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PMID: 8530346 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

The Journal of biological chemistry ·Vol. 270 ·No. 50 ·1995-12-15 ·Pages 29640-3

Hammond SM, Altshuller YM, Sung TC, Rudge SA, Rose K, Engebrecht J, Morris AJ, Frohman MA

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.

MeSH Terms

ADP-Ribosylation Factors Amino Acid Sequence Animals Bacteria/enzymology Baculoviridae Caenorhabditis elegans/enzymology Carrier Proteins/metabolism Cell Line Chlorocebus aethiops Cloning, Molecular Conserved Sequence Enzyme Activation GTP-Binding Proteins/metabolism Humans Kinetics Mice Molecular Sequence Data Multigene Family Phosphatidylcholines/metabolism Phosphatidylinositol 4,5-Diphosphate Phosphatidylinositol Phosphates/pharmacology Phospholipase D/genetics,metabolism Plants/enzymology Recombinant Proteins/metabolism Spodoptera Substrate Specificity Transfection

Chemicals

Carrier Proteins Phosphatidylcholines Phosphatidylinositol 4,5-Diphosphate Phosphatidylinositol Phosphates Recombinant Proteins Phospholipase D GTP-Binding Proteins ADP-Ribosylation Factors

Authors & Affiliations

8 authors, click to expand affiliations / ORCID

Hammond S M

Department of Pharmacological Sciences, State University of New York, Stony Brook 11794-8651, USA.

Altshuller Y M

Sung T C

Rudge S A

Rose K

Engebrecht J

Morris A J

Frohman M A

Article Info

Journal

The Journal of biological chemistry

Abbr.

J Biol Chem

ISSN

0021-9258

DOI

10.1074/jbc.270.50.29640

Published

1995-12-15

Pages

29640-3

Language

English

Region

United States

NLM ID

2985121R

Subset

Grants

NIGMS NIH HHS · GM4863903 · United States

NIGMS NIH HHS · GM50388 · United States

NICHD NIH HHS · HD29758 · United States

Databases

GENBANK

D27058, D33536, G00778, L33686, T76232, T88610, U38545, X28256, Z18424, Z33674

External Links

PubMed source DOI: 10.1074/jbc.270.50.29640 View journal details

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

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