PARTNER PROTEINS DETERMINE MULTIPLE FUNCTIONS OF HSP70

被引：133

作者：

RASSOW, J

VOOS, W

PFANNER, N

机构：

[1] Biochemisches Institut, Universität Freiburg, D-79104 Freiburg

来源：

TRENDS IN CELL BIOLOGY | 1995年 / 5卷 / 05期

关键词：

D O I：

10.1016/S0962-8924(00)89001-7

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The 70 kDa heat shock proteins (Hsp70s) are ubiquitous molecular chaperones that are best known for their participation in protein folding. However, evidence is accumulating that Hsp70s perform several other cellular functions in cooperation with specific soluble or membrane-bound partner proteins. While the basic function of Hsp70s is explained by their ability to bind unfolded polypeptide segments, the partner proteins appear to customize them for specific roles such as involvement in protein traffic and folding, translocation of preproteins across membranes, and gene regulation.

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页码：207 / 212

页数：6

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