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      Deubiquitinases and the new therapeutic opportunities offered to cancer

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      Author(s): , ,
      Publication date (Print):
      Journal: Endocrine-Related Cancer
      Publisher: Bioscientifica Ltd
      Keywords: deubiquitinases, USP7, USP22, CYLD, UCHL1, BAP1, A20, ataxin 3

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          Abstract

          Deubiquitinases (DUBs) play important roles and therefore are potential drug targets in various diseases including cancer and neurodegeneration. In this review, we recapitulate structure–function studies of the most studied DUBs including USP7, USP22, CYLD, UCHL1, BAP1, A20, as well as ataxin 3 and connect them to regulatory mechanisms and their growing protein interaction networks. We then describe DUBs that have been associated with endocrine carcinogenesis with a focus on prostate, ovarian, and thyroid cancer, pheochromocytoma, and adrenocortical carcinoma. The goal is enhancing our understanding of the connection between dysregulated DUBs and cancer to permit the design of therapeutics and to establish biomarkers that could be used in diagnosis and prognosis.

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          A genomic and functional inventory of deubiquitinating enzymes.

          Sebastian M.B. Nijman, Mark P.A. Luna-Vargas, Arno Velds … (2005)
          Posttranslational modification of proteins by the small molecule ubiquitin is a key regulatory event, and the enzymes catalyzing these modifications have been the focus of many studies. Deubiquitinating enzymes, which mediate the removal and processing of ubiquitin, may be functionally as important but are less well understood. Here, we present an inventory of the deubiquitinating enzymes encoded in the human genome. In addition, we review the literature concerning these enzymes, with particular emphasis on their function, specificity, and the regulation of their activity.
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            Histone H2A deubiquitinase activity of the Polycomb repressive complex PR-DUB.

            Johanna C Scheuermann, Andrés Gaytán de Ayala Alonso, Katarzyna Oktaba … (2010)
            Polycomb group (PcG) proteins are transcriptional repressors that control processes ranging from the maintenance of cell fate decisions and stem cell pluripotency in animals to the control of flowering time in plants. In Drosophila, genetic studies identified more than 15 different PcG proteins that are required to repress homeotic (HOX) and other developmental regulator genes in cells where they must stay inactive. Biochemical analyses established that these PcG proteins exist in distinct multiprotein complexes that bind to and modify chromatin of target genes. Among those, Polycomb repressive complex 1 (PRC1) and the related dRing-associated factors (dRAF) complex contain an E3 ligase activity for monoubiquitination of histone H2A (refs 1-4). Here we show that the uncharacterized Drosophila PcG gene calypso encodes the ubiquitin carboxy-terminal hydrolase BAP1. Biochemically purified Calypso exists in a complex with the PcG protein ASX, and this complex, named Polycomb repressive deubiquitinase (PR-DUB), is bound at PcG target genes in Drosophila. Reconstituted recombinant Drosophila and human PR-DUB complexes remove monoubiquitin from H2A but not from H2B in nucleosomes. Drosophila mutants lacking PR-DUB show a strong increase in the levels of monoubiquitinated H2A. A mutation that disrupts the catalytic activity of Calypso, or absence of the ASX subunit abolishes H2A deubiquitination in vitro and HOX gene repression in vivo. Polycomb gene silencing may thus entail a dynamic balance between H2A ubiquitination by PRC1 and dRAF, and H2A deubiquitination by PR-DUB.
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              Ubiquitin-dependent protein degradation.

              M. Hochstrasser (1996)
              A growing number of cellular regulatory mechanisms are being linked to protein modification by the polypeptide ubiquitin. These include key transitions in the cell cycle, class I antigen processing, signal transduction pathways, and receptor-mediated endocytosis. In most, but not all, of these examples, ubiquitination of a protein leads to its degradation by the 26S proteasome. Following attachment of ubiquitin to a substrate and binding of the ubiquitinated protein to the proteasome, the bound substrate must be unfolded (and eventually deubiquitinated) and translocated through a narrow set of channels that leads to the proteasome interior, where the polypeptide is cleaved into short peptides. Protein ubiquitination and deubiquitination are both mediated by large enzyme families, and the proteasome itself comprises a family of related but functionally distinct particles. This diversity underlies both the high substrate specificity of the ubiquitin system and the variety of regulatory mechanisms that it serves.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Endocr Relat Cancer
                Journal ID (iso-abbrev): Endocr. Relat. Cancer
                Journal ID (publisher-id): ERC
                Title: Endocrine-Related Cancer
                Publisher: Bioscientifica Ltd (Bristol )
                ISSN (Print): 1351-0088
                ISSN (Electronic): 1479-6821
                Publication date (Print): February 2015
                Volume: 22
                Issue: 1
                Pages: T35-T54
                Affiliations
                [1]Department of Biology, York University , 4700 Keele Street, Toronto, Ontario, Canada, M3J1P3
                Author notes
                Correspondence should be addressed to V Saridakis vsaridak@ 123456yorku.ca
                Article
                Publisher ID: ERC140516
                DOI: 10.1530/ERC-14-0516
                PMC ID: 4304536
                PubMed ID: 25605410
                SO-VID: 5d003942-64df-4397-a6cf-da465bc63828
                Copyright © © 2015 The authors
                License:

                This work is licensed under a Creative Commons Attribution 3.0 Unported License

                History
                Date revision received : 22 December 2014
                Date accepted : 23 December 2014
                Categories
                Subject: Thematic Review

                ScienceOpen disciplines: Oncology & Radiotherapy
                Keywords: deubiquitinases,usp7,usp22,cyld,uchl1,bap1,a20,ataxin 3
                Data availability:
                ScienceOpen disciplines: Oncology & Radiotherapy
                Keywords: deubiquitinases, usp7, usp22, cyld, uchl1, bap1, a20, ataxin 3

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