Multiple sites of in vivo phosphorylation in the MDM2 oncoprotein cluster within two important functional domains

Trevor J. Hay, David W. Meek

    Research output: Contribution to journalArticle

    51 Citations (Scopus)

    Abstract

    The MDM2 oncoprotein is a negative regulatory partner of the p53 tumour suppressor. MDM2 mediates ubiquitination of p53 and targets the protein to the cytoplasm for 26S proteosome-dependent degradation. In this paper, we show that MDM2 is modified in cultured cells by multisite phosphorylation. Deletion analysis of MDM2 indicated that the sites of modification fall into two clusters which map respectively within the N-terminal region encompassing the p53 binding domain and nuclear export sequence, and the central acidic domain that mediates p14(ARF) binding, p53 ubiquitination and cytoplasmic shuttling. The data are consistent with potential regulation of MDM2 function by multisite phosphorylation.
    Original languageEnglish
    Pages (from-to)183-186
    Number of pages4
    JournalFEBS Letters
    Volume478
    Issue number1-2
    DOIs
    Publication statusPublished - 28 Jul 2000

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