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Allosteric activation of the RNF146 ubiquitin ligase by a poly(ADP-ribosyl)ation signal

Author

Listed:
  • Paul A. DaRosa

    (University of Washington
    University of Washington)

  • Zhizhi Wang

    (University of Washington)

  • Xiaomo Jiang

    (Novartis Institutes for Biomedical Research)

  • Jonathan N. Pruneda

    (University of Washington
    Present address: Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.)

  • Feng Cong

    (Novartis Institutes for Biomedical Research)

  • Rachel E. Klevit

    (University of Washington)

  • Wenqing Xu

    (University of Washington)

Abstract

Structural and biochemical approaches are used to show how RNF146 activity is allosterically regulated by the binding of poly(ADP-ribose) ligand, and how substrate specificity is achieved with protein poly(ADP-ribosyl)ation and ubiquitination occurring in the same protein complex.

Suggested Citation

  • Paul A. DaRosa & Zhizhi Wang & Xiaomo Jiang & Jonathan N. Pruneda & Feng Cong & Rachel E. Klevit & Wenqing Xu, 2015. "Allosteric activation of the RNF146 ubiquitin ligase by a poly(ADP-ribosyl)ation signal," Nature, Nature, vol. 517(7533), pages 223-226, January.
    • Handle: RePEc:nat:nature:v:517:y:2015:i:7533:d:10.1038_nature13826
    DOI: 10.1038/nature13826
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