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- W2108681406 abstract "Human estrogen receptors α and β (ERα and ERβ) greatly differ in their target genes, transcriptional potency and cofactor-binding capacity, and are differentially expressed in various tissues. In classical estrogen response element (ERE)-mediated transactivation, ERβ has a markedly reduced activation potential compared with ERα; the mechanism underlying this difference is unclear. Here, we report that the binding of steroid receptor coactivator-1 (SRC-1) to the AF-1 domain of ERα is essential but not sufficient to facilitate synergy between the AF-1 and AF-2 domains, which is required for a full agonistic response to estradiol (E2). Complete synergy is achieved through the distinct hinge domain of ERα, which enables combined action of the AF-1 and AF-2 domains. AF-1 of ERβ lacks the capacity to interact with SRC-1, which prevents hinge-mediated synergy between AF-1 and AF-2, thereby explaining the reduced E2-mediated transactivation of ERβ. Transactivation of ERβ by E2 requires only the AF-2 domain. A weak agonistic response to tamoxifen occurs for ERα, but not for ERβ, and depends on AF-1 and the hinge-region domain of ERα." @default.
- W2108681406 created "2016-06-24" @default.
- W2108681406 creator A5006708192 @default.
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- W2108681406 date "2010-04-15" @default.
- W2108681406 modified "2023-10-13" @default.
- W2108681406 title "The hinge region of the human estrogen receptor determines functional synergy between AF-1 and AF-2 in the quantitative response to estradiol and tamoxifen" @default.
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- W2108681406 doi "https://doi.org/10.1242/jcs.061135" @default.
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