Journal
ANNUAL REVIEW OF BIOCHEMISTRY
Volume 78, Issue -, Pages 363-397Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev.biochem.78.082307.091526
Keywords
cell cycle; DNA damage; endocytosis; histone; proteasome; signal transduction
Categories
Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM030308] Funding Source: NIH RePORTER
- NIGMS NIH HHS [R01 GM030308-27, R01 GM030308] Funding Source: Medline
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Deubiquitinating enzymes (DUBs) are proteases that process ubiquitin or ubiquitin-like gene products, reverse the modification of proteins by a single ubiquitin(-like) protein, and remodel polyubiquitin(-like) chains on target proteins. The human genome encodes nearly 100 DUBs with specificity for ubiquitin in five gene families. Most DUB activity is cryptic, and conformational rearrangements often occur during the binding of ubiquitin and/or scaffold proteins. DUBs with specificity for ubiquitin contain insertions and extensions modulating DUB substrate specificity, protein-protein interactions, and Cellular localization. Binding partners and multiprotein complexes with which DUBs associate Modulate DUB activity and substrate specificity. Quantitative studies of activity and protein-protein interactions, together with genetic studies and the advent of RNAi, have led to new insights into the function of yeast and human DUBs. This review discusses ubiquitin-specific DUBs, some of the generalizations emerging from recent studies of the regulation of DUB activity, and their roles in various cellular processes.
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