Multiple C-terminal lysine residues target p53 for ubiquitin-proteasome-mediated degradation.

@article{Rodrguez2000MultipleCL,
  title={Multiple C-terminal lysine residues target p53 for ubiquitin-proteasome-mediated degradation.},
  author={Manuel S. Rodr{\'i}guez and Joana M. P. Desterro and Sonia Lain and D. P. Lane and Ron T. Hay},
  journal={Molecular and cellular biology},
  year={2000},
  volume={20 22},
  pages={8458-67}
}
In normal cells, p53 is maintained at a low level by ubiquitin-mediated proteolysis, but after genotoxic insult this process is inhibited and p53 levels rise dramatically. Ubiquitination of p53 requires the ubiquitin-activating enzyme Ubc5 as a ubiquitin conjugation enzyme and Mdm2, which acts as a ubiquitin protein ligase. In addition to the N-terminal region, which is required for interaction with Mdm2, the C-terminal domain of p53 modulates the susceptibility of p53 to Mdm2-mediated… CONTINUE READING

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