CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70

Shu-Bing Qian, Holly McDonough, Frank Boellmann, Douglas M. Cyr and Cam Patterson ()
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Shu-Bing Qian: Carolina Cardiovascular Biology Center
Holly McDonough: Carolina Cardiovascular Biology Center
Frank Boellmann: Carolina Cardiovascular Biology Center
Douglas M. Cyr: University of North Carolina
Cam Patterson: Carolina Cardiovascular Biology Center

Nature, 2006, vol. 440, issue 7083, 551-555

Abstract: CHIP — a co-chaperone/ubiquitin ligase — not only targets chaperone substrates for degradation, but mediates Hsp70 turnover after misfolded substrates have been depleted. The sequential catalysis of the CHIP-associated chaperone adaptor and its bound substrate provides a mechanism for maintaining homeostasis by tuning chaperone levels appropriately to reflect the status of protein folding within the cytoplasm.

Date: 2006
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DOI: 10.1038/nature04600

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