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rdf:type |
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lifeskim:mentions |
umls-concept:C0039635,
umls-concept:C0040649,
umls-concept:C0052441,
umls-concept:C0205314,
umls-concept:C0205341,
umls-concept:C0679622,
umls-concept:C0871261,
umls-concept:C1333198,
umls-concept:C1514562,
umls-concept:C1549781,
umls-concept:C1704632,
umls-concept:C1706817,
umls-concept:C2911692
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pubmed:issue |
14
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pubmed:dateCreated |
1997-5-8
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pubmed:databankReference |
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pubmed:abstractText |
To identify new proteins involved in dioxin-dependent signal transduction and transcriptional regulation, we used a yeast two-hybrid system to identify proteins that interact with the Ah receptor (AhR). We cloned a mouse cDNA, which encodes a novel approximately 37-kDa protein that binds to AhR; we have designated the protein as Ah receptor-interacting protein (AIP). The amino acid sequence of mouse AIP exhibits homology with members of the FK506-binding protein family. AIP also contains three tetratricopeptide repeat (TPR) motifs; the TPR sequence is present in proteins required for cell cycle control and RNA synthesis and in steroid receptor-binding immunophilins. Coimmunoprecipitation experiments in mouse hepatoma cells reveal that AIP is cytoplasmic and associates with unliganded Ah receptor and with hsp90; 2,3,7,8-tetrachlorodibenzo-p-dioxin treatment disrupts the AhR-AIP-hsp90 interaction. Overexpression of AIP augments the response of the CYP1A1 gene to 2,3,7,8-tetrachlorodibenzo-p-dioxin. Our data suggest that AIP influences ligand receptivity and/or nuclear targeting of AhR.
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pubmed:grant |
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8878-84
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9083006-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:9083006-Amino Acid Sequence,
pubmed-meshheading:9083006-Animals,
pubmed-meshheading:9083006-Base Sequence,
pubmed-meshheading:9083006-Carrier Proteins,
pubmed-meshheading:9083006-Cloning, Molecular,
pubmed-meshheading:9083006-Cytochrome P-450 CYP1A1,
pubmed-meshheading:9083006-Enzyme Induction,
pubmed-meshheading:9083006-HeLa Cells,
pubmed-meshheading:9083006-Humans,
pubmed-meshheading:9083006-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:9083006-Liver Neoplasms, Experimental,
pubmed-meshheading:9083006-Mice,
pubmed-meshheading:9083006-Molecular Sequence Data,
pubmed-meshheading:9083006-Proteins,
pubmed-meshheading:9083006-Receptors, Aryl Hydrocarbon,
pubmed-meshheading:9083006-Sequence Alignment,
pubmed-meshheading:9083006-Sequence Analysis, DNA,
pubmed-meshheading:9083006-Tetrachlorodibenzodioxin,
pubmed-meshheading:9083006-Transcription, Genetic,
pubmed-meshheading:9083006-Tumor Cells, Cultured
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pubmed:year |
1997
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pubmed:articleTitle |
A novel cytoplasmic protein that interacts with the Ah receptor, contains tetratricopeptide repeat motifs, and augments the transcriptional response to 2,3,7,8-tetrachlorodibenzo-p-dioxin.
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pubmed:affiliation |
Department of Molecular Pharmacology, Stanford University School of Medicine, Stanford, California 94305-5332, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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