Cooperation of molecular chaperones with the ubiquitin/proteasome system

被引：183

作者：

Esser, C

Alberti, S

Höhfeld, J

机构：

[1] Univ Bonn, Inst Zellbiol, Ulrich Haberland Str 61A, D-53121 Bonn, Germany

[2] Univ Bonn, Bonner Forum Biomed, D-53121 Bonn, Germany

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2004年 / 1695卷 / 1-3期

关键词：

molecular chaperone; ubiquitin/proteasome system; folding;

D O I：

10.1016/j.bbamcr.2004.09.020

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：

Molecular chaperones and energy-dependent proteases have long been viewed as opposing forces that control protein biogenesis. Molecular chaperones are specialized in protein folding, whereas energy-dependent proteases such as the proteasome mediate efficient protein degradation. Recent data, however, suggest that molecular chaperones directly cooperate with the ubiquicin/proteasorne system during protein quality control in eukaryotic cells. Modulating the intracellular balance of protein folding and protein degradation may open new strategies for the treatment of human diseases that involve chaperone pathways such as cancer and diverse amyloid diseases. (C) 2004 Elsevier B.V. All rights reserved.

引用

页码：171 / 188

页数：18

共 141 条

[1] The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator [J].