Cited by 193Ubiquitin and proteasome pathwaysProtein Degradation and InhibitorsNF-κB Signaling Pathways

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Activity-based ubiquitin-specific protease (USP) profiling of virus-infected and malignant human cells

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Ovaa, Huib, Kessler, Benedikt M., Rolén, Ulrika, Galardy, Paul J., Ploegh, Hidde L., Masucci, Maria G.·2004·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0308411100PMC PMC356937

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Abstract

The family of ubiquitin (Ub)-specific proteases (USP) removes Ub from Ub conjugates and regulates a variety of cellular processes. The human genome contains many putative USP-encoding genes, but little is known about USP tissue distribution, pattern of expression, activity, and substrate specificity. We have used a chemistry-based functional proteomics approach to identify active USPs in normal, virus-infected, and tumor-derived human cells. Depending on tissue origin and stage of activation/differentiation, different USP activity profiles were revealed. The activity of specific USPs, including USP5, -7, -9, -13, -15, and -22, was up-regulated by mitogen activation or virus infection in normal T and B lymphocytes. UCH-L1 was highly expressed in tumor cell lines of epithelial and hematopoietic cell origin but was not detected in freshly isolated and mitogen-activated cells. Up-regulation of this USP was a late event in the establishment of Epstein–Barr virus-immortalized lymphoblastoid cell lines and correlated with enhanced proliferation, suggesting a possible role in growth transformation.

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Authors: Ovaa, H., Kessler, B. M., Rolén, U., Galardy, P. J., Ploegh, H. L., & Masucci, M. G.
Affiliations: Harvard University (US)
Corresponding author: Masucci, Maria G.
ORCID: Ovaa, Huib
Kessler, Benedikt M.
Galardy, Paul J.
Ploegh, Hidde L.
Masucci, Maria G.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2004-02-11
Volume: 101
Issue: 8
Pages: 2253-2258
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.0308411100
PMC: PMC356937
OpenAlex: W2130935241
Cited by: 190
References: 49
Citations by year: 2026: 1 · 2025: 3 · 2024: 2 · 2023: 6 · 2022: 8 · 2021: 5 · 2020: 5 · 2019: 11 · 2018: 7 · 2017: 6 · 2016: 8 · 2015: 7 · 2014: 13 · 2013: 7 · 2012: 9
FWCI: 4.03
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Multiple Myeloma Research Foundation
Stiftelsen för Strategisk Forskning
Cancerfonden
Karolinska Institutet
National Institutes of Health
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 › Cancer Research › NF-κB Signaling Pathways
Keywords: ubiquitin-specific protease, deubiquitination, virus-infected cells, cancer cell lines, Epstein-Barr virus, UCHL1, USP5, USP7, USP13, USP15, USP22, lymphocyte activation, mitogen stimulation, cell proliferation, growth transformation, functional proteomics
MeSH terms: Ubiquitin-Specific Peptidase 7, B-Lymphocytes, Cell Line, Humans, Endopeptidases, Mass Spectrometry, T-Lymphocytes, Ubiquitin Thiolesterase, Cell Line, Tumor, Ubiquitin-Specific Proteases

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Activity-based ubiquitin-specific protease (USP) profiling of virus-infected and malignant human cells

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