| pubmed-article:10230404 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10230404 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:10230404 | lifeskim:mentions | umls-concept:C1334196 | lld:lifeskim |
| pubmed-article:10230404 | lifeskim:mentions | umls-concept:C0529099 | lld:lifeskim |
| pubmed-article:10230404 | lifeskim:mentions | umls-concept:C0271510 | lld:lifeskim |
| pubmed-article:10230404 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:10230404 | lifeskim:mentions | umls-concept:C1334084 | lld:lifeskim |
| pubmed-article:10230404 | lifeskim:mentions | umls-concept:C1419034 | lld:lifeskim |
| pubmed-article:10230404 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:10230404 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:10230404 | pubmed:dateCreated | 1999-5-27 | lld:pubmed |
| pubmed-article:10230404 | pubmed:abstractText | The estrogen receptors (ERs) alpha and beta possess a constitutive N-terminal activation function (AF-1) whose activity can be modulated by kinase signalling pathways. We demonstrate here that phosphorylation of AF-1 by MAP kinase (MAPK) leads to the recruitment of steroid receptor coactivator-1 (SRC-1) by ER beta in vitro. Enhancement of the interaction between SRC-1 and ER beta AF-1 is also observed in vivo in cells either treated with EGF or expressing activated Ras. Two serine residues in ER beta AF-1, of which one is contained within a motif present in other steroid receptors, are critical for physical interaction with SRC-1 and transcriptional activation. Our results establish a role for nuclear receptor phosphorylation in the recruitment of SRC-1 and provide a molecular basis for ligand-independent activation by ER beta via the MAPK pathway. | lld:pubmed |
| pubmed-article:10230404 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10230404 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10230404 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10230404 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10230404 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10230404 | pubmed:issn | 1097-2765 | lld:pubmed |
| pubmed-article:10230404 | pubmed:author | pubmed-author:LabrieFF | lld:pubmed |
| pubmed-article:10230404 | pubmed:author | pubmed-author:TremblayAA | lld:pubmed |
| pubmed-article:10230404 | pubmed:author | pubmed-author:GiguèreVV | lld:pubmed |
| pubmed-article:10230404 | pubmed:author | pubmed-author:TremblayG BGB | lld:pubmed |
| pubmed-article:10230404 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10230404 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:10230404 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10230404 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10230404 | pubmed:pagination | 513-9 | lld:pubmed |
| pubmed-article:10230404 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:10230404 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10230404 | pubmed:articleTitle | Ligand-independent recruitment of SRC-1 to estrogen receptor beta through phosphorylation of activation function AF-1. | lld:pubmed |
| pubmed-article:10230404 | pubmed:affiliation | Molecular Oncology Group, McGill University Health Centre, Montréal, Québec, Canada. | lld:pubmed |
| pubmed-article:10230404 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10230404 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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