Abstract
The mineralocorticoid and glucocorticoid receptors (MR and GR, respectively) are members of the intracellular receptor superfamily that bind as homodimers to the same hormone response elements (HREs). Physiological evidence suggests that MR and GR interact with each other in cells that express both receptors, implying that they might directly interact in the regulation of transcription initiation. Indeed, we have found that coexpressed MR and GR interact functionally at the transcriptional level and furthermore that they interact physically through heterodimer formation at a shared HRE in vitro and in vivo. We suggest from these findings that heterodimerization may play an important role in steroid receptor transcriptional regulation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alcohol Dehydrogenase / genetics
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Amino Acid Sequence
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Animals
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Base Sequence
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Cell Line
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Chlorocebus aethiops
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DNA-Binding Proteins / biosynthesis
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / metabolism*
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Drosophila
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Luciferases / biosynthesis
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Macromolecular Substances
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Oligodeoxyribonucleotides
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Point Mutation
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Promoter Regions, Genetic
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Protein Conformation
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Protein Multimerization
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Rats
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Receptors, Glucocorticoid / biosynthesis
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Receptors, Glucocorticoid / chemistry*
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Receptors, Glucocorticoid / metabolism*
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Receptors, Mineralocorticoid / biosynthesis
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Receptors, Mineralocorticoid / chemistry*
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Receptors, Mineralocorticoid / metabolism*
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Transcription, Genetic
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Transfection
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Zinc Fingers
Substances
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DNA-Binding Proteins
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Macromolecular Substances
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Oligodeoxyribonucleotides
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Receptors, Glucocorticoid
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Receptors, Mineralocorticoid
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Recombinant Proteins
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Alcohol Dehydrogenase
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Luciferases