ArticleMolecular and cellular biology1997
Retinoid X receptor:vitamin D3 receptor heterodimers promote stable preinitiation complex formation and direct 1,25-dihydroxyvitamin D3-dependent cell-free transcription.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 72 citations in OpenAlex.
- Dysregulation and gene polymorphisms of Vitamin D receptor: its implications in lipid metabolic disorders.Molecular biology reports · 2025Review
- [Power station sun and hormone factory skin : A current assessment of the importance of vitamin D metabolism during human evolution and strategies for UV prevention].Der Hautarzt; Zeitschrift fur Dermatologie, Venerologie, und verwandte Gebiete · 2020Review
- Polymorphism of insulin-like growth factor 1 gene and its relationship with reproductive performances and milk yield in Sarda dairy sheep.Veterinary and animal science · 2020Article
- Rapid agarose gel electrophoretic mobility shift assay for quantitating protein: RNA interactions.Analytical biochemistry · 2016Article
- Polymorphism of insulin-like growth factor 1 gene and its association with litter size in Small Tail Han sheep.Molecular biology reports · 2012Article
- Dysregulation of the peroxisome proliferator-activated receptor target genes by XPD mutations.Molecular and cellular biology · 2005Article
- The histone chaperone TAF-I/SET/INHAT is required for transcription in vitro of chromatin templates.Molecular and cellular biology · 2005Article
- Crystal structures of the vitamin D receptor complexed to superagonist 20-epi ligands.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Discrete roles for peroxisome proliferator-activated receptor gamma and retinoid X receptor in recruiting nuclear receptor coactivators.Molecular and cellular biology · 2000Article
- The DRIP complex and SRC-1/p160 coactivators share similar nuclear receptor binding determinants but constitute functionally distinct complexes.Molecular and cellular biology · 2000Article
- Ligand-dependent activation of transcription in vitro by retinoic acid receptor alpha/retinoid X receptor alpha heterodimers that mimics transactivation by retinoids in vivo.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- The TRAP220 component of a thyroid hormone receptor- associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- 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.Genes & development · 1998Article
- The histone acetylase PCAF is a nuclear receptor coactivator.Genes & development · 1998Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The numerous members of the steroid/nuclear hormone receptor superfamily act as direct transducers of circulating signals, such as steroids, thyroid hormone, and vitamin or lipid metabolites, and modulate the transcription of specific target genes, primarily as dimeric complexes. The receptors for 9-cis retinoic acid and 1,25-dihydroxyvitamin D3 [1,25(OH)2D3], RXR and VDR, respectively, as members of this superfamily, form a heterodimeric complex and bind cooperatively to vitamin D responsive elements (VDREs) to activate or repress the transcription of a multitude of genes which regulate a variety of physiological functions. To directly investigate RXR- and VDR-mediated transactivation, we developed a cell-free transcription system for 1,25(OH)2D3 signaling by utilizing crude nuclear extracts and a G-free cassette-based assay. Transcriptional enhancement in vitro was dependent on purified, exogenous RXR and VDR and was responsive to physiological concentrations of 1,25(OH)2D3. We found that RXR and VDR transactivated selectively from VDRE-linked templates exclusively as a heterodimeric complex, since neither receptor alone enhanced transcription in vitro. By the addition of low concentrations of the anionic detergent Sarkosyl to limit cell-free transcription to a single round and the use of agarose gel mobility shift experiments to assay factor complex assembly, we observed that 1,25(OH)2D3 enhanced RXR:VDR-mediated stabilization or assembly of preinitiation complexes to effect transcriptional enhancement from VDRE-linked promoter-containing DNA.
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Registered trials
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.