Deubiquitylating enzymes and disease

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 cell...

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Bibliographic Details
Published in:BMC biochemistry 2008-10, Vol.9 Suppl 1 (S1), p.S3-S3, Article S3
Main Authors: Singhal, Shweta, Taylor, Matthew C, Baker, Rohan T
Format: Article
Language:English
Subjects:
Animals
Endopeptidases - genetics
Endopeptidases - metabolism
Humans
Hydrolysis
Mutation
Neoplasms - enzymology
Neoplasms - metabolism
Review
Ubiquitin - metabolism
von Hippel-Lindau Disease - drug therapy
von Hippel-Lindau Disease - enzymology
von Hippel-Lindau Disease - metabolism
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Summary: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).
ISSN:1471-2091
1471-2091
DOI:10.1186/1471-2091-9-s1-s3