Stress and prions: Lessons from the yeast model

被引：67

作者：

Chernoff, Yury O. ^{[1
]}

机构：

[1] Georgia Inst Technol, Sch Biol, Atlanta, GA 30332 USA

[2] Georgia Inst Technol, Inst Bioengn & Biosci, Atlanta, GA 30332 USA

来源：

FEBS LETTERS | 2007年 / 581卷 / 19期

关键词：

amyloid; protein aggregation; chaperone; heat shock protein; ubiquitin; Saccharomyces cerevisiae; UBIQUITIN-PROTEASOME SYSTEM; SACCHAROMYCES-CEREVISIAE; HEAT-SHOCK; HSP104; CHAPERONE; AGGREGATION; PROPAGATION; PROTEINS; DISEASE; PSI+;

D O I：

10.1016/j.febslet.2007.04.075

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：

Yeast self-perpetuating amyloids (prions) provide a convenient model for studying the cellular control of highly ordered aggregates involved in mammalian protein assembly disorders. The very ability of an amyloid to propagate a prion state in yeast is determined by its interactions with the stress-inducible chaperone Hsp104. Prion formation and propagation are also influenced by other stress-related chaperones (Hsp70 and Hsp40), and by alterations of the protein trafficking and degradation networks. Some stress conditions induce prion formation or loss. It is proposed that prions arise as byproducts of the reversible assembly of highly ordered complexes, protecting certain proteins during unfavorable conditions. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：3695 / 3701

页数：7

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