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. 1995 Dec 1;270(5241):1491-4.
doi: 10.1126/science.270.5241.1491.

Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase

S Kato  1 , H Endoh, Y Masuhiro, T Kitamoto, S Uchiyama, H Sasaki, S Masushige, Y Gotoh, E Nishida, H Kawashima, D Metzger, P Chambon
Affiliations

Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase

S Kato et al. Science. .

Abstract

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 antiestrogen (tamoxifen)-induced transcriptional activity of wild-type ER, but not that of a mutant ER with an alanine in place of Ser118. Thus, the activity of the amino-terminal AF-1 of the ER is modulated by the phosphorylation of Ser118 through the Ras-MAPK cascade of the growth factor signaling pathways.

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