Inhibition of p53 degradation by Mdm2 acetylation.

@article{Wang2004InhibitionOP,
  title={Inhibition of p53 degradation by Mdm2 acetylation.},
  author={X. Henry Wang and Jan Taplick and Naama Geva and Moshe Oren},
  journal={FEBS letters},
  year={2004},
  volume={561 1-3},
  pages={195-201}
}
Mdm2 is a RING finger E3 ubiquitin ligase, which promotes ubiquitination and proteasomal degradation of the p53 tumor suppressor protein. Acetylation of p53 regulates p53's transcriptional activity and inhibits Mdm2-mediated p53 ubiquitination and degradation. We now report that Mdm2 is also a target for acetylation. Mdm2 is acetylated in vitro by CREB-binding protein (CBP) and to a lesser extent by p300, but not by p300/CPB-associated factor. Acetylation occurs primarily within the RING finger… CONTINUE READING

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