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The hormone binding domain of the mineralocorticoid receptor can regulate heterologous activities in cis.
Journal article

The hormone binding domain of the mineralocorticoid receptor can regulate heterologous activities in cis.

  • 1994-04-15
Published in:
  • Biochemical and biophysical research communications. - 1994
Aldosterone
Animals
Base Sequence
Binding Sites
Cell Line
Chlorocebus aethiops
Codon
DNA Primers
DNA-Binding Proteins
Fungal Proteins
Kidney
Luciferases
Molecular Sequence Data
Mutagenesis, Site-Directed
Plasmids
Polymerase Chain Reaction
Protein Kinases
Receptors, Mineralocorticoid
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Transcription, Genetic
Transfection
English Steroid receptors are maintained inactive in the absence of cognate ligand partly because of repression by their hormone binding domain (HBD). Proteins complexed with the unliganded HBD of vertebrate steroid receptors, including the heat-shock protein 90, have been implicated as components of a molecular switch. As such, the HBDs of both the glucocorticoid and estrogen receptors have been shown to be autonomous regulatory cassettes which can subject heterologous activities resident on the same polypeptide to hormonal control. We show that the HBD of the mineralocorticoid receptor (MR) carries a similar "protein inactivation" function. Thus, the MR HBD can be used as a movable regulatory domain, a powerful tool for aldosterone regulation of chimeric proteins.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/145369
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