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

Paul A. DaRosa, Zhizhi Wang, Xiaomo Jiang, Jonathan N. Pruneda, Feng Cong, Rachel E. Klevit () and Wenqing Xu ()
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Paul A. DaRosa: University of Washington
Zhizhi Wang: University of Washington
Xiaomo Jiang: Novartis Institutes for Biomedical Research
Jonathan N. Pruneda: University of Washington
Feng Cong: Novartis Institutes for Biomedical Research
Rachel E. Klevit: University of Washington
Wenqing Xu: University of Washington

Nature, 2015, vol. 517, issue 7533, 223-226

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.

Date: 2015
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DOI: 10.1038/nature13826

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