ArticleJournal of molecular endocrinology2022
Retinoic acid receptor structures: the journey from single domains to full-length complex.
Article in Journal of molecular endocrinology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- A Novel SXXLF Motif in the FXR N-Terminal Domain Mediates Coregulator and Interdomain Interactions.Chembiochem : a European journal of chemical biology · 2026Article
- Retinoid-X receptor action and disruption in development.Developmental biology · 2026Review
- Review
- The role of RARG in solid tumor progression and therapeutic potential.Discover oncology · 2026Review
- Molecular mechanism of the crosstalk between glucocorticoid receptor (GR) and hypoxia-inducible factor 3α (HIF-3α) pathways.Marine life science & technology · 2025Article
- New structural insights into the control of the retinoic acid receptors RAR/RXR by DNA, ligands, and transcriptional coregulators.Nucleic acids research · 2025Article
- Pharmacological targeting of BMAL1 modulates circadian and immune pathways.Nature chemical biology · 2025Article
- ALDH1A1 in breast cancer: A prospective target to overcome therapy resistance (Review).Oncology letters · 2025Review
- Targeting AFP-RARβ complex formation: a potential strategy for treating AFP-positive hepatocellular carcinoma.Molecular diversity · 2025Article
- Retinoid X receptor agonist 9CDHRA mitigates retinal ganglion cell apoptosis and neuroinflammation in a mouse model of glaucoma.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Simulations Reveal Unique Roles for the FXR Hinge in the FXR-RXR Nuclear Receptor Heterodimer.ACS bio & med chem Au · 2025Article
- Structural basis for the ligand-dependent activation of heterodimeric AHR-ARNT complex.Nature communications · 2025Article
- Surprising features of nuclear receptor interaction networks revealed by live-cell single-molecule imaging.eLife · 2025Article
- Pulse Activation of Retinoic Acid Receptor Enhances Hematopoietic Stem Cell Homing by Controlling CXCR4 Membrane Presentation.Stem cell reviews and reports · 2025Article
- Characterization of gut microbiome dysbiosis in calcium oxalate stone patients with comorbid metabolic syndrome.Frontiers in microbiology · 2025Article
- Targeting catalase in cancer.Redox biology · 2024Review
- Surprising Features of Nuclear Receptor Interaction Networks Revealed by Live Cell Single Molecule Imaging.bioRxiv : the preprint server for biology · 2024Article
- Oxidative Stress and the Nrf2/PPARγ Axis in the Endometrium: Insights into Female Fertility.Cells · 2024Review
- Article
- Retinoic acid receptor activation reprograms senescence response and enhances anti-tumor activity of natural killer cells.Cancer cell · 2024Article
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1 author.
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Abstract
The retinoic acid receptors (RARα, β, and γ) are multi-domain polypeptides that heterodimerize with retinoid X receptors (RXRα, β, and γ) to form functional transcription factors. Understanding the three-dimensional molecular organization of these nuclear receptors (NRs) began with RAR and RXR DNA-binding domains (DBDs), and were followed with studies on isolated ligand-binding domains (LBDs). The more complete picture emerged in 2017 with the multi-domain crystal structure of RXRα-RARβ on its response element with retinoic acid molecules and coactivator segments on both proteins. The analysis of that structure and its complementary studies have clarified the direct communication pathways within RXR-RAR polypeptides, through which DNA binding, protein-ligand, and protein-protein interactions are integrated for overall functional responses. Understanding the molecular connections in the RXR-RAR complex has benefited from direct observations of the multi-domain structures of RXRα-PPARγ, RXRα-LXRβ, HNF-4α homodimer, and androgen receptor homodimer, each bound to its response element. These comprehensive NR structures show unique quaternary architectures, yet all have DBD-DBD, LBD-LBD, and DBD-LBD domain-domain contacts within them. These convergence zones allow signals from discrete domains of their polypeptides to be propagated and integrated across their entire complex, shaping their overall responses in an allosteric fashion.
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