USP14 deubiquitinates proteasome-bound substrates that are ubiquitinated at multiple sites

Byung-Hoon Lee (), Ying Lu, Miguel A. Prado, Yuan Shi, Geng Tian, Shuangwu Sun, Suzanne Elsasser, Steven P. Gygi, Randall W. King () and Daniel Finley ()
Additional contact information
Byung-Hoon Lee: Harvard Medical School
Ying Lu: Harvard Medical School
Miguel A. Prado: Harvard Medical School
Yuan Shi: Harvard Medical School
Geng Tian: Harvard Medical School
Shuangwu Sun: Harvard Medical School
Suzanne Elsasser: Harvard Medical School
Steven P. Gygi: Harvard Medical School
Randall W. King: Harvard Medical School
Daniel Finley: Harvard Medical School

Nature, 2016, vol. 532, issue 7599, 398-401

Abstract: The proteasome-associated enzyme USP14 regulates protein degradation by removing ubiquitin from proteins; here it is shown that USP14 removes ubiquitin chains from in vitro generated cyclin B conjugates en bloc and within milliseconds, before the proteasome has a chance to initiate degradation, and proceeds until a single chain remains.

Date: 2016
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DOI: 10.1038/nature17433

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