Activity-based ubiquitin-specific protease (USP) profiling of virus-infected and malignant human cells.
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.[1]References
- Activity-based ubiquitin-specific protease (USP) profiling of virus-infected and malignant human cells. Ovaa, H., Kessler, B.M., Rolén, U., Galardy, P.J., Ploegh, H.L., Masucci, M.G. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
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