The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation.
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.[1]References
- The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation. Momand, J., Zambetti, G.P., Olson, D.C., George, D., Levine, A.J. Cell (1992) [Pubmed]
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