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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1999-5-27
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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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Estrogen Receptor beta,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Ifngr2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Ncoa1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Receptor Coactivator 1,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Estrogen,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interferon,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
513-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10230404-Amino Acid Sequence,
pubmed-meshheading:10230404-Animals,
pubmed-meshheading:10230404-COS Cells,
pubmed-meshheading:10230404-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:10230404-Epidermal Growth Factor,
pubmed-meshheading:10230404-Estrogen Receptor beta,
pubmed-meshheading:10230404-Gene Expression Regulation,
pubmed-meshheading:10230404-Genes, Reporter,
pubmed-meshheading:10230404-Histone Acetyltransferases,
pubmed-meshheading:10230404-Ligands,
pubmed-meshheading:10230404-Mice,
pubmed-meshheading:10230404-Molecular Sequence Data,
pubmed-meshheading:10230404-Mutation,
pubmed-meshheading:10230404-Nuclear Receptor Coactivator 1,
pubmed-meshheading:10230404-Phosphorylation,
pubmed-meshheading:10230404-Receptors, Estrogen,
pubmed-meshheading:10230404-Receptors, Interferon,
pubmed-meshheading:10230404-Signal Transduction,
pubmed-meshheading:10230404-Transcription Factors,
pubmed-meshheading:10230404-Transfection
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pubmed:year |
1999
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pubmed:articleTitle |
Ligand-independent recruitment of SRC-1 to estrogen receptor beta through phosphorylation of activation function AF-1.
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pubmed:affiliation |
Molecular Oncology Group, McGill University Health Centre, Montréal, Québec, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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