A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins.
A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins.
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DOI：
10.1016/j.str.2015.01.003
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发表时间：
2015-03-03
期刊：
影响因子：
5.7
通讯作者：
Page, Richard C.
中科院分区：
文献类型：
--
作者：
Zhang, Huaqun;Amick, Joseph;Chakravarti, Ritu;Santarriaga, Stephanie;Schlanger, Simon;McGlone, Cameron;Dare, Michelle;Nix, Jay C.;Scaglione, K. Matthew;Stuehr, Dennis J.;Misra, Saurav;Page, Richard C.
The ubiquitin ligase CHIP plays an important role in cytosolic protein quality control by ubiquitinating proteins chaperoned by Hsp70/Hsc70 and Hsp90, thereby targeting such substrate proteins for degradation. We present a 2.91 Å resolution structure of the TPR domain of CHIP in complex with the α-helical “lid” subdomain and unstructured “tail” of Hsc70. Surprisingly, the CHIP-TPR interacts with determinants within both the Hsc70-lid subdomain and the C-terminal PTIEEVD motif of the tail, exhibiting a novel mode of interaction between chaperones and TPR domains. We demonstrate that the interaction between CHIP and the Hsc70-lid subdomain is required for proper ubiquitination of Hsp70/Hsc70 or Hsp70/Hsc70-bound substrate proteins. Post-translational modifications of the Hsc70 lid and tail disrupt key contacts with the CHIP-TPR and may regulate CHIP-mediated ubiquitination. Our study shows how CHIP docks onto Hsp70/Hsc70 and defines a new bipartite mode of interaction between TPR domains and their binding partners.
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DOI：
10.1107/s0907444905036693
发表时间：
2006-01-01
影响因子：
2.2
作者：
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通讯作者：
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影响因子：
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影响因子：
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通讯作者：
--
影响因子：
4.8
作者：
Chakravarti, Ritu;Stuehr, Dennis J.
通讯作者：
Stuehr, Dennis J.