ArticleThe Journal of biological chemistry2010
Hormone binding and co-regulator binding to the glucocorticoid receptor are allosterically coupled.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
- Glucocorticoids, their uses, sexual dimorphisms, and diseases: new concepts, mechanisms, and discoveries.Physiological reviews · 2024Review
- The multivalency of the glucocorticoid receptor ligand-binding domain explains its manifold physiological activities.Nucleic acids research · 2022Article
- Corticosterone-mediated regulation and functions of miR-218-5p in rat brain.Scientific reports · 2022Article
- Dynamic allosteric communication pathway directing differential activation of the glucocorticoid receptor.Science advances · 2020Article
- Neurovascular glucocorticoid receptors and glucocorticoids: implications in health, neurological disorders and drug therapy.Drug discovery today · 2020Review
- A Model of Glucocorticoid Receptor Interaction With Coregulators Predicts Transcriptional Regulation of Target Genes.Frontiers in pharmacology · 2019Article
- Single-molecule force spectroscopy reveals folding steps associated with hormone binding and activation of the glucocorticoid receptor.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Genetically tunable frustration controls allostery in an intrinsically disordered transcription factor.eLife · 2017Article
- Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell.Chemical reviews · 2016Review
- Coupling of Conformational Transitions in the N-terminal Domain of the 51-kDa FK506-binding Protein (FKBP51) Near Its Site of Interaction with the Steroid Receptor Proteins.The Journal of biological chemistry · 2015Article
- Conformational Dynamics in FKBP Domains: Relevance to Molecular Signaling and Drug Design.Current molecular pharmacology · 2015Review
- Principles of allosteric interactions in cell signaling.Journal of the American Chemical Society · 2014Review
- Differential conformational dynamics in the closely homologous FK506-binding domains of FKBP51 and FKBP52.The Biochemical journal · 2014Article
- Article
- Rifampicin-independent interactions between the pregnane X receptor ligand binding domain and peptide fragments of coactivator and corepressor proteins.Biochemistry · 2012Article
- Structural dynamics, intrinsic disorder, and allostery in nuclear receptors as transcription factors.The Journal of biological chemistry · 2011Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glucocorticoid receptor initiates the cellular response to glucocorticoid steroid hormones in vertebrates. Co-regulator proteins dock to the receptor in response to hormone binding and potentiate the transcriptional activity of the receptor by modifying DNA and recruiting essential transcription factors like RNA polymerase II. Hormones and co-regulators bind at distinct sites in the ligand binding domain yet function cooperatively to mediate transcriptional control. This study reveals and quantifies energetic coupling between two binding sites using purified components. Using a library of peptides taken from co-regulator proteins, we determine the pattern of co-regulator binding to the glucocorticoid receptor ligand binding domain. We show that peptides from co-regulators differ in their effects on hormone binding and kinetics. Peptides from DAX1 and SRC1 bind with similar affinity, but DAX1 binding is coupled to hormone binding, and SRC1 is not. Mechanistic details of co-regulator binding and coupling to the hormone binding pocket are uncovered by analysis of properties endowed by mutation of a key residue in the allosteric network connecting the sites.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.