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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2003-1-28
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pubmed:abstractText |
Receptor interacting protein 140 (RIP140) interacts with retinoic acid receptor (RAR) and retinoid X receptor (RXR) constitutively, but hormone binding enhances this interaction. The ligand-independent interaction is mediated by the amino and central regions of RIP140 which contain a total of nine copies of the LXXLL motif, whereas the agonist-induced interaction is mediated by its carboxyl terminus which contains a novel motif (1063-1076, LTKTNPILYYMLQK). The ligand-independent interaction could be enhanced slightly by agonists, whereas the ligand-dependent interaction was strictly agonist dependent for both RAR and RXR. In the context of heterodimers, ligand occupancy of RXR played a more dominant role for both molecular interaction and biological activity of RIP140. Competition and mutation studies demonstrated an essential role for (1067)Asn and (1073)Met for a ligand-dependent interaction. A model was proposed to address the constitutive and agonist-dependent interaction of RIP140 with RAR/RXR.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Retinoic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Retinoid X Receptors,
http://linkedlifedata.com/resource/pubmed/chemical/Retinoids,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/nuclear receptor interacting...
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-2960
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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 |
42
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
971-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12549917-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:12549917-Amino Acid Sequence,
pubmed-meshheading:12549917-Animals,
pubmed-meshheading:12549917-Binding, Competitive,
pubmed-meshheading:12549917-COS Cells,
pubmed-meshheading:12549917-Cercopithecus aethiops,
pubmed-meshheading:12549917-Dimerization,
pubmed-meshheading:12549917-Ligands,
pubmed-meshheading:12549917-Models, Chemical,
pubmed-meshheading:12549917-Molecular Sequence Data,
pubmed-meshheading:12549917-Nuclear Proteins,
pubmed-meshheading:12549917-Peptide Fragments,
pubmed-meshheading:12549917-Protein Binding,
pubmed-meshheading:12549917-Receptors, Retinoic Acid,
pubmed-meshheading:12549917-Repressor Proteins,
pubmed-meshheading:12549917-Retinoid X Receptors,
pubmed-meshheading:12549917-Retinoids,
pubmed-meshheading:12549917-Transcription Factors,
pubmed-meshheading:12549917-Transfection
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pubmed:year |
2003
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pubmed:articleTitle |
Effects of retinoid ligands on RIP140: molecular interaction with retinoid receptors and biological activity.
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pubmed:affiliation |
Department of Pharmacology and Biochemistry, University of Minnesota Medical School, Minneapolis, Minnesota 55455, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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