Intracellular transport mechanisms of signal transducers

被引：118

作者：

Dorn, GW ^{[1
]}

Mochly-Rosen, D

机构：

[1] Univ Cincinnati, Dept Med, Cincinnati, OH 45267 USA

[2] Stanford Univ, Sch Med, Dept Mol Pharmacol, Stanford, CA 94305 USA

来源：

ANNUAL REVIEW OF PHYSIOLOGY | 2002年 / 64卷

关键词：

protein kinase C; protein kinase A; translocation; anchoring proteins; Rab GTPase;

D O I：

10.1146/annurev.physiol.64.081501.155903

中图分类号：

Q4 [生理学];

学科分类号：

071003 ;

摘要：

Recent discoveries have revolutionized our conceptions of enzyme-substrate specificity in signal transduction pathways. Protein kinases A and C are localized to discreet subcellular regions, and this localization changes in an isozyme-specific manner upon activation, a process referred to as translocation. The mechanisms for translocation involve interactions of soluble kinases with membrane-bound anchor proteins that recognize individual kinase isoenzymes and their state of activation. Recently, modulation of kinase-anchor protein interactions has been used to specifically regulate, positively or negatively, the activity of C kinase isozymes. Also described in this review is a role for the Rab family of small G proteins in regulating subcellular protein trafficking. The pathophysiological significance of disrupted subcellular protein transport in cell signaling and the potential therapeutic utility of targeted regulation of these events are in the process of being characterized.

引用

页码：407 / 429

页数：27

共 105 条

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