Abstract
The exact role of the central acidic domain of Mdm2 in p53 degradation remains unclear. We therefore performed a systematic and comprehensive analysis of the acidic domain using a series of short deletions and found that only a minor part of the domain was indispensable for Mdm2-mediated p53 ubiquitylation. Moreover, we identified a short stretch of acidic amino acids required for p53 degradation but not ubiquitylation, indicating that, in addition to p53 ubiquitylation, the acidic domain might be involved in a critical post-ubiquitylation step in p53 degradation. Rather than representing a single functional domain, different parts of the acidic region perform separate functions in p53 degradation, suggesting that it might be possible to therapeutically target them independently. Structured summary of protein interactionsMDM2 physically interacts with S6b by anti bait coimmunoprecipitation (View interaction)MDM2 physically interacts with p53 by anti bait coimmunoprecipitation (View interaction: 1, 2)MDM2 physically interacts with C8α by anti bait coimmunoprecipitation (View interaction: 1, 2)YY1 physically interacts with MDM2 by anti bait coimmunoprecipitation (View interaction)MDM2 physically interacts with S6a by anti bait coimmunoprecipitation (View interaction)
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