Activation of the Estrogen Receptor Through Phosphorylation by Mitogen-Activated Protein Kinase

@article{Kato1995ActivationOT,
  title={Activation of the Estrogen Receptor Through Phosphorylation by Mitogen-Activated Protein Kinase},
  author={Shigeaki Kato and Hideki Endoh and Yoshikazu Masuhiro and Takuya Kitamoto and Shimami Uchiyama and Haruna Sasaki and Shoichi Masushige and Yukiko Gotoh and Eisuke Nishida and Hiroyuki Kawashima and Daniel Metzger and Pierre Chambon},
  journal={Science},
  year={1995},
  volume={270},
  pages={1491 - 1494}
}
The phosphorylation of the human estrogen receptor (ER) serine residue at position 118 is required for full activity of the ER activation function 1 (AF-1). This Ser118 is phosphorylated by mitogen-activated protein kinase (MAPK) in vitro and in cells treated with epidermal growth factor (EGF) and insulin-like growth factor (IGF) in vivo. Overexpression of MAPK kinase (MAPKK) or of the guanine nucleotide binding protein Ras, both of which activate MAPK, enhanced estrogen-induced and… Expand
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TLDR
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TLDR
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TLDR
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