Phospholipase D1

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RefSeq (mRNA)



RefSeq (protein)



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Phospholipase D1 is an enzyme that in humans is encoded by the PLD1 gene.[1][2]


Phosphatidylcholine (PC)-specific phospholipases D (PLDs) EC 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][3]


Phospholipase D1 has been shown to interact with:



  1. Park SH, Chun YH, Ryu SH, Suh PG, Kim H (February 1999). "Assignment of human PLD1 to human chromosome band 3q26 by fluorescence in situ hybridization". Cytogenet Cell Genet. 82 (3–4): 224. doi:10.1159/000015105. PMID 9858822.
  2. Hammond SM, Altshuller YM, Sung TC, Rudge SA, Rose K, Engebrecht J, Morris AJ, Frohman MA (January 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. doi:10.1074/jbc.270.50.29640. PMID 8530346.
  3. "Entrez Gene: PLD1 phospholipase D1, phosphatidylcholine-specific".
  4. Ahn BH, Rhim H, Kim SY, Sung YM, Lee MY, Choi JY, Wolozin B, Chang JS, Lee YH, Kwon TK, Chung KC, Yoon SH, Hahn SJ, Kim MS, Jo YH, Min DS (April 2002). "alpha-Synuclein interacts with phospholipase D isozymes and inhibits pervanadate-induced phospholipase D activation in human embryonic kidney-293 cells". J. Biol. Chem. 277 (14): 12334–42. doi:10.1074/jbc.M110414200. PMID 11821392.
  5. 5.0 5.1 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. doi:10.1074/jbc.M001695200. PMID 10764771.
  6. Walker SJ, Wu WJ, Cerione RA, Brown HA (May 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.
  7. Zhang Y, Redina O, Altshuller YM, Yamazaki M, Ramos J, Chneiweiss H, Kanaho Y, Frohman MA (November 2000). "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.
  8. Oishi K, Takahashi M, Mukai H, Banno Y, Nakashima S, Kanaho Y, Nozawa Y, Ono Y (May 2001). "PKN regulates phospholipase D1 through direct interaction". J. Biol. Chem. 276 (21): 18096–101. doi:10.1074/jbc.M010646200. PMID 11259428.
  9. Luo JQ, Liu X, Hammond SM, Colley WC, Feig LA, Frohman MA, Morris AJ, Foster DA (June 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.
  10. Kim JH, Lee SD, Han JM, Lee TG, Kim Y, Park JB, Lambeth JD, Suh PG, Ryu SH (July 1998). "Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA". FEBS Lett. 430 (3): 231–5. doi:10.1016/s0014-5793(98)00661-9. PMID 9688545.
  11. Genth H, Schmidt M, Gerhard R, Aktories K, Just I (February 2003). "Activation of phospholipase D1 by ADP-ribosylated RhoA". Biochem. Biophys. Res. Commun. 302 (1): 127–32. doi:10.1016/s0006-291x(03)00112-8. PMID 12593858.
  12. Cai S, Exton JH (May 2001). "Determination of interaction sites of phospholipase D1 for RhoA". Biochem. J. 355 (Pt 3): 779–85. doi:10.1042/bj3550779. PMC 1221795. PMID 11311142.
  13. Lewis JA, Scott SA, Lavieri R, Buck JR, Selvy PE, Stoops SL, Armstrong MD, Brown HA, Lindsley CW (April 2009). "Design and synthesis of isoform-selective phospholipase D (PLD) inhibitors. Part I: Impact of alternative halogenated privileged structures for PLD1 specificity". Bioorg. Med. Chem. Lett. 19 (7): 1916–20. doi:10.1016/j.bmcl.2009.02.057. PMC 3791604. PMID 19268584.

Further reading