PhosphoPlus® Estrogen Receptor α (Ser167) Antibody Duet #12108
Inquiry Info. # 12108
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Background
Estrogen receptor α (ERα), a member of the steroid receptor superfamily, contains highly conserved DNA binding and ligand binding domains (1). Through its estrogen-independent and estrogen-dependent activation domains (AF-1 and AF-2, respectively), ERα regulates transcription by recruiting coactivator proteins and interacting with general transcriptional machinery (2). Phosphorylation at multiple sites provides an important mechanism to regulate ERα activity (3-5). Ser104, 106, 118, and 167 are located in the amino-terminal transcription activation function domain AF-1, and phosphorylation of these serine residues plays an important role in regulating ERα activity. Ser118 may be the substrate of the transcription regulatory kinase CDK7 (5). Ser167 may be phosphorylated by p90RSK and Akt (4,6). According to the research literature, phosphorylation at Ser167 may confer tamoxifen resistance in breast cancer patients (4).
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- Glass, C.K. and Rosenfeld, M.G. (2000) Genes Dev 14, 121-41.
- Chen, D. et al. (1999) Mol Cell Biol 19, 1002-15.
- Campbell, R.A. et al. (2001) J Biol Chem 276, 9817-24.
- Chen, D. et al. (2000) Mol Cell 6, 127-37.
- Joel, P.B. et al. (1998) Mol Cell Biol 18, 1978-84.
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