The p53 isoforms are differentially modified by Mdm2

Suzanne Camus, Sergio Menendez, Kenneth Fernandes, Nelly Kua, Geng Liu, Dimitris P. Xirodimas, David P. Lane, Jean-Christophe Bourdon

    Research output: Contribution to journalArticlepeer-review

    30 Citations (Scopus)


    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 p53 beta. Altogether, our data indicates that Mdm2 can distinguish between the p53 isoforms and modify them differently.

    Original languageEnglish
    Pages (from-to)1646-1655
    Number of pages10
    JournalCell Cycle
    Issue number8
    Publication statusPublished - 15 Apr 2012


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