| pubmed-article:18358233 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18358233 | lifeskim:mentions | umls-concept:C0205102 | lld:lifeskim |
| pubmed-article:18358233 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:18358233 | lifeskim:mentions | umls-concept:C0012503 | lld:lifeskim |
| pubmed-article:18358233 | lifeskim:mentions | umls-concept:C0036884 | lld:lifeskim |
| pubmed-article:18358233 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:18358233 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:18358233 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:18358233 | pubmed:dateCreated | 2008-5-5 | lld:pubmed |
| pubmed-article:18358233 | pubmed:abstractText | The arylhydrocarbon receptor (AhR) mediates sex steroid hormone-related actions in both normal physiology and in dioxin toxicity. In addition to regulation of direct target genes, the ligand-activated AhR associates with estrogen or androgen receptors (ERalpha or AR) to regulate transcription as a functional unit. Given that endogenous and exogenous AhR-ligands are structurally diverse, it is unclear whether cross-talk regulation of ERalpha/AR by the activated AhR is an intrinsic function of the AhR or the result of ligand-type-selective differences. To ensure uniform activity of the AhR irrespective of ligand-type-specific differences, we employed CA-AhR, which lacks the ligand-binding domain and has a constitutive activity. We found that CA-AhR, in the absence of a ligand, acted as a transcriptional co-regulator for the unliganded ERalpha/AR as well as for mutants of ERalpha/AR lacking a ligand-binding domain. CA-AhR was recruited to estrogen-/androgen-responsive promoters with endogenous ERalpha/AR. Moreover, CA-AhR had an E3 ubiquitin ligase activity and promoted proteasomal degradation of ERalpha/AR. Thus, these findings indicate that the cross-talk function of the AhR with sex hormone receptors is an intrinsic function of the AhR. | lld:pubmed |
| pubmed-article:18358233 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18358233 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18358233 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18358233 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18358233 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18358233 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18358233 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18358233 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18358233 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18358233 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18358233 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:18358233 | pubmed:issn | 1090-2104 | lld:pubmed |
| pubmed-article:18358233 | pubmed:author | pubmed-author:KatoShigeakiS | lld:pubmed |
| pubmed-article:18358233 | pubmed:author | pubmed-author:Fujii-Kuriyam... | lld:pubmed |
| pubmed-article:18358233 | pubmed:author | pubmed-author:BabaAtsushiA | lld:pubmed |
| pubmed-article:18358233 | pubmed:author | pubmed-author:OhtakeFumiaki... | lld:pubmed |
| pubmed-article:18358233 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18358233 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:18358233 | pubmed:volume | 370 | lld:pubmed |
| pubmed-article:18358233 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18358233 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18358233 | pubmed:pagination | 541-6 | lld:pubmed |
| pubmed-article:18358233 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:18358233 | pubmed:meshHeading | pubmed-meshheading:18358233... | lld:pubmed |
| pubmed-article:18358233 | pubmed:meshHeading | pubmed-meshheading:18358233... | lld:pubmed |
| pubmed-article:18358233 | pubmed:meshHeading | pubmed-meshheading:18358233... | lld:pubmed |
| pubmed-article:18358233 | pubmed:meshHeading | pubmed-meshheading:18358233... | lld:pubmed |
| pubmed-article:18358233 | pubmed:meshHeading | pubmed-meshheading:18358233... | lld:pubmed |
| pubmed-article:18358233 | pubmed:meshHeading | pubmed-meshheading:18358233... | lld:pubmed |
| pubmed-article:18358233 | pubmed:meshHeading | pubmed-meshheading:18358233... | lld:pubmed |
| pubmed-article:18358233 | pubmed:meshHeading | pubmed-meshheading:18358233... | lld:pubmed |
| pubmed-article:18358233 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18358233 | pubmed:articleTitle | Intrinsic AhR function underlies cross-talk of dioxins with sex hormone signalings. | lld:pubmed |
| pubmed-article:18358233 | pubmed:affiliation | Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan. | lld:pubmed |
| pubmed-article:18358233 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18358233 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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