Phospholipase D is present on Golgi-enriched membranes and its activation by ADP ribosylation factor is sensitive to brefeldin A.

Ktistakis NT, Brown HA, Sternweis PC, Roth MG
Proc Natl Acad Sci U S A. 1995 92 (11): 4952-6

PMID: 7761430 · PMCID: PMC41825 · DOI:10.1073/pnas.92.11.4952

ADP ribosylation factor (ARF) is a small guanosine triphosphate (GTP)-binding protein that regulates the binding of coat proteins to membranes and is required for several stages of vesicular transport. ARF also stimulates phospholipase D (PLD) activity, which can alter the lipid content of membranes by conversion of phospholipids into phosphatidic acid. Abundant PLD activity was found in Golgi-enriched membranes from several cell lines. Golgi PLD activity was greatly stimulated by ARF and GTP analogs and this stimulation could be inhibited by brefeldin A (BFA), a drug that blocks binding of ARF to Golgi membranes. Furthermore, in Golgi membranes from BFA-resistant PtK1 cells, basal PLD activity was high and not stimulated by exogenous ARF or GTP analogs. Thus, ARF activates PLD on the Golgi complex, suggesting a possible link between transport events and the underlying architecture of the lipid bilayer.

MeSH Terms (21)

ADP-Ribosylation Factors Animals Brefeldin A Carrier Proteins Cell Fractionation Cell Line CHO Cells Cricetinae Cyclopentanes Dogs Dose-Response Relationship, Drug Enzyme Activation Golgi Apparatus GTP-Binding Proteins Guanosine 5'-O-(3-Thiotriphosphate) Intracellular Membranes Kinetics Orthomyxoviridae Phospholipase D Protein Binding Protein Synthesis Inhibitors

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