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 language | English |
|---|---|
| Pages (from-to) | 29640-29643 |
| Number of pages | 4 |
| Journal | Journal of Biological Chemistry |
| Volume | 270 |
| Issue number | 50 |
| DOIs | |
| State | Published - Dec 15 1995 |
Bibliographical note
Funding Information:Accepted Januaty 9. 1992. From the Department ofPsychiatry, University ofPittsburgh School of Medicine, and the Western Psychiatric Institute and Clinic, Pittsburgh, PA. Preparation of this article was supported in part by NIMH grant MH 33990 and a grant from the W. T. Grant Foundation. Reprint requests to Dr. Bowring. WPiC, 3811 O'Hara Street, Pittsburgh, PA 15213. 0890-8567/92/3104-0611$03.00/0©1992 by the American Academy of Child and Adolescent Psychiatry.
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology