Post-translational modification of p53

D. W. Meek

    Research output: Contribution to journalArticle

    142 Citations (Scopus)

    Abstract

    The p53 tumor suppressor protein is extensively post-translationally modified, mostly by phosphorylation. The phosphorylation sites are clustered into two distinct domains within the p53 polypeptide and the protein kinases and phosphatases which modify many of these sites have been identified. In addition, signaling pathways which modulate the phosphorylation state of p53, leading perhaps to changes in its activity, are being actively investigated. Similarly, the transforming proteins of DNA tumor viruses modulate p53 phosphorylation and may therefore be useful tools for probing these regulatory mechanisms. Given the very potent effects of p53 on cell growth and the extent of phosphorylation of this protein, p53 may well be controlled tightly and coordinately by more than one signaling mechanism.
    Original languageEnglish
    Pages (from-to)203-210
    Number of pages8
    JournalSeminars in Cancer Biology
    Volume5
    Issue number3
    Publication statusPublished - 1994

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    Post Translational Protein Processing
    Phosphorylation
    DNA Tumor Viruses
    Tumor Suppressor Protein p53
    Phosphoprotein Phosphatases
    Protein Kinases
    Proteins
    Peptides
    Growth

    Cite this

    Meek, D. W. / Post-translational modification of p53. In: Seminars in Cancer Biology. 1994 ; Vol. 5, No. 3. pp. 203-210.
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    Meek, DW 1994, 'Post-translational modification of p53', Seminars in Cancer Biology, vol. 5, no. 3, pp. 203-210.

    Post-translational modification of p53. / Meek, D. W.

    In: Seminars in Cancer Biology, Vol. 5, No. 3, 1994, p. 203-210.

    Research output: Contribution to journalArticle

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    AB - The p53 tumor suppressor protein is extensively post-translationally modified, mostly by phosphorylation. The phosphorylation sites are clustered into two distinct domains within the p53 polypeptide and the protein kinases and phosphatases which modify many of these sites have been identified. In addition, signaling pathways which modulate the phosphorylation state of p53, leading perhaps to changes in its activity, are being actively investigated. Similarly, the transforming proteins of DNA tumor viruses modulate p53 phosphorylation and may therefore be useful tools for probing these regulatory mechanisms. Given the very potent effects of p53 on cell growth and the extent of phosphorylation of this protein, p53 may well be controlled tightly and coordinately by more than one signaling mechanism.

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    JO - Seminars in Cancer Biology

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