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• W2597367890 abstract "Without a glucocorticoid (GC) ligand, the transcription factor glucocorticoid receptor (GR) is largely cytoplasmic, with its GC-binding domain held in high affinity conformation by a cluster of chaperones. Binding a GC causes serial dis- and re-associations with chaperones, translocation of the GR to the nucleus, where it binds to DNA sites and associates with coregulatory proteins and basic transcription complexes. Herein, we describe the effects of a potent protective osmolyte, trimethylamine N-oxide (TMAO), on a conditions-dependent activation-labile mutant GR (GRact/l), which under GR-activating conditions cannot bind GCs in cells or in cell cytosols. In both cells and cytosols, TMAO restores binding to GRact/l by stabilizing it in complex with chaperones. Cells bathed in much lower concentrations of TMAO than those required in vitro show restoration of GC binding, presumably due to intracellular molecular crowding effects." @default.
• W2597367890 created "2017-03-23" @default.
• W2597367890 creator A5006537594 @default.
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• W2597367890 date "2017-03-16" @default.
• W2597367890 modified "2023-10-15" @default.
• W2597367890 title "Restored mutant receptor:Corticoid binding in chaperone complexes by trimethylamine N-oxide" @default.
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• W2597367890 doi "https://doi.org/10.1371/journal.pone.0174183" @default.
• W2597367890 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5354453" @default.
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• W2597367890 hasPublicationYear "2017" @default.
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