Breaking the chains: structure and function of the deubiquitinases.
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.
Komander
David
D
Medical Research Council, Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 0QH, UK. dk@mrc-lmb.cam.ac.uk
Clague
Michael J
MJ
Urbé
Sylvie
S
D000818:Animals; D055162:Biocatalysis; D010450:Endopeptidases / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D013379:Substrate Specificity
D010450:Endopeptidases