DNA sequences that act as high affinity targets for the vitamin D3 receptor in the absence of the retinoid X receptor

1994 ◽  
Vol 8 (3) ◽  
pp. 265-273 ◽  
Author(s):  
L. P. Freedman
Keyword(s):  
Vitamin D3 ◽  
Dna Sequences ◽  
Retinoid X Receptor ◽  
D3 Receptor ◽  
Vitamin D3 Receptor ◽  
High Affinity

scholarly journals Interaction of Two Novel 14-Epivitamin D3 Analogs with Vitamin D3 Receptor-Retinoid X Receptor Heterodimers on Vitamin D3 Responsive Elements

2001 ◽  
Vol 16 (4) ◽  
pp. 625-638 ◽  
Author(s):  
Lieve Verlinden ◽  
Annemieke Verstuyf ◽  
Marcus Quack ◽  
Mark Van Camp ◽  
Evelyne Van Etten ◽  
...  
Keyword(s):  
Vitamin D3 ◽  
Retinoid X Receptor ◽  
D3 Receptor ◽  
Vitamin D3 Receptor

Impact of the Vitamin D3 receptor on growth-regulatory pathways in mammary gland and breast cancer

2002 ◽  
Vol 83 (1-5) ◽  
pp. 85-92 ◽  
Author(s):  
JoEllen Welsh ◽  
Jennifer A. Wietzke ◽  
Glendon M. Zinser ◽  
Sarah Smyczek ◽  
Saara Romu ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Mammary Gland ◽  
Vitamin D3 ◽  
D3 Receptor ◽  
Regulatory Pathways ◽  
Vitamin D3 Receptor

Ligand modulates the conversion of DNA-bound vitamin D3 receptor (VDR) homodimers into VDR-retinoid X receptor heterodimers

1994 ◽  
Vol 14 (5) ◽  
pp. 3329-3338
Author(s):  
B Cheskis ◽  
L P Freedman
Keyword(s):  
Ligand Binding ◽  
Vitamin D3 ◽  
Hormone Receptors ◽  
Steroid Receptors ◽  
Dependent Manner ◽  
D3 Receptor ◽  
Vitamin D3 Receptor ◽  
Binding Domains

Protein dimerization facilitates cooperative, high-affinity interactions with DNA. Nuclear hormone receptors, for example, bind either as homodimers or as heterodimers with retinoid X receptors (RXR) to half-site repeats that are stabilized by protein-protein interactions mediated by residues within both the DNA- and ligand-binding domains. In vivo, ligand binding among the subfamily of steroid receptors unmasks the nuclear localization and DNA-binding domains from a complex with auxiliary factors such as the heat shock proteins. However, the role of ligand is less clear among nuclear receptors, since they are constitutively localized to the nucleus and are presumably associated with DNA in the absence of ligand. In this study, we have begun to explore the role of the ligand in vitamin D3 receptor (VDR) function by examining its effect on receptor homodimer and heterodimer formation. Our results demonstrate that VDR is a monomer in solution; VDR binding to a specific DNA element leads to the formation of a homodimeric complex through a monomeric intermediate. We find that 1,25-dihydroxyvitamin D3, the ligand for VDR, decreases the amount of the DNA-bound VDR homodimer complex. It does so by significantly decreasing the rate of conversion of DNA-bound monomer to homodimer and at the same time enhancing the dissociation of the dimeric complex. This effectively stabilizes the bound monomeric species, which in turn serves to favor the formation of a VDR-RXR heterodimer. The ligand for RXR, 9-cis retinoic acid, has the opposite effect of destabilizing the heterodimeric-DNA complex. These results may explain how a nuclear receptor can bind DNA constitutively but still act to regulate transcription in a fully hormone-dependent manner.

Mechanisms of gene regulation by vitamin D3 receptor: a network of coactivator interactions

Gene ◽  
2000 ◽  
Vol 246 (1-2) ◽  
pp. 9-21 ◽  
Author(s):  
Christophe Rachez ◽  
Leonard P. Freedman
Keyword(s):  
Gene Regulation ◽  
Vitamin D3 ◽  
D3 Receptor ◽  
Vitamin D3 Receptor
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