pubmed-article:15383530 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15383530 | lifeskim:mentions | umls-concept:C0006622 | lld:lifeskim |
pubmed-article:15383530 | lifeskim:mentions | umls-concept:C0009209 | lld:lifeskim |
pubmed-article:15383530 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:15383530 | lifeskim:mentions | umls-concept:C0020242 | lld:lifeskim |
pubmed-article:15383530 | lifeskim:mentions | umls-concept:C0040649 | lld:lifeskim |
pubmed-article:15383530 | lifeskim:mentions | umls-concept:C1516692 | lld:lifeskim |
pubmed-article:15383530 | lifeskim:mentions | umls-concept:C1824520 | lld:lifeskim |
pubmed-article:15383530 | pubmed:issue | 48 | lld:pubmed |
pubmed-article:15383530 | pubmed:dateCreated | 2004-11-23 | lld:pubmed |
pubmed-article:15383530 | pubmed:abstractText | The aryl hydrocarbon receptor (AHR) and AHR nuclear translocator (ARNT) are DNA binding transcription factors with basic helix-loop-helix/Per-Arnt-Sim (bHLH-PAS) domains. These two proteins form a heterodimer that mediates the toxic and biological effects of the environmental contaminant and AHR ligand 2,3,7,8-tetrachlorodibenzo-p-dioxin. The coiled-coil protein coiled-coil coactivator (Co-CoA) is a secondary coactivator for nuclear receptors and enhances nuclear receptor function by interacting with the bHLH-PAS domain of p160 coactivators. We report here that CoCoA also binds the bHLH-PAS domains of AHR and ARNT and functions as a potent primary coactivator for them; i.e. CoCoA does not require p160 coactivators for binding to and serving as a coactivator for AHR and ARNT. Endogenous CoCoA was recruited to a natural AHR target gene promoter in a 2,3,7,8-tetrachlorodibenzo-p-dioxin -dependent manner. Moreover, reduction of CoCoA mRNA levels by small interfering RNA inhibited the transcriptional activation by AHR and ARNT. Our data support a physiological role for CoCoA as a transcriptional coactivator in AHR/ARNT-mediated transcription. | lld:pubmed |
pubmed-article:15383530 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15383530 | pubmed:language | eng | lld:pubmed |
pubmed-article:15383530 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15383530 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:15383530 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15383530 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15383530 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15383530 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15383530 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15383530 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15383530 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15383530 | pubmed:month | Nov | lld:pubmed |
pubmed-article:15383530 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:15383530 | pubmed:author | pubmed-author:StallcupMicha... | lld:pubmed |
pubmed-article:15383530 | pubmed:author | pubmed-author:KimJeong... | lld:pubmed |
pubmed-article:15383530 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15383530 | pubmed:day | 26 | lld:pubmed |
pubmed-article:15383530 | pubmed:volume | 279 | lld:pubmed |
pubmed-article:15383530 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15383530 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15383530 | pubmed:pagination | 49842-8 | lld:pubmed |
pubmed-article:15383530 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:15383530 | pubmed:meshHeading | pubmed-meshheading:15383530... | lld:pubmed |
pubmed-article:15383530 | pubmed:meshHeading | pubmed-meshheading:15383530... | lld:pubmed |
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pubmed-article:15383530 | pubmed:meshHeading | pubmed-meshheading:15383530... | lld:pubmed |
pubmed-article:15383530 | pubmed:meshHeading | pubmed-meshheading:15383530... | lld:pubmed |
pubmed-article:15383530 | pubmed:meshHeading | pubmed-meshheading:15383530... | lld:pubmed |
pubmed-article:15383530 | pubmed:meshHeading | pubmed-meshheading:15383530... | lld:pubmed |
pubmed-article:15383530 | pubmed:meshHeading | pubmed-meshheading:15383530... | lld:pubmed |
pubmed-article:15383530 | pubmed:meshHeading | pubmed-meshheading:15383530... | lld:pubmed |
pubmed-article:15383530 | pubmed:meshHeading | pubmed-meshheading:15383530... | lld:pubmed |
pubmed-article:15383530 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:15383530 | pubmed:articleTitle | Role of the coiled-coil coactivator (CoCoA) in aryl hydrocarbon receptor-mediated transcription. | lld:pubmed |
pubmed-article:15383530 | pubmed:affiliation | Department of Pathology and Department of Biochemistry and Molecular Biology, University of Southern California, Los Angeles, California 90089, USA. | lld:pubmed |
pubmed-article:15383530 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15383530 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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