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

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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

DOI 10.1146/annurev.biochem.78.082307.091526PMC PMC2734102

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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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A sensitive fluorescence intensity assay for deubiquitinating proteases using ubiquitin-rhodamine110-glycine as substrate
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ChlaDub1 ofChlamydia trachomatissuppresses NF-κB activation and inhibits IκBα ubiquitination and degradation
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DUB-2 Is a Member of a Novel Family of Cytokine-inducible Deubiquitinating Enzymes
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The CAP-Gly Domain of CYLD Associates with the Proline-Rich Sequence in NEMO/IKKγ
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14-3-3-dependent inhibition of the deubiquitinating activity of UBPY and its cancellation in the M phase
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Role of Bmi1 in H2A Ubiquitylation and Hox Gene Silencing
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Identification and Characterization of a Drosophila Proteasome Regulatory Network
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See all 1,396

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
Publisher: Annual Reviews
Published: 2009-06-01
Volume: 78
Issue: 1
Pages: 363-397
ISSN: 0066-4154 (ISSN-L)
1545-4509
DOI: 10.1146/annurev.biochem.78.082307.091526
PMC: PMC2734102
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: green
www.ncbi.nlm.nih.gov
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
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › 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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Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes.

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