Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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.


Journal article


Mol Cell

Publication Date





181 - 193


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