10.1111/j.1523-1747.2003.12614.x.
  13. Czarny M, Fiucci G, Lavie Y, Banno Y, Nozawa Y, Liscovitch M (February 2000). "Phospholipase D2: functional interaction with caveolin in low-density membrane microdomains". FEBS Lett. 467 (2-3): 326–32. PMID 10675563. doi:10.1016/s0014-5793(00)01174-1.
  14. Kim JH, Lee S, Park JB, Lee SD, Kim JH, Ha SH, Hasumi K, Endo A, Suh PG, Ryu SH (June 2003). "Hydrogen peroxide induces association between glyceraldehyde 3-phosphate dehydrogenase and phospholipase D2 to facilitate phospholipase D2 activation in PC12 cells". J. Neurochem. 85 (5): 1228–36. PMID 12753082. doi:10.1046/j.1471-4159.2003.01755.x.
  15. Jang IH, Lee S, Park JB, Kim JH, Lee CS, Hur EM, Kim IS, Kim KT, Yagisawa H, Suh PG, Ryu SH (May 2003). "The direct interaction of phospholipase C-gamma 1 with phospholipase D2 is important for epidermal growth factor signaling". J. Biol. Chem. 278 (20): 18184–90. PMID 12646582. doi:10.1074/jbc.M208438200.
  16. Han JM, Kim JH, Lee BD, Lee SD, Kim Y, Jung YW, Lee S, Cho W, Ohba M, Kuroki T, Suh PG, Ryu SH (March 2002). "Phosphorylation-dependent regulation of phospholipase D2 by protein kinase C delta in rat Pheochromocytoma PC12 cells". J. Biol. Chem. 277 (10): 8290–7. PMID 11744693. doi:10.1074/jbc.M108343200.
  17. Ahn BH, Kim SY, Kim EH, Choi KS, Kwon TK, Lee YH, Chang JS, Kim MS, Jo YH, Min DS (May 2003). "Transmodulation between phospholipase D and c-Src enhances cell proliferation". Mol. Cell. Biol. 23 (9): 3103–15. PMC 153190Freely accessible. PMID 12697812. doi:10.1128/mcb.23.9.3103-3115.2003.
  18. Kantonen S, Hatton N, Mahankali M, Henkels KM, Park H, Cox D, Gomez-Cambronero J (November 2011). "A novel phospholipase D2-Grb2-WASp heterotrimer regulates leukocyte phagocytosis in a two-step mechanism". Mol. Cell. Biol. 31 (22): 4524–37. PMC 3209255Freely accessible. PMID 21930784. doi:10.1128/MCB.05684-11.
  19. Lavieri RR, Scott SA, Selvy PE, Kim K, Jadhav S, Morrison RD, Daniels JS, Brown HA, Lindsley CW (September 2010). "Design, Synthesis, and Biological Evaluation of Halogenated N-(2-(4-Oxo-1-phenyl-1,3,8-triazaspiro[4.5]decan-8-yl)ethyl)benzamides: Discovery of an Isoform-Selective Small Molecule Phospholipase D2 Inhibitor". J. Med. Chem. 53 (18): 6706–19. PMC 3179181Freely accessible. PMID 20735042. doi:10.1021/jm100814g.

Further reading

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