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

Author

Listed:
  • Byung-Hoon Lee

    (Harvard Medical School)

  • Ying Lu

    (Harvard Medical School)

  • Miguel A. Prado

    (Harvard Medical School)

  • Yuan Shi

    (Harvard Medical School
    † Present address: Department of Molecular and Clinical Pharmacology, Factor 10-638, 650 Charles E. Young Drive South, University of Los Angeles, Los Angeles, California 90095, USA.)

  • Geng Tian

    (Harvard Medical School)

  • Shuangwu Sun

    (Harvard Medical School
    Life Sciences Institute, Zhejiang University)

  • Suzanne Elsasser

    (Harvard Medical School)

  • Steven P. Gygi

    (Harvard Medical School)

  • Randall W. King

    (Harvard Medical School)

  • Daniel Finley

    (Harvard Medical School)

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.

Suggested Citation

  • Byung-Hoon Lee & Ying Lu & Miguel A. Prado & Yuan Shi & Geng Tian & Shuangwu Sun & Suzanne Elsasser & Steven P. Gygi & Randall W. King & Daniel Finley, 2016. "USP14 deubiquitinates proteasome-bound substrates that are ubiquitinated at multiple sites," Nature, Nature, vol. 532(7599), pages 398-401, April.
    • Handle: RePEc:nat:nature:v:532:y:2016:i:7599:d:10.1038_nature17433
    DOI: 10.1038/nature17433
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    Cited by:

    1. Xiangwei Wu & Yunxiang Du & Lu-Jun Liang & Ruichao Ding & Tianyi Zhang & Hongyi Cai & Xiaolin Tian & Man Pan & Lei Liu, 2024. "Structure-guided engineering enables E3 ligase-free and versatile protein ubiquitination via UBE2E1," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    2. Ka Ying Sharon Hung & Sven Klumpe & Markus R. Eisele & Suzanne Elsasser & Geng Tian & Shuangwu Sun & Jamie A. Moroco & Tat Cheung Cheng & Tapan Joshi & Timo Seibel & Duco Dalen & Xin-Hua Feng & Ying L, 2022. "Allosteric control of Ubp6 and the proteasome via a bidirectional switch," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    3. Dongni Shi & Xianqiu Wu & Yunting Jian & Junye Wang & Chengmei Huang & Shuang Mo & Yue Li & Fengtian Li & Chao Zhang & Dongsheng Zhang & Huizhong Zhang & Huilin Huang & Xin Chen & Y. Alan Wang & Chuyo, 2022. "USP14 promotes tryptophan metabolism and immune suppression by stabilizing IDO1 in colorectal cancer," Nature Communications, Nature, vol. 13(1), pages 1-18, December.

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