Breaking the chains: structure and function of the deubiquitinases

D Komander, MJ Clague, S Urbé - Nature reviews Molecular cell …, 2009 - nature.com
Nature reviews Molecular cell biology, 2009nature.com
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 …
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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