Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family

Scott M. Hammond, Yelena M. Altshuller, Tsung Chang Sung, Simon A. Rudge, Kristine Rose, JoAnne Engebrecht, Andrew J. Morris, Michael A. Frohman

Research output: Contribution to journalArticle

583 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)29640-29643
Number of pages4
JournalJournal of Biological Chemistry
Volume270
Issue number50
DOIs
StatePublished - Dec 15 1995
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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    Hammond, S. M., Altshuller, Y. M., Sung, T. C., Rudge, S. A., Rose, K., Engebrecht, J., Morris, A. J., & Frohman, M. A. (1995). Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family. Journal of Biological Chemistry, 270(50), 29640-29643. https://doi.org/10.1074/jbc.270.50.29640