Heat-shock protein 90, a chaperone for folding and regulation

被引：664

作者：

Picard, D ^{[1
]}

机构：

[1] Univ Geneva, Dept Biol Cellulaire, CH-1211 Geneva 4, Switzerland

来源：

CELLULAR AND MOLECULAR LIFE SCIENCES | 2002年 / 59卷 / 10期

关键词：

molecular chaperone; protein folding; p23; Hop; Cdc37; immunophilins;

D O I：

10.1007/PL00012491

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：

Heat-shock protein 90 (Hsp90) is an abundant and highly conserved molecular chaperone that is essential for viability in eukaryotes. Hsp90 fulfills a housekeeping function in contributing to the folding, maintenance of structural integrity and proper regulation of a subset of cytosolic proteins. A remarkable proportion of its substrates are proteins involved in cell cycle control and signal transduction. Hsp90 acts with a cohort of Hsp90 co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. The large conformational flexibility of Hsp90 and a multitude of dynamic co-chaperone complexes contribute to generating functional diversity, and allow Hsp90 to assist a wide range of substrates.

引用

页码：1640 / 1648

页数：9

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