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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
16
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pubmed:dateCreated |
1993-7-7
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pubmed:abstractText |
A subclass of erbA-related nuclear receptors has been shown to require interaction with an auxiliary protein(s) from nuclear extract in order to achieve high affinity DNA binding in vitro. The retinoid X receptor recently has been demonstrated to be such an auxiliary protein as it enhances specific DNA binding by thyroid hormone receptors, retinoic acid receptors, and the vitamin D receptor. Mutation of a highly conserved 20-amino acid region within the ligand-binding domain of thyroid hormone receptor beta disrupts its physical association with auxiliary protein from JEG-3 cells as well as with recombinant retinoid X receptor beta. The homologous 20-amino acid regions from retinoic acid receptor alpha and the vitamin D receptor also are critical determinants of the heterodimeric interaction between these receptors and JEG-3 cell auxiliary protein as well as retinoid X receptor beta. However, the same region of retinoid X receptor beta appears to play a minor, if any, role in heterodimerization. In addition, transfection studies indicate that disruption of heterodimerization impairs the ability of these receptors to function as ligand-dependent transcriptional activators.
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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/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Retinoic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Thyroid Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Retinoid X Receptors,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Tretinoin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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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 |
5
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pubmed:volume |
268
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pubmed:geneSymbol |
erbA
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11534-41
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8389356-Amino Acid Sequence,
pubmed-meshheading:8389356-Animals,
pubmed-meshheading:8389356-Carrier Proteins,
pubmed-meshheading:8389356-Cell Line,
pubmed-meshheading:8389356-DNA-Binding Proteins,
pubmed-meshheading:8389356-Humans,
pubmed-meshheading:8389356-Kinetics,
pubmed-meshheading:8389356-Macromolecular Substances,
pubmed-meshheading:8389356-Molecular Sequence Data,
pubmed-meshheading:8389356-Multigene Family,
pubmed-meshheading:8389356-Mutagenesis, Site-Directed,
pubmed-meshheading:8389356-Nuclear Proteins,
pubmed-meshheading:8389356-Proto-Oncogene Proteins,
pubmed-meshheading:8389356-Rats,
pubmed-meshheading:8389356-Receptors, Cell Surface,
pubmed-meshheading:8389356-Receptors, Retinoic Acid,
pubmed-meshheading:8389356-Receptors, Thyroid Hormone,
pubmed-meshheading:8389356-Retinoid X Receptors,
pubmed-meshheading:8389356-Sequence Homology, Amino Acid,
pubmed-meshheading:8389356-Transcription Factors,
pubmed-meshheading:8389356-Transfection,
pubmed-meshheading:8389356-Tretinoin
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pubmed:year |
1993
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pubmed:articleTitle |
Dimerization interfaces of thyroid hormone, retinoic acid, vitamin D, and retinoid X receptors.
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pubmed:affiliation |
Endocrinology Division, University of Michigan Medical Center, Ann Arbor 48109-0678.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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