| Literature DB >> 8530346 |
S M Hammond1, Y M Altshuller, T C Sung, S A Rudge, K Rose, J Engebrecht, A J Morris, M A Frohman.
Abstract
Activation of phosphatidylcholine-specific phospholipase D (PLD) has been implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. We report here the identification of the first human PLD cDNA, which defines a new and highly conserved gene family. Characterization of recombinant human PLD1 reveals that it is membrane-associated, selective for phosphatidylcholine, stimulated by phosphatidylinositol 4,5-bisphosphate, activated by the monomeric G-protein ADP-ribosylation factor-1, and inhibited by oleate. PLD1 likely encodes the gene product responsible for the most widely studied endogenous PLD activity.Entities:
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Year: 1995 PMID: 8530346 DOI: 10.1074/jbc.270.50.29640
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157