PHOSPHOLIPASE-D IS PRESENT ON GOLGI-ENRICHED MEMBRANES AND ITS ACTIVATION BY ADP-RIBOSYLATION FACTOR IS SENSITIVE TO BREFELDIN-A

被引：175

作者：

KTISTAKIS, NT ^{[1
]}

BROWN, HA ^{[1
]}

STERNWEIS, PC ^{[1
]}

ROTH, MG ^{[1
]}

机构：

[1] UNIV TEXAS,SW MED CTR,DEPT PHARMACOL,DALLAS,TX 75235

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1995年 / 92卷 / 11期

关键词：

D O I：

10.1073/pnas.92.11.4952

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：4952 / 4956

页数：5

共 33 条

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