Cited by 1,396Ubiquitin and proteasome pathwaysProtein Degradation and InhibitorsEnzyme Structure and Function

Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes.

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Reyes-Turcu, Francisca E., Ventii, Karen H., Wilkinson, Keith D.·2009·Annual Review of Biochemistry

Abstract

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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Crossref · 10.1146/annurev.biochem.78.082307.091526

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  • The catalytic domains of all USPs possess a characteristic papain-like fold with a "thumb, palm, fingers" sub-domain architecture.

    “Despite differences in size, the catalytic domains of all USPs possess a characteristic papain-like fold with a “thumb, palm, fingers” sub-domain architecture (Reyes-Turcu et al., 2009)”

    From USP7 Is a Master Regulator of Genome Stability (2020) · cites this paper as Reyes-Turcu et al., 2009

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  1. [6]Fang S Weissman AM A field guide to ubiquitylation. Cell Mol Life Sci 2004 61 1546 61 15224180 PMC11138666

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Authors
Reyes-Turcu, F. E., Ventii, K. H., & Wilkinson, K. D.
Affiliations
  • Laboratory of Biochemistry and Molecular Biology, NCI, National Institutes of Health, Bethesda, Maryland 20892
  • Emory University (US)
Corresponding author
Wilkinson, Keith D.
Venue
Annual Review of Biochemistry
Published
2009-06-01
Volume
78
Issue
1
Pages
363-397
ISSN
  • 0066-4154 (ISSN-L)
  • 1545-4509
OpenAlex
W2139364069
Cited by
1,396
References
221
Citations by year
2026: 31 · 2025: 70 · 2024: 79 · 2023: 57 · 2022: 77 · 2021: 90 · 2020: 114 · 2019: 70 · 2018: 66 · 2017: 94 · 2016: 85 · 2015: 76 · 2014: 109 · 2013: 102 · 2012: 113
FWCI
6.96
Type
journal article
Language
en
Open access
Locations
  • Annual Review of Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Institute of General Medical Sciences (R01GM030308)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords
deubiquitinase, ubiquitin, ubiquitin-like proteins, polyubiquitin chains, protein-protein interaction
MeSH terms
Animals, Humans, Endopeptidases, Protein Structure, Tertiary, Ubiquitin, Ubiquitination

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