Hsp90 and Co-Chaperones Twist the Functions of Diverse Client Proteins

被引：206
作者：
Zuehlke, Abbey
Johnson, Jill L. [1 ]
机构：
[1] Univ Idaho, Dept Microbiol Mol Biol & Biochem, Moscow, ID 83844 USA
来源：
BIOPOLYMERS | 2010年 / 93卷 / 03期
基金：
美国国家科学基金会; 美国国家卫生研究院;
关键词：
molecular machines; protein folding; molecular chaperones; MOLECULAR CHAPERONE; SACCHAROMYCES-CEREVISIAE; CAPACITOR; MECHANISM; COMPLEX; BINDING; CONFORMATION; INHIBITION; ACTIVATOR; MACHINE;
D O I：
10.1002/bip.21292
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：
Hsp90 molecular chaperones are required for the stability and activity of a diverse range of client proteins that have critical roles in signal transduction, cellular trafficking, chromatinf remodeling, cell growth, differentiation, and reproduction. Mammalian cells contain three types of Hsp90s: cytosolic Hsp90, mitochondrial Trap-1, and Grp94 of the endoplasmic reticulum. Each of the Hsp90s, as. well as the bacterial homolog, HtpG, hydrolyze ATP and undergo similar conformational changes. Unlike the other forms of Hsp90, cytosolic Hsp90 function is dependent on a battery of co-chaperone proteins that regulate the ATPase activity of Hsp90 or direct Hsp90 to interact with specific client proteins. This review will summarize what is known about Hsp90's ability to mediate the folding and activation of diverse client proteins that contribute to human diseases, such as cancer and fungal and viral infections. (C) 2009 Wiley Periodicals, Inc. Biopolymers 93: 211-217, 2010.
引用
收藏
页码：211 / 217
页数：7
相关论文
共 61 条
[1]   Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex [J].
Ali, MMU ;
Roe, SM ;
Vaughan, CK ;
Meyer, P ;
Panaretou, B ;
Piper, PW ;
Prodromou, C ;
Pearl, LH .
NATURE, 2006, 440 (7087) :1013-1017
[2]   Molecular chaperones and protein kinase quality control [J].
Caplan, Avrom J. ;
Mandal, Atin K. ;
Theodoraki, Maria A. .
TRENDS IN CELL BIOLOGY, 2007, 17 (02) :87-92
[3]   GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway [J].
Chadli, A ;
Graham, JD ;
Abel, MG ;
Jackson, TA ;
Gordon, DF ;
Wood, WM ;
Felts, SJ ;
Horwitz, KB ;
Toft, D .
MOLECULAR AND CELLULAR BIOLOGY, 2006, 26 (05) :1722-1730
[4]   Hop as an adaptor in the heat shock protein 70 (Hsp70) and Hsp90 chaperone machinery [J].
Chen, SY ;
Smith, DF .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (52) :35194-35200
[5]   OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD [J].
Christianson, John C. ;
Shaler, Thomas A. ;
Tyler, Ryan E. ;
Kopito, Ron R. .
NATURE CELL BIOLOGY, 2008, 10 (03) :272-U13
[6]   The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins [J].
Connell, P ;
Ballinger, CA ;
Jiang, JH ;
Wu, YX ;
Thompson, LJ ;
Höhfeld, J ;
Patterson, C .
NATURE CELL BIOLOGY, 2001, 3 (01) :93-96
[7]   Hsp90 potentiates the rapid evotution of new traits: Drug resistance in diverse fungi [J].
Cowen, LE ;
Lindquist, S .
SCIENCE, 2005, 309 (5744) :2185-2189
[8]   Harnessing Hsp90 function as a powerful, broadly effective therapeutic strategy for fungal infectious disease [J].
Cowen, Leah E. ;
Singh, Sheena D. ;
Koehler, Julia R. ;
Collins, Cathy ;
Zaas, Aimee K. ;
Schell, Wiley A. ;
Aziz, Hamza ;
Mylonakis, Eleftherios ;
Perfect, John R. ;
Whitesell, Luke ;
Lindquist, Susan .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2009, 106 (08) :2818-2823
[9]   FK506-binding protein 52 phosphorylation: A potential mechanism for regulating steroid hormone receptor activity [J].
Cox, Marc B. ;
Riggs, Daniel L. ;
Hessling, Martin ;
Schumacher, Felix ;
Buchner, Johannes ;
Smith, David F. .
MOLECULAR ENDOCRINOLOGY, 2007, 21 (12) :2956-2967
[10]   Functioning of the Hsp90 machine in chaperoning checkpoint kinase 1 (Chk1) and the progesterone receptor (PR) [J].
Felts, Sara J. ;
Karnitz, Larry M. ;
Toft, David O. .
CELL STRESS & CHAPERONES, 2007, 12 (04) :353-363
1234567