Higher -Order Assembly of BRCC36–KIAA0157 Is Required for DUB Activity and Biological Function

@inproceedings{Zeqiraj2015HigherA,
  title={Higher -Order Assembly of BRCC36–KIAA0157 Is Required for DUB Activity and Biological Function},
  author={Elton Zeqiraj and Lei Tian and Christopher A. Piggott and Monica C. Pillon and Nicole M. Duffy and Derek F.J. Ceccarelli and Alexander F. A. Keszei and Kristina Lorenzen and Igor Kurinov and Stephen M Orlicky and Gerald D. Gish and Albert J. R. Heck and Alba Guarn{\'e} and Roger A. Greenberg and Frank Sicheri},
  booktitle={Molecular cell},
  year={2015}
}
BRCC36 is a Zn(2+)-dependent deubiquitinating enzyme (DUB) that hydrolyzes lysine-63-linked ubiquitin chains as part of distinct macromolecular complexes that participate in either interferon signaling or DNA-damage recognition. The MPN(+) domain protein BRCC36 associates with pseudo DUB MPN(-) proteins KIAA0157 or Abraxas, which are essential for BRCC36 enzymatic activity. To understand the basis for BRCC36 regulation, we have solved the structure of an active BRCC36-KIAA0157 heterodimer and… CONTINUE READING
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Crystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11

  • G. R. Pathare, I. Nagy, +7 authors W. Baumeister
  • Proc. Natl. Acad. Sci. USA
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