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The p53 isoforms are differentially modified by Mdm2
Authors:Suzanne Camus  Sergio Menéndez  Kenneth Fernandes  Nelly Kua  Geng Liu  Dimitris P Xirodimas  David P Lane  Jean-Christophe Bourdon
Institution:1.Institute of Molecular and Cell Biology; Singapore;2.University of Dundee; College of Medicine; Centre for Oncology and Molecular Medicine; Dundee, UK;3.Centre de Recherche de Biochimie Macromoléculaire - UMR 5237; CNRS; Montpellier, France
Abstract:The discovery that the single p53 gene encodes several different p53 protein isoforms has initiated a flurry of research into the function and regulation of these novel p53 proteins. Full-length p53 protein level is primarily regulated by the E3-ligase Mdm2, which promotes p53 ubiquitination and degradation. Here, we report that all of the novel p53 isoforms are ubiquitinated and degraded to varying degrees in an Mdm2-dependent and -independent manner, and that high-risk human papillomavirus can degrade some but not all of the novel isoforms, demonstrating that full-length p53 and the p53 isoforms are differentially regulated. In addition, we provide the first evidence that Mdm2 promotes the NEDDylation of p53β. Altogether, our data indicates that Mdm2 can distinguish between the p53 isoforms and modify them differently.
Keywords:degradation  isoform  Mdm2  NEDD8  neddylation  nutlin  p53  splice  Ubiquitination
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