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Activity-based ubiquitin-specific protease (USP) profiling of virus-infected and malignant human cells
Open accessAbstract
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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“Unique DUB activity was additionally identified following EBV establishment of latency and correlated with changes in cell proliferation rates.”
From The Impact of Mass Spectrometry–Based Proteomics on Fundamental Discoveries in Virology (2014) · cites this paper as [145]
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“By using AP of active DUBs and MS analysis, the activities of several DUBs were found to be strongly upregulated in EBV-infected lymphocytes (145).”
From The Impact of Mass Spectrometry–Based Proteomics on Fundamental Discoveries in Virology (2014) · cites this paper as [145]
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Metadata
- 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.
- 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
- 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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