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rdf:type |
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lifeskim:mentions |
umls-concept:C0034843,
umls-concept:C0086418,
umls-concept:C0127400,
umls-concept:C0205224,
umls-concept:C0449432,
umls-concept:C1179435,
umls-concept:C1363844,
umls-concept:C1524073,
umls-concept:C1548799,
umls-concept:C1551336,
umls-concept:C1705248
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pubmed:issue |
1-2
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pubmed:dateCreated |
2004-7-13
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pubmed:abstractText |
Nuclear hormone receptors interact with the basal-transcriptional complex and/or coactivators to regulate transcriptional activation. These activator-target interactions recruit the transcriptional machinery to the promoter and may also stimulate transcriptional events subsequent to the binding of the machinery to the promoter or enhancer element. We describe a novel functional interaction of the nuclear thyroid receptor (TR), with a human Mediator component (hSrb7), and a human TFIIH component (hMo15). In mammalian two-hybrid experiments as well as in GST-pull down assays, hSrb7 interacts with TR but not with other nuclear receptors such as the retinoic acid receptor (RAR) or the vitamin D receptor (VDR). Whereas hMo15 also interacts with VDR and RAR in mammalian two-hybrid assays, no association of hSrb7 with VDR or RAR is found. Accordingly, cotransfection of TR and hSrb7 increases thyroid hormone (T3)-dependent transcription in an AF-2-dependent manner, while hSrb7 causes no stimulation of vitamin D- or retinoic acid-mediated transactivation. These results reveal a novel co-activator role for hSrb7 and hMo15 on TR transcriptional responses, and demonstrate that different receptors can selectively target different co-activators or general transcription factors to stimulate transcription.
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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/Antineoplastic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Furylfuramide,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/MED21 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Mediator Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Calcitriol,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Retinoic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Thyroid Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Thyroid Hormones,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor TFIIH,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, TFII,
http://linkedlifedata.com/resource/pubmed/chemical/Tretinoin,
http://linkedlifedata.com/resource/pubmed/chemical/Vitamin D,
http://linkedlifedata.com/resource/pubmed/chemical/cyclin-dependent kinase-activating...
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0303-7207
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
222
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
41-51
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15249124-Animals,
pubmed-meshheading:15249124-Antineoplastic Agents,
pubmed-meshheading:15249124-COS Cells,
pubmed-meshheading:15249124-Cercopithecus aethiops,
pubmed-meshheading:15249124-Cyclin-Dependent Kinases,
pubmed-meshheading:15249124-Furylfuramide,
pubmed-meshheading:15249124-Glutathione Transferase,
pubmed-meshheading:15249124-HeLa Cells,
pubmed-meshheading:15249124-Humans,
pubmed-meshheading:15249124-Mediator Complex,
pubmed-meshheading:15249124-Receptors, Calcitriol,
pubmed-meshheading:15249124-Receptors, Retinoic Acid,
pubmed-meshheading:15249124-Receptors, Thyroid Hormone,
pubmed-meshheading:15249124-Thyroid Hormones,
pubmed-meshheading:15249124-Trans-Activators,
pubmed-meshheading:15249124-Transcription, Genetic,
pubmed-meshheading:15249124-Transcription Factor TFIIH,
pubmed-meshheading:15249124-Transcription Factors,
pubmed-meshheading:15249124-Transcription Factors, TFII,
pubmed-meshheading:15249124-Transcriptional Activation,
pubmed-meshheading:15249124-Transfection,
pubmed-meshheading:15249124-Tretinoin,
pubmed-meshheading:15249124-Two-Hybrid System Techniques,
pubmed-meshheading:15249124-Vitamin D
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pubmed:year |
2004
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pubmed:articleTitle |
hSrb7, an essential human Mediator component, acts as a coactivator for the thyroid hormone receptor.
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pubmed:affiliation |
Unidad de Investigación, Hospital Universitario de Getafe, 28905 Getafe, Madrid, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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