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The binding of RB to MDM2 is shown to be essential for RB to overcome both the antiapoptotic function of MDM2 and the MDM2-dependent degradation of p53. The RB-MDM2 interaction does not prevent MDM2 from inhibiting p53-dependent transcription, but the RB-MDM2 complex still binds to p53. Since RB specifically rescues the apoptotic function but not the transcriptional activity of p53 from negative regulation by MDM2, transactivation by wild-type p53 is not required for the apoptotic function of p53. However, an RB-MDM2-p53 trimeric complex is active in p53-mediated transrepression. These data link directly the function of two tumor suppressor proteins and demonstrate a novel role of RB in regulating the apoptotic function of p53.

Type

Journal article

Journal

Mol Cell

Publication Date

02/1999

Volume

3

Pages

181 - 193

Keywords

Apoptosis, Binding Sites, Carrier Proteins, Cell Cycle Proteins, DNA-Binding Proteins, E2F Transcription Factors, Female, Gene Expression, Genes, Retinoblastoma, Genes, p53, Humans, Macromolecular Substances, Nuclear Proteins, Peptide Fragments, Phosphorylation, Protein Binding, Protein Processing, Post-Translational, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-mdm2, Retinoblastoma Protein, Retinoblastoma-Binding Protein 1, Transcription Factor DP1, Transcription Factors, Transcriptional Activation, Transfection, Tumor Cells, Cultured, Tumor Suppressor Protein p53