ArticleGenes & development1998
A novel protein complex that interacts with the vitamin D3 receptor in a ligand-dependent manner and enhances VDR transactivation in a cell-free system.
Article in Genes & development, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.
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Who cites it
108 citing papers in PubMed, 397 citations in OpenAlex.
- The role of vitamin D receptor signaling in hair follicle health and alopecia: Current understanding and therapeutic implications.Journal of cell communication and signaling · 2026Review
- Nuclear receptor coregulator interactions: beyond the switch.Genes & development · 2026Review
- Interindividual Genetic Differences Drive Discordance Between Serum Calcidiol and Calcitriol Concentrations in Females.Endocrinology · 2025Article
- 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
- Transcriptional Cofactors for Thyroid Hormone Receptors.Endocrinology · 2025Review
- Vitamin D Receptor Regulates the Expression of the Grainyhead-Like 1 Gene.International journal of molecular sciences · 2024Article
- Genetically Engineered Mice Unveil In Vivo Roles of the Mediator Complex.International journal of molecular sciences · 2023Review
- Molecular determinants of MED1 interaction with the DNA bound VDR-RXR heterodimer.Nucleic acids research · 2020Article
- Mediator complex interaction partners organize the transcriptional network that defines neural stem cells.Nature communications · 2019Article
- Dido3-dependent SFPQ recruitment maintains efficiency in mammalian alternative splicing.Nucleic acids research · 2019Article
- The Function of the Vitamin D Receptor and a Possible Role of Enhancer RNA in Epigenomic Regulation of Target Genes: Implications for Bone Metabolism.Journal of bone metabolism · 2019Review
- Targeting an oncogenic kinase/phosphatase signaling network for cancer therapy.Acta pharmaceutica Sinica. B · 2018Review
- Cyclin C regulates adipogenesis by stimulating transcriptional activity of CCAAT/enhancer-binding protein α.The Journal of biological chemistry · 2017Article
- Regulation of metabolism by the Mediator complex.Biophysics reports · 2016Article
- Inhibitors for the Vitamin D Receptor-Coregulator Interaction.Vitamins and hormones · 2016Review
- Hepatic TRAP80 selectively regulates lipogenic activity of liver X receptor.The Journal of clinical investigation · 2015Article
- Dido3-dependent HDAC6 targeting controls cilium size.Nature communications · 2014Article
- Metformin interferes with bile acid homeostasis through AMPK-FXR crosstalk.The Journal of clinical investigation · 2014Article
- Development of novel Vitamin D Receptor-Coactivator Inhibitors.ACS medicinal chemistry letters · 2014Article
- Role of Vitamin D Metabolism and Activity on Carcinogenesis.Oncology research · 2014Review
48 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Nuclear receptors transduce hormonal signals by binding directly to DNA target sites in promoters and modulating the transcription of linked genes. Receptor-mediated transactivation appears to be potentiated in response to ligand by a number of coactivators that may provide key interactions with components of the transcription preinitiation complex and/or alter chromatin structure. Here, we use the vitamin D3 receptor ligand-binding domain (VDR LBD) as an affinity matrix to identify components of a transcriptionally active nuclear extract that interact with VDR in response to ligand. We describe the purification of a complex of at least 10 VDR interacting proteins (DRIPs) ranging from 65 to 250 kD that associate with the receptor in a strictly 1,25-dihydroxyvitamin D3-dependent manner. These proteins also appear to interact with other, but not all, nuclear receptors, such as the thyroid hormone receptor. The DRIPs are distinct from known nuclear receptor coactivators, although like these coactivators, their interaction also requires the AF-2 transactivation motif of VDR. In addition, the DRIP complex contains histone acetyltransferase activity, indicating that at least one or more of the DRIPs may function at the level of nucleosomal modification. However, we show that the DRIPs selectively enhance the transcriptional activity of VDR on a naked DNA template utilizing a cell-free, ligand-dependent transcription assay. Moreover, this activity can be specifically depleted from the extract by liganded, but not unliganded, VDR-LBD. Overexpression of DRIP100 in vivo resulted in a strong squelching of VDR transactivation, suggesting the sequestration of other limiting factors, including components of the DRIP complex. These results demonstrate the existence of a new complex of novel functional nuclear receptor coactivators.
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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.