Breaking the chains: structure and function of the deubiquitinases - PubMed (original) (raw)

Review

doi: 10.1038/nrm2731.

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• PMID: 19626045
• DOI: 10.1038/nrm2731

Review

Breaking the chains: structure and function of the deubiquitinases

David Komander et al. Nat Rev Mol Cell Biol. 2009 Aug.

Abstract

Ubiquitylation is a reversible protein modification that is implicated in many cellular functions. Recently, much progress has been made in the characterization of a superfamily of isopeptidases that remove ubiquitin: the deubiquitinases (DUBs; also known as deubiquitylating or deubiquitinating enzymes). Far from being uniform in structure and function, these enzymes display a myriad of distinct mechanistic features. The small number (<100) of DUBs might at first suggest a low degree of selectivity; however, DUBs are subject to multiple layers of regulation that modulate both their activity and their specificity. Due to their wide-ranging involvement in key regulatory processes, these enzymes might provide new therapeutic targets.

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