Phosphatidic acid signaling regulation of Ras superfamily of small guanosine triphosphatases

被引：72

作者：

Zhang, Yueqiang ^{[1
]}

Du, Guangwei ^{[1
]}

机构：

[1] Univ Texas Hlth Sci Ctr Houston, Dept Integrat Biol & Pharmacol, Houston, TX 77030 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS | 2009年 / 1791卷 / 09期

基金：

美国国家卫生研究院;

关键词：

Phospholipid; Phosphatidic acid; Phospholipase D; Diacylglycerol kinase; Ras; Small GTPase; DIACYLGLYCEROL-KINASE-ALPHA; GTPASE-ACTIVATING PROTEIN; ADP-RIBOSYLATION FACTOR; T-CELL ANERGY; PHOSPHOLIPASE-D; PLASMA-MEMBRANE; EXCHANGE FACTOR; BINDING PROTEINS; GROWTH-FACTOR; N-TERMINUS;

D O I：

10.1016/j.bbalip.2009.05.013

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Phosphatidic acid (PA) has been increasingly recognized as an important signaling lipid regulating cell growth and proliferation, membrane trafficking, and cytoskeletal reorganization. Recent studies indicate that the signaling PA generated from phospholipase D (PLD) and diacylglycerol kinase (DGK) plays critical roles in regulating the activity of some members of Ras superfamily of small guanosine triphosphatases (GTPases), such as Ras, Rac and Arf. Change of PA levels regulates the activity of small GTPases by modulating membrane localization and activity of small GTPase regulatory proteins, guanine nucleotide exchange factors (GEFs) and GTPase activating proteins (GAPs). In addition. PA also targets some small GTPases to membranes by direct binding. This review summarizes the roles of PLD and DGK in regulating the activity of several Ras superfamily members and cellular processes they control. Some future directions and the implication of PA regulation of Ras small GTPases in pathology are also discussed. (C) 2009 Elsevier B.V. All rights reserved.

引用

页码：850 / 855

页数：6

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