A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins.


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 tetratricopeptide repeat (TPR) domain of CHIP in complex with the α-helical lid subdomain and… (More)
DOI: 10.1016/j.str.2015.01.003

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