Journal of Molecular Biology
Regular ArticleAgonist-triggered Modulation of the Activated and Silent State of the Vitamin D3 Receptor by Interaction with Co-repressors and Co-activators☆,☆☆
References (37)
- et al.
Crystal structure of the nuclear receptor for vitamin D bound to its natural ligand
Mol. Cell
(2000) - et al.
The nuclear receptor ligand-binding domain: structure and function
Curr. Opin. Cell Biol.
(1998) - et al.
Metabolism of the vitamin D analog EB1089: identification of in vivo and in vitro liver metabolites and their biological activities
Biochem. Pharmacol.
(1997) - et al.
EB1089: a new vitamin D analogue that inhibits the growth of breast cancer cells in vivo and in vitro
Biochem. Pharmacol.
(1992) - et al.
Ligand-dependent conformational changes in thyroid hormone and retinoic acid receptors are potentially enhanced by heterodimerization with retinoid X receptor
J. Steroid Biochem. Mol. Biol.
(1993) - et al.
Distinct conformational changes induced by 20-epi analogues of 1α,25- dihydroxyvitamin D3 are associated with enhanced activation of the vitamin D receptor
J. Biol. Chem.
(1995) - et al.
Differential interaction of 1α,25-dihydroxyvitamin D3 analogues and their 20-epi homologues with the vitamin D receptor
J. Biol. Chem.
(1997) - et al.
Antagonistic action of a 25-carboxylic ester analogue of 1α,25-dihydroxyvitamin D3 is mediated by a lack of ligand-induced vitamin D receptor interaction with co-activators
J. Biol. Chem.
(2000) - et al.
Dynamic stabilization of nuclear receptor ligand binding domains by hormone or co-repressor binding
Mol. Cell
(2000) - et al.
Co-activators and co-repressors in the integration of transcriptional responses
Curr. Opin. Cell Biol.
(1998)
Functional characterization of a 1,25-dihydroxyvitamin D3 receptor binding site found in the rat atrial natriuretic factor promoter
Biochem. Biophys. Res. Commun.
Gene regulation by vitamin D3
Crit. Rev. Eukaryot. Gene Expr.
The vitamin D3 receptor in the context of the nuclear receptor superfamily: the central role of retinoid X receptor
Endocrine
Mechanisms of nuclear signalling by vitamin D3. Interplay with retinoid and thyroid hormone signalling
Eur. J. Biochem.
Ligand- independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor
Nature
Alien, a highly conserved protein with characteristics of a co-repressor for members of the nuclear hormone receptor superfamily
Mol. Cell. Biol.
Coactivation and corepression in transcriptional regulation by steroid/nuclear hormone receptors
Crit. Rev. Eukaryot. Gene Expr.
Steroid receptor co-activator-1 is a histone acetyltransferase
Nature
Cited by (44)
Genomic signaling of vitamin D
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2017, Molecular and Cellular EndocrinologyCitation Excerpt :This epigenetic event decreases the concentration of available 1,25(OH)2D3 within the tumor tissue. The second level of interaction of vitamin D endocrinology with the epigenome comprises direct protein-protein interaction of VDR with chromatin components, such as members of the Mediator complex (Rachez et al., 1999) or co-activators of the NCOA family (Herdick and Carlberg, 2000), which have HAT activity leading to local chromatin opening. In turn, the interaction of VDR with co-repressor proteins, such as NCOR1 (Polly et al., 2000), mediates the contact with HDACs that close chromatin at the respective genomic loci.
Vitamin D Signaling Modulators in Cancer Therapy
2016, Vitamins and HormonesCitation Excerpt :In some cases, multiple copies of the VDREs are positioned not only in the proximal promoter but dispersed up to several thousand kilobases of 5′ of the transcription start site in vitamin D responsive genes (Vaisanen, Dunlop, Sinkkonen, Frank, & Carlberg, 2005). Transcription activation through 1,25D3 and VDR is enhanced by nuclear receptor coactivator proteins such as steroid receptor coactivators, vitamin D receptor interacting protein complexes (Barletta, Freedman, & Christakos, 2002; Herdick & Carlberg, 2000; MacDonald, Baudino, Tokumaru, Dowd, & Zhang, 2001; Zhang et al., 2003). In addition, 1,25D3 may act independent of VDR/DNA binding through nongenomic pathways (Norman et al., 1992).
Components of the CCR4-NOT complex function as nuclear hormone receptor coactivators via association with the NRC-interacting factor NIF-1
2008, Journal of Biological Chemistry
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Abbreviations used: 1α,25(OH)2D3, 1α,25-dihydroxyvitamin D3; AF-2, (trans) activation function-2; ANF, atrial natriuretic factor; c1LPD, agonistic conformation; c3LPD, non-agonistic conformation; DR3, direct repeat spaced by three nucleotides; EC50, half maximal activation; FBS, fetal bovine serum; GST, glutathione S-transferase; IPTG, isopropyl-β-d-thio-galactopyranoside; LPD, limited protease digestion; LBD, ligand binding domain; NCoR, nuclear receptor co-repressor; RXR, retinoid X receptor; SRC-1, steroid receptor co-activator-1; VDR, 1α,25(OH)2D3 receptor; VDRE, 1α,25(OH)2D3 response element; DMSO, dimethylsulfoxide
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Edited by J. Karn
- f1
Corresponding author
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E-mail address of the corresponding author: [email protected]