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BMC Biochem. 2008 Oct 21;9 Suppl 1:S3. doi: 10.1186/1471-2091-9-S1-S3.

Deubiquitylating enzymes and disease.

Author information

1
Ubiquitin Laboratory, Division of Molecular Bioscience, The John Curtin School of Medical Research, The Australian National University, Canberra, ACT 0200, Australia. Shweta.Singhal@anu.edu.au

Abstract

Deubiquitylating enzymes (DUBs) can hydrolyze a peptide, amide, ester or thiolester bond at the C-terminus of UBIQ (ubiquitin), including the post-translationally formed branched peptide bonds in mono- or multi-ubiquitylated conjugates. DUBs thus have the potential to regulate any UBIQ-mediated cellular process, the two best characterized being proteolysis and protein trafficking. Mammals contain some 80-90 DUBs in five different subfamilies, only a handful of which have been characterized with respect to the proteins that they interact with and deubiquitylate. Several other DUBs have been implicated in various disease processes in which they are changed by mutation, have altered expression levels, and/or form part of regulatory complexes. Specific examples of DUB involvement in various diseases are presented. While no specific drugs targeting DUBs have yet been described, sufficient functional and structural information has accumulated in some cases to allow their rapid development. PUBLICATION HISTORY : Republished from Current BioData's Targeted Proteins database (TPdb; http://www.targetedproteinsdb.com).

PMID:
19007433
PMCID:
PMC2582804
DOI:
10.1186/1471-2091-9-S1-S3
[Indexed for MEDLINE]
Free PMC Article

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