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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2000-10-3
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pubmed:abstractText |
The autonomous activation function-2 (AF-2) in the mineralocorticoid receptor (MR) E/F domain is known to play a major role in the ligand-induced transactivation function of MR; however, it remained unclear about the transactivation function of its A/B domain. We therefore tried to characterize the MR A/B domain as the AF-1 and further studied the actions of known coactivators for AF-2 in the E/F ligand-binding domain in the function of the MR A/B domain. Deletion analyses of rat and human MRs revealed that the A/B domains harbor a transactivation function acting as AF-1. The MR mutant (E959Q) with a point mutation in helix 12, which causes a complete loss of MR AF-2 activity, still retained ligand-induced transactivation function, indicating a significant role for AF-1 in the full activity of the ligand-induced MR function. Among the coactivators tested to potentiate the MR AF-2, TIF2 and p300 potentiated the MR AF-1 through two different core regions [amino acids (a.a.) 1-169, a.a. 451-603] and exhibited functional interactions with the MR A/B domain in the cultured cells. However, such interactions were undetectable in a yeast and in an in vitro glutathione-S-transferase pull-down assay, indicating that the functional interaction of TIF2 and p300 with the MR A/B domain to support the MR AF-1 activity require some unknown nuclear factor(s) or a proper modification of the A/B domain in the cells.
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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/E1A-Associated p300 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Ep300 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/NCOA2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ncoa2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Receptor Coactivator 2,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Mineralocorticoid,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0888-8809
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
889-99
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:10847590-Animals,
pubmed-meshheading:10847590-Blotting, Western,
pubmed-meshheading:10847590-COS Cells,
pubmed-meshheading:10847590-E1A-Associated p300 Protein,
pubmed-meshheading:10847590-Escherichia coli,
pubmed-meshheading:10847590-Gene Deletion,
pubmed-meshheading:10847590-Genetic Vectors,
pubmed-meshheading:10847590-Glutathione Transferase,
pubmed-meshheading:10847590-Humans,
pubmed-meshheading:10847590-Nuclear Proteins,
pubmed-meshheading:10847590-Nuclear Receptor Coactivator 2,
pubmed-meshheading:10847590-Point Mutation,
pubmed-meshheading:10847590-Rats,
pubmed-meshheading:10847590-Receptors, Mineralocorticoid,
pubmed-meshheading:10847590-Recombinant Fusion Proteins,
pubmed-meshheading:10847590-Saccharomyces cerevisiae,
pubmed-meshheading:10847590-Structure-Activity Relationship,
pubmed-meshheading:10847590-Trans-Activators,
pubmed-meshheading:10847590-Transcription Factors,
pubmed-meshheading:10847590-Transcriptional Activation,
pubmed-meshheading:10847590-Transfection
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pubmed:year |
2000
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pubmed:articleTitle |
Characterization of transactivational property and coactivator mediation of rat mineralocorticoid receptor activation function-1 (AF-1).
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pubmed:affiliation |
Pharmacological Research Department, Teikoku Hormone Manufacturing Company, Ltd., Tokyo, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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