title: The role of PRDMs in cancer: one family, two sides.
abstract: The PRDM family of proteins share a unique structure, with an N-terminal PR domain, which has a potential methyltransferase activity, followed by a distinct number of zinc fingers at the C-terminus, potentially mediating protein-protein, protein-RNA or protein-DNA interactions. Interestingly, despite no comprehensive functional data, all family members have been associated with deletions, mutations, epigenetic silencing or overexpression, in multiple cancer types. The intriguing observation is that different isoforms exist for almost all PRDM family members. These isoforms are not only differentially regulated, but play opposite roles in cancer, in what has been termed 'Yin and Yang' regulation, typical of this class of epigenetic regulators. Collectively, these findings set the stage for future intervention, by targeting directly their intrinsic catalytic activities, or indirectly, pathways that differentially regulate tumor suppressor/oncogenic isoform-expression.
authors.affiliation: Institute of Molecular and Cell Biology (IMCB), A*STAR (Agency for Science, Technology and Research), 61 Biopolis Drive, Proteos Building #3-06, 138673 Singapore, Singapore; Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, 8 Medical Drive, Singapore 117597, Singapore.
authors.forename: Slim
authors.initials: S
authors.lastname: Mzoughi
authors.affiliation: Institute of Molecular and Cell Biology (IMCB), A*STAR (Agency for Science, Technology and Research), 61 Biopolis Drive, Proteos Building #3-06, 138673 Singapore, Singapore.
authors.forename: Ying Xim
authors.initials: YX
authors.lastname: Tan
authors.affiliation: Institute of Molecular and Cell Biology (IMCB), A*STAR (Agency for Science, Technology and Research), 61 Biopolis Drive, Proteos Building #3-06, 138673 Singapore, Singapore.
authors.forename: Diana
authors.initials: D
authors.lastname: Low
authors.affiliation: Institute of Molecular and Cell Biology (IMCB), A*STAR (Agency for Science, Technology and Research), 61 Biopolis Drive, Proteos Building #3-06, 138673 Singapore, Singapore; Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, 8 Medical Drive, Singapore 117597, Singapore; National Cancer Centre Singapore, 11 Hospital Drive, Singapore 169610, Singapore. Electronic address: eguccione@imcb.a-star.edu.sg.
authors.forename: Ernesto
authors.initials: E
authors.lastname: Guccione
mesh_terms: D004268:DNA-Binding Proteins / Q000235:genetics; D015972:Gene Expression Regulation, Neoplastic / Q000235:genetics; D006801:Humans; D005810:Multigene Family / Q000235:genetics; D009369:Neoplasms / Q000235:genetics*; D000074462:Positive Regulatory Domain I-Binding Factor 1; D060066:Protein Interaction Maps / Q000235:genetics*; D000071376:RNA-Binding Motifs / Q000235:genetics; D012097:Repressor Proteins / Q000235:genetics*
chemical_list: D004268:DNA-Binding Proteins; D012097:Repressor Proteins; C087042:PRDM1 protein, human; D000074462:Positive Regulatory Domain I-Binding Factor 1