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PMID: 19626045 Published · ppublish English Journal Article Review

Breaking the chains: structure and function of the deubiquitinases.

Nature reviews. Molecular cell biology ·Vol. 10 ·No. 8 ·2009-08-00 ·Pages 550-63

Komander D, Clague MJ, Urbé S

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.

MeSH Terms
Animals Biocatalysis Endopeptidases/chemistry,metabolism Humans Substrate Specificity
Chemicals
Endopeptidases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Komander David
Medical Research Council, Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 0QH, UK. dk@mrc-lmb.cam.ac.uk
Clague Michael J
Urbé Sylvie
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Article Info
Journal
Nature reviews. Molecular cell biology
Abbr.
Nat Rev Mol Cell Biol
ISSN
1471-0080
Published
2009-08-00
Pages
550-63
Language
English
Region
England
NLM ID
100962782
Subset
IM
Grants
Medical Research Council · MC_U105192732 · United Kingdom
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