Molecular chaperones and protein quality control

被引：1262

作者：

Bukau, Bernd

Weissman, Jonathan

Horwich, Arthur

机构：

[1] Heidelberg Univ, Zentrum Mol Biol, D-69120 Heidelberg, Germany

[2] Univ Calif San Francisco, Dept Cellular & Mol Pharmacol, San Francisco, CA 94143 USA

[3] Univ Calif San Francisco, Howard Hughes Med Inst, San Francisco, CA 94143 USA

[4] Scripps Res Inst, La Jolla, CA 92037 USA

[5] Yale Univ, Sch Med, Howard Hughes Med Inst, New Haven, CT 06510 USA

[6] Yale Univ, Sch Med, Dept Genet, New Haven, CT 06510 USA

来源：

CELL | 2006年 / 125卷 / 03期

关键词：

D O I：

10.1016/j.cell.2006.04.014

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：

In living cells, both newly made and preexisting polypeptide chains are at constant risk for misfolding and aggregation. In accordance with the wide diversity of misfolded forms, elaborate quality-control strategies have evolved to counter these inevitable mishaps. Recent reports describe the removal of aggregates from the cytosol; reveal mechanisms for protein quality control in the endoplasmic reticulum; and provide new insight into two classes of molecular chaperones, the Hsp70 system and the AAA+ (Hsp100) unfoldases. © 2006 Elsevier Inc. All rights reserved.

引用

收藏

页码：443 / 451

页数：9

相关论文

共 48 条

[1] Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death [J].

Arrasate, M ;

Mitra, S ;

Schweitzer, ES ;

Segal, MR ;

Finkbeiner, S .

NATURE, 2004, 431 (7010) :805-810

[2] Impairment of the ubiquitin-proteasome system by protein aggregation [J].

Bence, NF ;

Sampat, RM ;

Kopito, RR .

SCIENCE, 2001, 292 (5521) :1552-1555

[3] Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation [J].

Bennett, EJ ;

Bence, NF ;

Jayakumar, R ;

Kopito, RR .

MOLECULAR CELL, 2005, 17 (03) :351-365

[4] p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death [J].

Bjorkoy, G ;

Lamark, T ;

Brech, A ;

Outzen, H ;

Perander, M ;

Overvatn, A ;

Stenmark, H ;

Johansen, T .

JOURNAL OF CELL BIOLOGY, 2005, 171 (04) :603-614

[5] Yos9p: A sweet-toothed bouncer of the secretory pathway [J].

Cormier, JH ;

Pearse, BR ;

Hebert, DN .

MOLECULAR CELL, 2005, 19 (06) :717-719

[6] On the mechanism of sensing unfolded protein in the endoplasmic reticulum [J].

Credle, JJ ;

Finer-Moore, JS ;

Papa, FR ;

Stroud, RM ;

Walter, P .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (52) :18773-18784

[7] Nucleotide dependent motion and mechanism of action of p97/VCP [J].

DeLaBarre, B ;

Brunger, AT .

JOURNAL OF MOLECULAR BIOLOGY, 2005, 347 (02) :437-452

[8] Quality control in the endoplasmic reticulum [J].

Ellgaard, L ;

Helenius, A .

NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2003, 4 (03) :181-191

[9] Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen [J].

Gai', DH ;

Zhao, R ;

Li, DW ;

Finkielstein, CV ;

Chen, XS .

CELL, 2004, 119 (01) :47-60

[10] RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin [J].

Gautschi, M ;

Lilie, H ;

Fünfschilling, U ;

Mun, A ;

Ross, S ;

Lithgow, T ;

Rücknagel, P ;

Rospert, S .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (07) :3762-3767

← 1 2 3 4 5 →