ArticleNucleic acids research2020
Molecular determinants of MED1 interaction with the DNA bound VDR-RXR heterodimer.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 46 citations in OpenAlex.
- Beyond bones, vitamin D as a sunshine hormone in type 2 diabetes mellitus and its complications.iScience · 2026Review
- Vitamin D and Metabolic Dysfunction-Associated Steatotic Liver Disease: Molecular Mechanisms and Clinical Implications-A Narrative Review.International journal of molecular sciences · 2026Review
- Genetic, Clinical and Neuroradiological Spectrum of MED-Related Disorders: An Updated Review.Genes · 2025Review
- Deciphering the causal relationships between plasma metabolites, peripheral cells, inflammatory factors and DLBCL for discovering novel therapeutic targets.Discover oncology · 2025Article
- The Mediator Complex: A Regulatory Hub for Transcriptional Activity of Nuclear Receptors.Cells · 2025Review
- 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
- An IDR-dependent mechanism for nuclear receptor control of Mediator interaction with RNA polymerase II.Molecular cell · 2024Article
- Regulation of the RNA polymerase II pre-initiation complex by its associated coactivators.Nature reviews. Genetics · 2023Review
- A structural mechanism of nuclear receptor biased agonism.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Mediator complex as a master regulator of transcription by RNA polymerase II.Nature reviews. Molecular cell biology · 2022Review
- Vitamin D and Its Receptor from a Structural Perspective.Nutrients · 2022Review
- Vitamin D and Its Target Genes.Nutrients · 2022Review
- Conformational Changes of RORγ During Response Element Recognition and Coregulator Engagement.Journal of molecular biology · 2021Article
- Biological evaluation and synthesis of calcitroic acid.Bioorganic chemistry · 2021Review
- Super-enhancer-associated TMEM44-AS1 aggravated glioma progression by forming a positive feedback loop with Myc.Journal of experimental & clinical cancer research : CR · 2021Article
- What do Transcription Factors Interact With?Journal of molecular biology · 2021Review
- Structure of the human Mediator-bound transcription preinitiation complex.Science (New York, N.Y.) · 2021Article
- Structure of mammalian Mediator complex reveals Tail module architecture and interaction with a conserved core.Nature communications · 2021Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The MED1 subunit of the Mediator complex is an essential coactivator of nuclear receptor-mediated transcriptional activation. While structural requirements for ligand-dependent binding of classical coactivator motifs of MED1 to numerous nuclear receptor ligand-binding domains have been fully elucidated, the recognition of the full-length or truncated coactivator by full nuclear receptor complexes remain unknown. Here we present structural details of the interaction between a large part of MED1 comprising its structured N-terminal and the flexible receptor-interacting domains and the mutual heterodimer of the vitamin D receptor (VDR) and the retinoid X receptor (RXR) bound to their cognate DNA response element. Using a combination of structural and biophysical methods we show that the ligand-dependent interaction between VDR and the second coactivator motif of MED1 is crucial for complex formation and we identify additional, previously unseen, interaction details. In particular, we identified RXR regions involved in the interaction with the structured N-terminal domain of MED1, as well as VDR regions outside the classical coactivator binding cleft affected by coactivator recruitment. These findings highlight important roles of each receptor within the heterodimer in selective recognition of MED1 and contribute to our understanding of the nuclear receptor-coregulator complexes.
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