title: 53BP1 Goes Back to Its p53 Roots.
abstract: In this issue of Molecular Cell, Cuella-Martin et al. (2016) revisit the role of 53BP1 in p53-dependent responses and find that these functions are separable from its widely known function in DNA repair.
authors.affiliation: The Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital and Department of Molecular Genetics, University of Toronto, Toronto, ON M5G 1X5, Canada. Electronic address: durocher@lunenfeld.ca.
authors.forename: Daniel
authors.initials: D
authors.lastname: Durocher
authors.affiliation: The Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital and Department of Molecular Genetics, University of Toronto, Toronto, ON M5G 1X5, Canada.
authors.forename: Laurence
authors.initials: L
authors.lastname: Pelletier
mesh_terms: D001665:Binding Sites; D002843:Chromatin / Q000737:chemistry / Q000378:metabolism; D053903:DNA Breaks, Double-Stranded; D004260:DNA Repair; D005786:Gene Expression Regulation; D006801:Humans; D061986:MCF-7 Cells; D011401:Promoter Regions, Genetic; D011485:Protein Binding; D055503:Protein Multimerization; D015398:Signal Transduction; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D000071857:Tumor Suppressor p53-Binding Protein 1 / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D043222:Ubiquitin Thiolesterase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism
chemical_list: D002843:Chromatin; C498301:TP53BP1 protein, human; D016159:Tumor Suppressor Protein p53; D000071857:Tumor Suppressor p53-Binding Protein 1; C442902:USP28 protein, human; D043222:Ubiquitin Thiolesterase