ArticleProceedings of the National Academy of Sciences of the United States of America1995
Transcription factor TFIIB and the vitamin D receptor cooperatively activate ligand-dependent transcription.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 212 citations in OpenAlex.
- Vitamin D Receptor Regulates the Expression of the Grainyhead-Like 1 Gene.International journal of molecular sciences · 2024Article
- Mutations in the vitamin D receptor and hereditary vitamin D-resistant rickets.BoneKEy reports · 2014Review
- Small-molecule hormones: molecular mechanisms of action.International journal of endocrinology · 2013Article
- Vitamin D resistance and colon cancer prevention.Carcinogenesis · 2012Review
- The role of vitamin D receptor mutations in the development of alopecia.Molecular and cellular endocrinology · 2011Review
- Runx2 control of organization, assembly and activity of the regulatory machinery for skeletal gene expression.Oncogene · 2004Review
- Nuclear microenvironments support physiological control of gene expression.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2003Review
- Novel ATPase of SNF2-like protein family interacts with androgen receptor and modulates androgen-dependent transcription.Molecular biology of the cell · 2002Article
- Interaction of the 1alpha,25-dihydroxyvitamin D3 receptor at the distal promoter region of the bone-specific osteocalcin gene requires nucleosomal remodelling.The Biochemical journal · 2002Article
- Human TAF(II)55 interacts with the vitamin D(3) and thyroid hormone receptors and with derivatives of the retinoid X receptor that have altered transactivation properties.Molecular and cellular biology · 1999Article
- Oestrogen receptor facilitates the formation of preinitiation complex assembly: involvement of the general transcription factor TFIIB.The Biochemical journal · 1998Article
- Activation of androgen receptor function by a novel nuclear protein kinase.Molecular biology of the cell · 1998Article
- Identification of a novel RING finger protein as a coregulator in steroid receptor-mediated gene transcription.Molecular and cellular biology · 1998Article
- The corepressor N-CoR and its variants RIP13a and RIP13Delta1 directly interact with the basal transcription factors TFIIB, TAFII32 and TAFII70.Nucleic acids research · 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
- TFIID (TBP) stabilizes the binding of MyoD to its DNA site at the promoter and MyoD facilitates the association of TFIIB with the preinitiation complex.Nucleic acids research · 1998Article
- Functional interaction of the bovine papillomavirus E2 transactivation domain with TFIIB.Journal of virology · 1998Article
- Retinoid X receptor:vitamin D3 receptor heterodimers promote stable preinitiation complex formation and direct 1,25-dihydroxyvitamin D3-dependent cell-free transcription.Molecular and cellular biology · 1997Article
- Role of hydrophobic amino acid clusters in the transactivation activity of the human glucocorticoid receptor.Molecular and cellular biology · 1997Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The active metabolite of vitamin D, 1,25-dihydroxyvitamin D3 [1,25(OH)2D3], regulates gene transcription through binding to the vitamin D receptor (VDR), a member of the nuclear hormone receptor superfamily. Sequence-specific transcription factors, including nuclear hormone receptors, are thought to interact with the basal transcription complex to regulate transcription. In glutathione S-transferase fusion-based protein-protein binding assays we found that VDR specifically binds to TFIIB, a component of the basal complex, and that the interaction requires select domains of each protein. To assess the functional significance of this interaction, transfection assays were performed with a 1,25(OH)2D3-responsive reporter construct. In P19 embryonal carcinoma cells cotransfection of VDR and TFIIB cooperatively activated reporter transcription, while each factor alone gave very low to no activation. This activation was dependent on 1,25(OH)2D3 and the dose of TFIIB and VDR transfected, demonstrating that a nuclear hormone receptor functionally interacts with TFIIB in vivo. In contrast, transfection of NIH 3T3 cells generated strong reporter activation by 1,25(OH)2D3 in the presence of VDR alone, and cotransfection of TFIIB led to specific dose-dependent repression of reporter activity. Taken together, these results indicate that TFIIB-nuclear hormone receptor interaction plays a critical role in ligand-dependent transcription, which is apparently modulated by a cell-type-specific accessory factor.
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