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    Cell. 1992 Jun 26;69(7):1237-45.

    The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation.

    Momand J, Zambetti GP, Olson DC, George D, Levine AJ.

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    Department of Molecular Biology, Lewis Thomas Laboratory, Princeton University, New Jersey 08544-1014.

    Abstract

    A cellular phosphoprotein with an apparent molecular mass of 90 kd (p90) that forms a complex with both mutant and wild-type p53 protein has been characterized, purified, and identified. The protein was identified as a product of the murine double minute 2 gene (mdm-2). The mdm-2 gene enhances the tumorigenic potential of cells when it is overexpressed and encodes a putative transcription factor. To determine if mdm-2 could modulate p53 transactivation, a p53-responsive element from the muscle creatine kinase gene was employed. A wild-type p53-expressing plasmid enhanced the expression of the p53-responsive element when cotransfected into cells that contain no endogenous p53. When a cosmid expressing mdm-2 was transfected with this p53-expressing plasmid, the transactivation of the p53-responsive element was inhibited. Thus, a product of the mdm-2 oncogene forms a tight complex with the p53 protein, and the mdm-2 oncogene can inhibit p53-mediated transactivation.

    PMID:
    1535557
    [PubMed - indexed for MEDLINE]

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