rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2008-5-5
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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.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Androgens,
http://linkedlifedata.com/resource/pubmed/chemical/Dioxins,
http://linkedlifedata.com/resource/pubmed/chemical/Estrogen Receptor alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Estrogens,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Androgen,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Aryl Hydrocarbon,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1090-2104
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pubmed:author |
|
pubmed:issnType |
Electronic
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pubmed:day |
13
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pubmed:volume |
370
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
541-6
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:18358233-Androgens,
pubmed-meshheading:18358233-Cell Line, Tumor,
pubmed-meshheading:18358233-Dioxins,
pubmed-meshheading:18358233-Estrogen Receptor alpha,
pubmed-meshheading:18358233-Estrogens,
pubmed-meshheading:18358233-Gene Expression Regulation,
pubmed-meshheading:18358233-Humans,
pubmed-meshheading:18358233-Ligands,
pubmed-meshheading:18358233-Mutation,
pubmed-meshheading:18358233-Promoter Regions, Genetic,
pubmed-meshheading:18358233-Proteasome Endopeptidase Complex,
pubmed-meshheading:18358233-Protein Structure, Tertiary,
pubmed-meshheading:18358233-Receptors, Androgen,
pubmed-meshheading:18358233-Receptors, Aryl Hydrocarbon,
pubmed-meshheading:18358233-Transcription, Genetic,
pubmed-meshheading:18358233-Ubiquitin-Protein Ligases
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pubmed:year |
2008
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pubmed:articleTitle |
Intrinsic AhR function underlies cross-talk of dioxins with sex hormone signalings.
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pubmed:affiliation |
Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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