Phosphorylation of estrogen receptor alpha blocks its acetylation and regulates estrogen sensitivity.

@article{Cui2004PhosphorylationOE,
  title={Phosphorylation of estrogen receptor alpha blocks its acetylation and regulates estrogen sensitivity.},
  author={Yukun Cui and Mao Zhang and Richard C Pestell and Edward M. Curran and Wade V. Welshons and Suzanne A W Fuqua},
  journal={Cancer research},
  year={2004},
  volume={64 24},
  pages={9199-208}
}
Estrogen receptor (ER) alpha is mutated (lysine 303 to arginine, K303R) in approximately one third of premalignant breast hyperplasias, which renders breast cancer cells expressing the mutant receptor hypersensitive for proliferation in response to low doses of estrogen. It is known that ERalpha is posttranslationally modified by protein acetylation and phosphorylation by a number of secondary messenger signaling cascades. The K303R ERalpha mutation resides at a major protein acetylation site… CONTINUE READING

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