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pubmed-article:11358671pubmed:abstractTextEstrogens are essential regulators in the development and control of reproductive functions. The estrogenic signal is now known to be transduced by two estrogen receptors, ERalpha and ERbeta. Hormone-dependent transcriptional activation of ER and other nuclear receptors involves assembly of a coactivation complex which includes various cofactors such as the steroid receptor-coactivators (SRC) and CREB binding protein (CBP). Our findings on ERbeta have revealed a ligand-independent activation pathway which involves growth factor-mediated phosphorylation of ERbeta activation function-1 (AF-1) and subsequent recruitment of SRC-1 independently of the presence of estrogens. The presence of the cointegrator CBP is also shown to potentiate the SRC-1-mediated ERbeta ligand-independent activation, suggesting that CBP may participate in unliganded ERbeta coactivation. These findings demonstrate the ability of alternate signaling pathways to mediate coregulator assembly, hence resulting in ligand-independent activation of ERbeta.lld:pubmed
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pubmed-article:11358671pubmed:articleTitleContribution of steroid receptor coactivator-1 and CREB binding protein in ligand-independent activity of estrogen receptor beta.lld:pubmed
pubmed-article:11358671pubmed:affiliationSte-Justine Hospital Research Center, University of Montreal, Montréal, QC, Canada H3T 1C5. atremblay@justine.umontreal.calld:pubmed
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