Hsp90 - From signal transduction to cell transformation

被引：69

作者：

Brown, Mark A. ^{[1
]}

Zhu, Li ^{[1
]}

Schmidt, Christian ^{[1
]}

Tucker, Philip W. ^{[1
]}

机构：

[1] Univ Texas, Inst Cellular & Mol Biol, Sect Mol Genet & Microbiol, Austin, TX 78712 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2007年 / 363卷 / 02期

关键词：

Hsp90; heat shock protein; molecular chaperone; ATPase; genetic capacitor;

D O I：

10.1016/j.bbrc.2007.08.054

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：

The molecular chaperone, Hsp90, facilitates the maturation and/or activation of over 100 'client proteins' involved in signal transduction and transcriptional regulation. Largely an enigma among the families of heat shock proteins, Hsp90 is central to processes broadly ranging from cell cycle regulation to cellular transformation. Here, we review the contemporary body of knowledge regarding the biochemical mechanisms of Hsp90 and update the most current paradigms defining its involvement in both normal and pathological cell physiology. (C) 2007 Elsevier Inc. All rights reserved.

引用

页码：241 / 246

页数：6

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