The HSP90 chaperone machinery

被引：1019

作者：

Schopf, Florian H. ^{[1
]}

Biebl, Maximilian M. ^{[1
]}

Buchner, Johannes ^{[1
]}

机构：

[1] Tech Univ Munich, Ctr Integrated Prot Sci, Dept Chem, Garching, Germany

来源：

NATURE REVIEWS MOLECULAR CELL BIOLOGY | 2017年 / 18卷 / 06期

关键词：

HEAT-SHOCK-PROTEIN; WILD-TYPE P53; ATP-COMPETITIVE INHIBITORS; TUMOR-SUPPRESSOR PROTEIN; P23 MOLECULAR CHAPERONE; ESCHERICHIA-COLI HSP90; NITRIC-OXIDE SYNTHASE; E3 UBIQUITIN LIGASE; IN-VIVO FUNCTION; STEROID-RECEPTOR;

D O I：

10.1038/nrm.2017.20

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The heat shock protein 90 (HSP90) chaperone machinery is a key regulator of proteostasis under both physiological and stress conditions in eukaryotic cells. As HSP90 has several hundred protein substrates (or 'clients'), it is involved in many cellular processes beyond protein folding, which include DNA repair, development, the immune response and neurodegenerative disease. A large number of co-chaperones interact with HSP90 and regulate the ATPase-associated conformational changes of the HSP90 dimer that occur during the processing of clients. Recent progress has allowed the interactions of clients with HSP90 and its co-chaperones to be defined. Owing to the importance of HSP90 in the regulation of many cellular proteins, it has become a promising drug target for the treatment of several diseases, which include cancer and diseases associated with protein misfolding.

引用

页码：345 / 360

页数：16

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