The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation.

@article{Esser2005TheCU,
  title={The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation.},
  author={Claudia Esser and Martin Scheffner and J{\"o}rg H{\"o}hfeld},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 29},
  pages={27443-8}
}
The cellular level of the tumor suppressor p53 is tightly regulated through induced degradation via the ubiquitin/proteasome system. The ubiquitin ligase Mdm2 plays a pivotal role in stimulating p53 turnover. However, recently additional ubiquitin ligases have been identified that participate in the degradation of the tumor suppressor. Apparently, multiple degradation pathways are employed to ensure proper destruction of p53. Here we show that the chaperone-associated ubiquitin ligase CHIP is… CONTINUE READING

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