Interplay between ribosomal protein S27a and MDM2 protein in p53 activation in response to ribosomal stress.

@article{Sun2011InterplayBR,
  title={Interplay between ribosomal protein S27a and MDM2 protein in p53 activation in response to ribosomal stress.},
  author={X. L. Sun and Tiffany Devine and Kishore B Challagundla and Mu-Shui Dai},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 26},
  pages={22730-41}
}
Ribosomal proteins play a critical role in tightly coordinating p53 signaling with ribosomal biogenesis. Several ribosomal proteins have been shown to induce and activate p53 via inhibition of MDM2. Here, we report that S27a, a small subunit ribosomal protein synthesized as an 80-amino acid ubiquitin C-terminal extension protein (CEP80), functions as a novel regulator of the MDM2-p53 loop. S27a interacts with MDM2 at the central acidic domain of MDM2 and suppresses MDM2-mediated p53… CONTINUE READING

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