Unraveling the CHIP:Hsp70 complex as an information processor for protein quality control

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• 作者：Jamie VanPelt ; Richard C. Page ; ^{pagerc@miamioh.edu}
• 关键词：Protein quality control ; Ubiquitination ; Protein refolding ; Allostery ; Dynamics
• 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：1865
• 期：2
• 页码：133-141
• 全文大小：1295 K
• 卷排序：1865

文摘

The CHIP:Hsp70 complex stands at the crossroads of the cellular protein quality control system. Hsp70 facilitates active refolding of misfolded client proteins, while CHIP directs ubiquitination of misfolded client proteins bound to Hsp70. The direct competition between CHIP and Hsp70 for the fate of misfolded proteins leads to the question: how does the CHIP:Hsp70 complex execute triage decisions that direct misfolded proteins for either refolding or degradation? The current body of literature points toward action of the CHIP:Hsp70 complex as an information processor that takes inputs in the form of client folding state, dynamics, and posttranslational modifications, then outputs either refolded or ubiquitinated client proteins. Herein we examine the CHIP:Hsp70 complex beginning with the structure and function of CHIP and Hsp70, followed by an examination of recent studies of the interactions and dynamics of the CHIP:Hsp70 complex.