HSP90 at the hub of protein homeostasis: emerging mechanistic insights

被引：1392

作者：

Taipale, Mikko ^{[1
]}

Jarosz, Daniel F. ^{[1
,2
]}

Lindquist, Susan ^{[1
,2
]}

机构：

[1] Whitehead Inst Biomed Res, Cambridge, MA 02142 USA

[2] MIT, Howard Hughes Med Inst, Dept Biol, Cambridge, MA 02139 USA

来源：

NATURE REVIEWS MOLECULAR CELL BIOLOGY | 2010年 / 11卷 / 07期

关键词：

HEAT-SHOCK-PROTEIN; MOLECULAR CHAPERONE HSP90; VIRUS TRANSFORMING PROTEIN; ESCHERICHIA-COLI HSP90; 7-AMINO ACID SEQUENCE; NITRIC-OXIDE SYNTHASE; N-TERMINAL DOMAIN; ATPASE ACTIVITY; GLUCOCORTICOID-RECEPTOR; CRYSTAL-STRUCTURE;

D O I：

10.1038/nrm2918

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that facilitates the maturation of a wide range of proteins (known as clients). Clients are enriched in signal transducers, including kinases and transcription factors. Therefore, HSP90 regulates diverse cellular functions and exerts marked effects on normal biology, disease and evolutionary processes. Recent structural and functional analyses have provided new insights on the transcriptional and biochemical regulation of HSP90 and the structural dynamics it uses to act on a diverse client repertoire. Comprehensive understanding of how HSP90 functions promises not only to provide new avenues for therapeutic intervention, but to shed light on fundamental biological questions.

引用

页码：515 / 528

页数：14

共 177 条

[11] THE SPECIFIC INTERACTION OF THE ROUS-SARCOMA VIRUS TRANSFORMING PROTEIN, PP60SRC, WITH 2 CELLULAR PROTEINS [J].