rdf:type |
|
lifeskim:mentions |
umls-concept:C0035679,
umls-concept:C0040649,
umls-concept:C0127400,
umls-concept:C0755397,
umls-concept:C1257890,
umls-concept:C1335237,
umls-concept:C1363844,
umls-concept:C1412133,
umls-concept:C1514873,
umls-concept:C1539082,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636
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pubmed:issue |
1
|
pubmed:dateCreated |
2005-7-1
|
pubmed:abstractText |
Human TRAP/Mediator is a key coactivator for many transcription factors that act through direct interactions with distinct subunits, and MED1/TRAP220 is the main subunit target for various nuclear receptors. Remarkably, the current study shows that MED1/TRAP220 only exists in a TRAP/Mediator subpopulation (less then 20% of the total) that is greatly enriched in specific TRAP/Mediator subunits and is tightly associated with a near stoichiometeric level of RNA polymerase II. Importantly, this MED1/TRAP220-containing holoenzyme supports both basal- and activator-dependent transcription in an in vitro system lacking additional RNA polymerase II. Furthermore, chromatin immunoprecipitation experiments demonstrate an activator-selective recruitment of MED1/TRAP220-containing versus MED1/TRAP220-deficient TRAP/Mediator complexes to estrogen receptor (ER) and p53 target genes, respectively. Finally, RNAi studies show that MED1/TRAP220 is required for ER-mediated transcription and estrogen-dependent breast cancer cell growth. These observations have significant implications for our current understanding of the composition, heterogeneity, and functional specificity of TRAP/Mediator complexes.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Endodeoxyribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Luciferases,
http://linkedlifedata.com/resource/pubmed/chemical/MBD4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/MED1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Mediator Complex Subunit 1,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Polymerase II,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Estrogen,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Protein p53
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
|
pubmed:issn |
1097-2765
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
1
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pubmed:volume |
19
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
89-100
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15989967-Breast Neoplasms,
pubmed-meshheading:15989967-Cell Line, Tumor,
pubmed-meshheading:15989967-Chromatin Immunoprecipitation,
pubmed-meshheading:15989967-Endodeoxyribonucleases,
pubmed-meshheading:15989967-Escherichia coli,
pubmed-meshheading:15989967-Female,
pubmed-meshheading:15989967-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:15989967-Genes, Reporter,
pubmed-meshheading:15989967-Humans,
pubmed-meshheading:15989967-Luciferases,
pubmed-meshheading:15989967-Mediator Complex Subunit 1,
pubmed-meshheading:15989967-RNA Interference,
pubmed-meshheading:15989967-RNA Polymerase II,
pubmed-meshheading:15989967-Receptors, Estrogen,
pubmed-meshheading:15989967-Transcription, Genetic,
pubmed-meshheading:15989967-Transcription Factors,
pubmed-meshheading:15989967-Tumor Suppressor Protein p53
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pubmed:year |
2005
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pubmed:articleTitle |
MED1/TRAP220 exists predominantly in a TRAP/ Mediator subpopulation enriched in RNA polymerase II and is required for ER-mediated transcription.
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pubmed:affiliation |
Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, 1230 York Avenue, New York, New York 10021, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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