Dynamics in the p53-Mdm2 ubiquitination pathway.
Changes over time in how p53 and Mdm2 proteins regulate each other through tagging for breakdown
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Abstract
The stability of the tumor suppressor p53 is predominantly regulated by the E3 ligase Mdm2 through the ubiquitin-proteasomal pathway.
- Mdm2 is capable of catalyzing both mono- and polyubiquitination of p53, indicating a dynamic regulation process.
- Deubiquitination is critical for maintaining the stability of both p53 and Mdm2.
- Regulatory factors such as HAUSP, p14(ARF), and MdmX influence p53 ubiquitination and deubiquitination.
- The interplay between these factors and Mdm2 adds complexity to the regulation of p53 stability.
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