Molecular chaperones: The busy life of Hsp90

被引：131

作者：

Mayer, MP ^{[1
]}

Bukau, B ^{[1
]}

机构：

[1] Univ Freiburg, Inst Biochem & Mol Biol, D-79104 Freiburg, Germany

来源：

CURRENT BIOLOGY | 1999年 / 9卷 / 09期

关键词：

D O I：

10.1016/S0960-9822(99)80203-6

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 heat shock protein Hsp90 is a molecular chaperone which assists the refolding of misfolded proteins, but also has highly selective functions in normal metabolism. These dual functions enable Hsp90 to connect environmental conditions with developmental processes and to buffer genetic changes.

引用

页码：R322 / R325

页数：4

共 18 条

[1]

Bose S, 1999, MOL CHAPERONES FOLDI, P637

[2] Growing up in a dangerous environment: A network of multiple targeting and folding pathways for nascent polypeptides in the cytosol [J].

Bukau, B ;

Hesterkamp, T ;

Luirink, J .

TRENDS IN CELL BIOLOGY, 1996, 6 (12) :480-486

[3]

BUKAU B, 1999, MOL CHAPERONES FOLDI

[4] The human cytosolic molecular chaperones hsp90, Hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding [J].

Freeman, BC ;

Morimoto, RI .

EMBO JOURNAL, 1996, 15 (12) :2969-2979

[5] Modular folding and evidence for phosphorylation-induced stabilization of an hsp90-dependent kinase [J].

Hartson, SD ;

Ottinger, EA ;

Huang, WJ ;

Barany, G ;

Burn, P ;

Matts, RL .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (14) :8475-8482

[6] Cdc37: A protein kinase chaperone? [J].

Hunter, T ;

Poon, RYC .

TRENDS IN CELL BIOLOGY, 1997, 7 (04) :157-161

[7] Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome [J].

Loo, MA ;

Jensen, TJ ;

Cui, LY ;

Hou, YX ;

Chang, XB ;

Riordan, JR .

EMBO JOURNAL, 1998, 17 (23) :6879-6887

[8] The complexity of Raf-1 regulation [J].

Morrison, DK ;

Cutler, RE .

CURRENT OPINION IN CELL BIOLOGY, 1997, 9 (02) :174-179

[9] In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone [J].

Nathan, DF ;

Vos, MH ;

Lindquist, S .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (24) :12949-12956

[10] ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo [J].

Panaretou, B ;

Prodromou, C ;

Roe, SM ;

O'Brien, R ;

Ladbury, JE ;

Piper, PW ;

Pearl, LH .

EMBO JOURNAL, 1998, 17 (16) :4829-4836

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