Lipid activation of protein kinases

被引：123

作者：

Newton, Alexandra C. ^{[1
]}

机构：

[1] Univ Calif San Diego, Dept Pharmacol, La Jolla, CA 92093 USA

来源：

JOURNAL OF LIPID RESEARCH | 2009年 / 50卷

基金：

美国国家卫生研究院;

关键词：

protein kinase C; Akt; diacylglycerol; phosphatidylinositol-3,4,5-tris phosphate; ENCODED FLUORESCENT REPORTER; MEMBRANE-TARGETING MODULES; LIVING CELLS; C1; DOMAIN; PHOSPHORYLATION; PKC; PATHWAY; PARADIGM; CALCIUM; CANCER;

D O I：

10.1194/jlr.R800064-JLR200

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：

Lipids acutely control the amplitude, duration, and subcellular location of signaling by lipid second messenger-responsive kinases. Typically, this activation is controlled by membrane-targeting modules that allosterically control the function of kinase domains within the same polypeptide. Protein kinase C (PKC) has served as the archetypal lipid-regulated kinase, providing a prototype for lipid-controlled kinase activation that is followed by kinases throughout the kinome, including its close cousin, Akt (protein kinase B). jlr This review addresses the molecular mechanisms by which PKC and Akt transduce signals propagated by the two major lipid second messenger pathways in cells, those of diacylglycerol signaling and phosphatidylinositol-3,4,5-trisphosphate (PIP3) signaling, respectively.-Newton, A. C. Lipid activation of protein kinases. J. Lipid Res. 2009. S266-S271.

引用

页码：S266 / S271

页数：6

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