Deubiquitylating enzymes and disease - PubMed (original) (raw)

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Deubiquitylating enzymes and disease

Shweta Singhal et al. BMC Biochem. 2008.

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).

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References

1. 1. Baker RT, Tobias JT, Varshavsky A. Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family. J Biol Chem. 1992;267:23364–23375. - PubMed
2. 1. Matsui S, Sandberg AA, Negoro S, Seon BK, Goldstein G. Isopeptidase: a novel eukaryotic enzyme that cleaves isopeptide bonds. Proc Natl Acad Sci USA. 1982;79:1535–1539. doi: 10.1073/pnas.79.5.1535. - DOI - PMC - PubMed
3. 1. Pickart CM, Rose IA. Ubiquitin carboxyl-terminal hydrolase acts on ubiquitin carboxyl-terminal amides. J Biol Chem. 1985;260:7903–7910. - PubMed
4. 1. Mayer AN, Wilkinson KD. Detection, resolution, and nomenclature of multiple ubiquitin carboxyl-terminal esterases from bovine calf thymus. Biochemistry. 1989;28:166–172. doi: 10.1021/bi00427a024. - DOI - PubMed
5. 1. Amerik AY, Hochstrasser M. Mechanism and function of deubiquitinating enzymes. Biochim Biophys Acta. 2004;1695:189–207. doi: 10.1016/j.bbamcr.2004.10.003. - DOI - PubMed

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