Polypeptide transfer from Hsp40 to Hsp70 molecular chaperones

被引：58
|
作者：
Summers, Daniel W. [1 ]
Douglas, Peter M. [1 ]
Ramos, Carlos H. I. [2 ]
Cyr, Douglas M. [1 ]
机构：
[1] Univ N Carolina, Dept Cell & Dev Biol, Chapel Hill, NC 27599 USA
[2] Univ Estadual Campinas, UNICAMP, Inst Chem, Dept Organ Chem, BR-13083970 Campinas, SP, Brazil
来源：
TRENDS IN BIOCHEMICAL SCIENCES | 2009年 / 34卷 / 05期
基金：
美国国家卫生研究院;
关键词：
ENDOPLASMIC-RETICULUM; ESCHERICHIA-COLI; PROTEINS; DNAJ; FARNESYLATION; DEGRADATION; BINDING; FAMILY; ATPASE;
D O I：
10.1016/j.tibs.2008.12.009
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：
Heat shock protein 40 (Hsp40) co-chaperones assist in cellular protein folding and degradation through the binding and delivery of non-native proteins to heat shock protein 70 (Hsp70). The mechanism for substrate transfer from Hsp40s to Hsp70 is unknown. Two recent studies provide new details that shed light on novel mechanisms for substrate recognition by Hsp40s and a common mechanism for polypeptide transfer to Hsp70.
引用
收藏
页码：230 / 233
页数：4
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