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

書誌事項

公開日
1995-12
DOI
  • 10.1126/science.270.5241.1491
公開者
American Association for the Advancement of Science (AAAS)

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説明

<jats:p> 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 Ser <jats:sup>118</jats:sup> 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 Ser <jats:sup>118</jats:sup> . Thus, the activity of the amino-terminal AF-1 of the ER is modulated by the phosphorylation of Ser <jats:sup>118</jats:sup> through the Ras-MAPK cascade of the growth factor signaling pathways. </jats:p>

収録刊行物

  • Science

    Science 270 (5241), 1491-1494, 1995-12

    American Association for the Advancement of Science (AAAS)

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