The remarkable multivalency of the Hsp70 chaperones

被引：0
|
作者：
Erik R. P. Zuiderweg
Lawrence E. Hightower
Jason E. Gestwicki
机构：
[1] The University of Michigan Medical School,Department of Biological Chemistry
[2] University of Connecticut,Department of Molecular and Cell Biology
[3] University of California at San Francisco,Institute for Neurodegenerative Disease
来源：
Cell Stress and Chaperones | 2017年 / 22卷
关键词：
Hsc70; Protein-protein interactions; Protein-drug interactions; Structural biology; Crystallography; NMR spectroscopy;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
Hsp70 proteins are key to maintaining intracellular protein homeostasis. To carry out this task, they employ a large number of cochaperones and adapter proteins. Here, we review what is known about the interaction between the chaperones and partners, with a strong slant toward structural biology. Hsp70s in general, and Hsc70 (HSPA8) in particular, display an amazing array of interfaces with their protein cofactors. We also review the known interactions between Hsp70s with lipids and with active compounds that may become leads toward Hsp70 modulation for treatment of a variety of diseases.
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收藏
页码：173 / 189
页数：16
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