蛋白激酶的脂质激活作用。
Lipid activation of protein kinases.
作者信息
Newton Alexandra C
机构信息
Department of Pharmacology, University of California at San Diego, La Jolla, CA 92093-0721, USA.
出版信息
J Lipid Res. 2009 Apr;50 Suppl(Suppl):S266-71. doi: 10.1194/jlr.R800064-JLR200. Epub 2008 Nov 24.
Abstract
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). 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.
摘要
脂质可急性调控由脂质第二信使应答激酶介导的信号传导的幅度、持续时间和亚细胞定位。通常，这种激活由膜靶向模块控制，这些模块通过变构作用控制同一多肽内激酶结构域的功能。蛋白激酶C（PKC）一直是典型的脂质调节激酶，为脂质控制的激酶激活提供了一个原型，整个激酶组中的激酶都遵循这种激活方式，包括其近亲Akt（蛋白激酶B）。本综述探讨了PKC和Akt转导细胞中两条主要脂质第二信使途径（分别为二酰基甘油信号传导途径和磷脂酰肌醇-3,4,5-三磷酸（PIP3）信号传导途径）所传播信号的分子机制。
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