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The mechanism of OTUB1-mediated inhibition of ubiquitination

Author

Listed:
  • Reuven Wiener

    (Johns Hopkins University School of Medicine)

  • Xiangbin Zhang

    (Johns Hopkins University School of Medicine)

  • Tao Wang

    (Johns Hopkins University School of Medicine
    Present address: National Institute of Allergy and Infectious Diseases, Vaccine Research Center, 40 Convent Drive, Bethesda, Maryland 20892, USA)

  • Cynthia Wolberger

    (Johns Hopkins University School of Medicine)

Abstract

OTUB1 is an atypical deubiquitinating enzyme which prevents ubiquitin attachment and is important in the DNA damage pathway; structural analysis of OTUB1 in complex with an E2 ubiquitin-conjugating enzyme reveals that the ability of OTUB1 to inhibit ubiquitin chain synthesis is regulated by an allosteric feedback mechanism.

Suggested Citation

  • Reuven Wiener & Xiangbin Zhang & Tao Wang & Cynthia Wolberger, 2012. "The mechanism of OTUB1-mediated inhibition of ubiquitination," Nature, Nature, vol. 483(7391), pages 618-622, March.
    • Handle: RePEc:nat:nature:v:483:y:2012:i:7391:d:10.1038_nature10911
    DOI: 10.1038/nature10911
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