MDMX inhibits the p300/CBP-mediated acetylation of p53.

The p300/CBP-mediated acetylation of p53 significantly potentiates p53-mediated transactivation and growth inhibition. MDM2 inhibits the acetylation of p53 by p300/CBP through a mechanism that requires a stable p53-MDM2 interaction and that is sensitive to the deacetylase inhibitor, TSA. MDMX is an MDM2-like protein that shares with MDM2 the ability to ...
interact with p53 and, in turn, inhibit p53-mediated transcription. It was therefore of interest to determine if MDMX could also inhibit the acetylation of p53 by p300/CBP. We demonstrate that MDMX dramatically inhibits the acetylation of p53 induced by both endogenous and ectopically expressed p300/CBP. We also demonstrate that the p53-binding domain of MDMX is required for the MDMX-mediated inhibition of p53 acetylation. Our results indicate that MDMX shares with MDM2 the ability to regulate a potentially important post-translational modification of p53. These results may have important biologic implications with respect to the MDMX-mediated regulation of p53 activity during development.
Mesh Terms:
Acetylation, Animals, Binding Sites, Cell Line, DNA-Activated Protein Kinase, DNA-Binding Proteins, E1A-Associated p300 Protein, Humans, Mice, Mice, Knockout, Models, Biological, Nuclear Proteins, Protein Processing, Post-Translational, Protein Structure, Tertiary, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-mdm2, Recombinant Proteins, Trans-Activators, Transfection, Tumor Suppressor Protein p53
DNA Cell Biol.
Date: Jul. 01, 2002
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