ArticleMolecular and cellular biology2001
Determinants of CoRNR-dependent repression complex assembly on nuclear hormone receptors.
Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed.
- Stomach at the crossroads: nuclear receptor signaling at the interface between what we are and what we eat.Physiological reviews · 2026Review
- Nuclear receptor coregulator interactions: beyond the switch.Genes & development · 2026Review
- Negative regulation of TbioRxiv : the preprint server for biology · 2026Article
- New structural insights into the control of the retinoic acid receptors RAR/RXR by DNA, ligands, and transcriptional coregulators.Nucleic acids research · 2025Article
- An intrinsically disordered region controlling condensation of a circadian clock component and rhythmic transcription in the liver.Molecular cell · 2023Article
- The psychiatric risk gene BRD1 modulates mitochondrial bioenergetics by transcriptional regulation.Translational psychiatry · 2022Article
- Role of Peroxisome Proliferator-Activated Receptors (PPARs) in Energy Homeostasis of Dairy Animals: Exploiting Their Modulation through Nutrigenomic Interventions.International journal of molecular sciences · 2021Review
- Endogenous and combination retinoids are active in myelomonocytic leukemias.Haematologica · 2021Article
- Strategies for developing pregnane X receptor antagonists: Implications from metabolism to cancer.Medicinal research reviews · 2020Review
- PPARγ S273 Phosphorylation Modifies the Dynamics of Coregulator Proteins Recruitment.Frontiers in endocrinology · 2020Article
- Regulation of RXR-RAR Heterodimers by RXR- and RAR-Specific Ligands and Their Combinations.Cells · 2019Article
- Integrative regulation of physiology by histone deacetylase 3.Nature reviews. Molecular cell biology · 2019Review
- Binding mode prediction and MD/MMPBSA-based free energy ranking for agonists of REV-ERBα/NCoR.Journal of computer-aided molecular design · 2017Article
- Short linear motif acquisition, exon formation and alternative splicing determine a pathway to diversity for NCoR-family co-repressors.Open biology · 2015Article
- Molecular mechanisms of transcriptional control by Rev-erbα: An energetic foundation for reconciling structure and binding with biological function.Protein science : a publication of the Protein Society · 2015Article
- Nuclear receptor Rev-erbα: up, down, and all around.Trends in endocrinology and metabolism: TEM · 2014Review
- Inhibition of HDAC3 promotes ligand-independent PPARγ activation by protein acetylation.Journal of molecular endocrinology · 2014Article
- Structural insights into selective agonist actions of tamoxifen on human estrogen receptor alpha.Journal of molecular modeling · 2014Article
- The adenovirus 55 residue E1A protein is a transcriptional activator and binds the unliganded thyroid hormone receptor.The Journal of general virology · 2014Article
- Nuclear receptor corepressor complexes in cancer: mechanism, function and regulation.American journal of clinical and experimental urology · 2014Review
3 more citing papers are in PubMed but not listed here.
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Abstract
Ligand-dependent exchange of coactivators and corepressors is the fundamental regulator of nuclear hormone receptor (NHR) function. The interaction surfaces of coactivators and corepressors are similar but distinct enough to allow the ligand to function as a switch. Multiple NHRs share features that allow corepressor binding, and each of two distinct corepressors (N-CoR and SMRT) contains two similar CoRNR motifs that interact with NHRs. Here we report that the specificity of corepressor-NHR interaction is determined by the individual NHR interacting with specific CoRNR boxes within a preferred corepressor. First, receptors have distinct preferences for CoRNR1 versus CoRNR2. For example, the retinoic acid receptor binds CoRNR1, while RXR interacts almost exclusively with CoRNR2. Second, the NHR preference for N-CoR or SMRT is due to differences in CoRNR1 but not CoRNR2. Moreover, within a single corepressor, affinity for different NHRs is determined by distinct regions flanking CoRNR1. The highly specific determinants of NHR-corepressor interaction and preference suggest that repression is regulated by the permissibility of selected receptor-CoRNR-corepressor combinations. Interestingly, different NHR surfaces contribute to binding of CoRNR1 and CoRNR2, suggesting a model to explain corepressor binding to NHR heterodimers.
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