Phospholipase D1

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Phospholipase D1, phosphatidylcholine-specific
Identifiers
Symbol PLD1
External IDs OMIM602382 MGI109585 HomoloGene116234 ChEMBL: 2536 GeneCards: PLD1 Gene
EC number 3.1.4.4
RNA expression pattern
PBB GE PLD1 215723 s at tn.png
PBB GE PLD1 215724 at tn.png
PBB GE PLD1 177 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 5337 18805
Ensembl ENSG00000075651 ENSMUSG00000027695
UniProt Q13393 Q3UWT7
RefSeq (mRNA) NM_001130081 NM_001164056
RefSeq (protein) NP_001123553 NP_001157528
Location (UCSC) Chr 3:
171.32 – 171.53 Mb
Chr 3:
27.94 – 28.13 Mb
PubMed search [1] [2]

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

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][3]

Interactions[edit]

Phospholipase D1 has been shown to interact with RALA,[4][5] BIN1,[6] Amphiphysin,[6] Alpha-synuclein,[7] PEA15,[8] RHOA,[9][10] Protein kinase N1[11] and CDC42.[12]

Inhibitors[edit]

References[edit]

  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. ^ Luo, J Q; Liu X; Hammond S M; Colley W C; Feig L A; Frohman M A; Morris A J; Foster D A (June 1997). "RalA interacts directly with the Arf-responsive, PIP2-dependent phospholipase D1". Biochem. Biophys. Res. Commun. (UNITED STATES) 235 (3): 854–9. doi:10.1006/bbrc.1997.6793. ISSN 0006-291X. PMID 9207251. 
  5. ^ Kim, J H; Lee S D; Han J M; Lee T G; Kim Y; Park J B; Lambeth J D; Suh P G; Ryu S H (July 1998). "Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA". FEBS Lett. (NETHERLANDS) 430 (3): 231–5. doi:10.1016/S0014-5793(98)00661-9. ISSN 0014-5793. PMID 9688545. 
  6. ^ a b Lee, C; Kim S R; Chung J K; Frohman M A; Kilimann M W; Rhee S G (June 2000). "Inhibition of phospholipase D by amphiphysins". J. Biol. Chem. (UNITED STATES) 275 (25): 18751–8. doi:10.1074/jbc.M001695200. ISSN 0021-9258. PMID 10764771. 
  7. ^ Ahn, Bong-Hyun; Rhim Hyangshuk, Kim Shi Yeon, Sung Young-Mo, Lee Mun-Yong, Choi Ju-Youn, Wolozin Benjamin, Chang Jong-Soo, Lee Young Han, Kwon Taeg Kyu, Chung Kwang Chul, Yoon Shin-Hee, Hahn Sang June, Kim Myung-Suk, Jo Yang-Hyeok, Min Do Sik (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. (United States) 277 (14): 12334–42. doi:10.1074/jbc.M110414200. ISSN 0021-9258. PMID 11821392. 
  8. ^ Zhang, Y; Redina O; Altshuller Y M; Yamazaki M; Ramos J; Chneiweiss H; Kanaho Y; Frohman M A (November 2000). "Regulation of expression of phospholipase D1 and D2 by PEA-15, a novel protein that interacts with them". J. Biol. Chem. (UNITED STATES) 275 (45): 35224–32. doi:10.1074/jbc.M003329200. ISSN 0021-9258. PMID 10926929. 
  9. ^ Genth, Harald; Schmidt Martina; Gerhard Ralf; Aktories Klaus; Just Ingo (February 2003). "Activation of phospholipase D1 by ADP-ribosylated RhoA". Biochem. Biophys. Res. Commun. (United States) 302 (1): 127–32. doi:10.1016/S0006-291X(03)00112-8. ISSN 0006-291X. PMID 12593858. 
  10. ^ Cai, S; Exton J H (May 2001). "Determination of interaction sites of phospholipase D1 for RhoA". Biochem. J. (England) 355 (Pt 3): 779–85. ISSN 0264-6021. PMC 1221795. PMID 11311142. 
  11. ^ 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. (United States) 276 (21): 18096–101. doi:10.1074/jbc.M010646200. ISSN 0021-9258. PMID 11259428. 
  12. ^ Walker, S J; Wu W J; Cerione R A; Brown H A (May 2000). "Activation of phospholipase D1 by Cdc42 requires the Rho insert region". J. Biol. Chem. (UNITED STATES) 275 (21): 15665–8. doi:10.1074/jbc.M000076200. ISSN 0021-9258. PMID 10747870. 
  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. PMID 19268584. 

Further reading[edit]