ArticleThe Journal of biological chemistry2020
Agonist binding directs dynamic competition among nuclear receptors for heterodimerization with retinoid X receptor.
Article in The Journal of biological chemistry, 2020. 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, 43 citations in OpenAlex.
- Randomized Controlled Clinical Trial of Pediatric Pneumococcus and Hepatitis A Vaccinations With or Without a High-Dose Oral Vitamin A Supplement.Biomolecules · 2025Trial
- Genome-wide chromatin profiling reveals a nonlimiting role for RXR in macrophage-like cells stimulated with multiple nuclear receptor agonists.The Journal of biological chemistry · 2026Article
- Retinoid-X receptor action and disruption in development.Developmental biology · 2026Review
- Astragaloside IV inhibits the progression of hypertensive heart disease via the RXRA/PPARG/SIRT3 axis.Journal of molecular medicine (Berlin, Germany) · 2025Article
- Dietary Supplementation with Chenodeoxycholic Acid or Ursodeoxycholic Acid Modulates Growth, Thyroid Status, and Hepatopancreatic-Intestinal Health in Juvenile Little Yellow CroakerAntioxidants (Basel, Switzerland) · 2025Article
- An in silico to in vivo approach identifies retinoid-X receptor activating tert-butylphenols used in food contact materials.Scientific reports · 2025Article
- Article
- Genomic regions occupied by both RARα and VDR are involved in the convergence and cooperation of retinoid and vitamin D signaling pathways.Nucleic acids research · 2025Article
- Surprising features of nuclear receptor interaction networks revealed by live-cell single-molecule imaging.eLife · 2025Article
- Investigating the Role and Underlying Mechanisms of 18β-Glycyrrhetinic Acid in the Therapy of Ulcerative Colitis Through Modulation of the PPAR-γ/NF-κB Signaling Pathway.Journal of inflammation research · 2025Article
- Surprising Features of Nuclear Receptor Interaction Networks Revealed by Live Cell Single Molecule Imaging.bioRxiv : the preprint server for biology · 2024Article
- A multidisciplinary approach disclosing unexplored Aflatoxin B1 roles in severe impairment of vitamin D mechanisms of action.Cell biology and toxicology · 2023Article
- How Estrogen, Testosterone, and Sex Differences Influence Serum Immunoglobulin Isotype Patterns in Mice and Humans.Viruses · 2023Article
- Agonist-controlled competition of RAR and VDR nuclear receptors for heterodimerization with RXR is manifested in their DNA binding.The Journal of biological chemistry · 2023Article
- Retinol Binding Protein, Sunlight Hours, and the Influenza Virus-Specific Immune Response.Biomedicines · 2022Article
- Vitamin D and Its Receptor from a Structural Perspective.Nutrients · 2022Review
- Doxorubicin impacts chromatin binding of HMGB1, Histone H1 and retinoic acid receptor.Scientific reports · 2022Article
- Cooperativity as quantification and optimization paradigm for nuclear receptor modulators.Chemical science · 2022Article
- RXRA DT448/9PP generates a dominant active variant capable of inducing maturation in acute myeloid leukemia cells.Haematologica · 2022Article
- Transcriptome shifts triggered by vitamin A and SCD genotype interaction in Duroc pigs.BMC genomics · 2022Article
Corrections and comments
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Authors and funding
13 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Retinoid X receptor (RXR) plays a pivotal role as a transcriptional regulator and serves as an obligatory heterodimerization partner for at least 20 other nuclear receptors (NRs). Given a potentially limiting/sequestered pool of RXR and simultaneous expression of several RXR partners, we hypothesized that NRs compete for binding to RXR and that this competition is directed by specific agonist treatment. Here, we tested this hypothesis on three NRs: peroxisome proliferator-activated receptor gamma (PPARγ), vitamin D receptor (VDR), and retinoic acid receptor alpha (RARα). The evaluation of competition relied on a nuclear translocation assay applied in a three-color imaging model system by detecting changes in heterodimerization between RXRα and one of its partners (NR1) in the presence of another competing partner (NR2). Our results indicated dynamic competition between the NRs governed by two mechanisms. First, in the absence of agonist treatment, there is a hierarchy of affinities between RXRα and its partners in the following order: RARα > PPARγ > VDR. Second, upon agonist treatment, RXRα favors the liganded partner. We conclude that recruiting RXRα by the liganded NR not only facilitates a stimulus-specific cellular response but also might impede other NR pathways involving RXRα.
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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.