Auto-ubiquitination of Mdm2 enhances its substrate ubiquitin ligase activity.

@article{Ranaweera2013AutoubiquitinationOM,
  title={Auto-ubiquitination of Mdm2 enhances its substrate ubiquitin ligase activity.},
  author={Ruchira S. Ranaweera and Xiaolu Yang},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 26},
  pages={18939-46}
}
The RING domain E3 ubiquitin ligase Mdm2 is the master regulator of the tumor suppressor p53. It targets p53 for proteasomal degradation, restraining the potent activity of p53 and enabling cell survival and proliferation. Like most E3 ligases, Mdm2 can also ubiquitinate itself. How Mdm2 auto-ubiquitination may influence its substrate ubiquitin ligase activity is undefined. Here we show that auto-ubiquitination of Mdm2 is an activating event. Mdm2 that has been conjugated to polyubiquitin… CONTINUE READING

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