Mapping the Domains of the Interaction of the Vitamin D Receptor and Steroid Receptor Coactivator-1

1997 ◽  
Vol 12 (1) ◽  
pp. 57-65 ◽  
Author(s):  
R. K. Gill
Keyword(s):  
Vitamin D ◽  
Vitamin D Receptor ◽  
Steroid Receptor ◽  
Steroid Receptor Coactivator

scholarly journals Mapping the Domains of the Interaction of the Vitamin D Receptor and Steroid Receptor Coactivator-1

1998 ◽  
Vol 12 (1) ◽  
pp. 57-65 ◽  
Author(s):  
Rajbir K. Gill ◽  
Loretta M. Atkins ◽  
Bruce W. Hollis ◽  
Norman H. Bell
Keyword(s):  
Vitamin D ◽  
Mutation Analysis ◽  
Vitamin D Receptor ◽  
Deletion Mutant ◽  
Active Form ◽  
Steroid Receptor ◽  
Deletion Mutation ◽  
Biologically Active ◽  
Dependent Manner ◽  
Steroid Receptor Coactivator

Abstract The vitamin D receptor (VDR) binds to the vitamin D response element (VDRE) and mediates the effects of the biologically active form of vitamin D, 1,25-dihydroxyvitamin D3[ 1,25-(OH)2D3], on gene expression. The VDR binds to the VDRE as a heterodimeric complex with retinoid X receptor. In the present study, we have used a yeast two-hybrid system to clone complementary DNA that codes for VDR-interacting protein(s). We found that the human steroid receptor coactivator-1 (SRC-1) interacts with the VDR in a ligand-dependent manner, as demonstrated by β-galactosidase production. The interaction of the VDR and the SRC-1 takes place at physiological concentrations of 1,25(OH)2D3. A 48.2-fold stimulation of β-galactosidase activity was observed in the presence of 10−10m 1,25-(OH)2D3. In addition, a direct interaction between the ligand-activated glutathione-S-transferase-VDR and 35S-labeled SRC-1 was observed in vitro. Deletion-mutation analysis of the VDR established that the ligand-dependent activation domain (AF-2) of the VDR is required for the interaction with SRC-1. One deletion mutant, pGVDR-(1–418), bound the ligand but failed to interact with the SRC-1, whereas another deletion mutant, pGVDR-(1–423), bound the ligand and interacted with the SRC-1. We demonstrated that all the deletion mutants were expressed as analyzed by a Gal4 DNA-binding domain antibody. Deletion mutation analysis of the SRC-1 demonstrated that 27 amino acids (DPCNTNPTPMTKATPEEIKLEAQS-QFT) of the SRC-1 are essential for interaction with the AF-2 motif of the VDR.

Vitamin D receptor gene polymorphisms and steroid receptor status among Saudi women with breast cancer

Gene ◽  
2015 ◽  
Vol 558 (2) ◽  
pp. 215-219 ◽  
Author(s):  
Dalal M. Nemenqani ◽  
Rehab A. Karam ◽  
Mona G. Amer ◽  
Tamer M. Abd El Rahman
Keyword(s):  
Breast Cancer ◽  
Vitamin D ◽  
Vitamin D Receptor ◽  
Gene Polymorphisms ◽  
Receptor Gene ◽  
Steroid Receptor ◽  
Vitamin D Receptor Gene ◽  
Receptor Status ◽  
Saudi Women ◽  
Receptor Gene Polymorphisms

scholarly journals Calmodulin-Dependent Kinase IV Stimulates Vitamin D Receptor-Mediated Transcription

2005 ◽  
Vol 19 (9) ◽  
pp. 2309-2319 ◽  
Author(s):  
Tara I. Ellison ◽  
Diane R. Dowd ◽  
Paul N. MacDonald
Keyword(s):  
Gene Expression ◽  
Vitamin D ◽  
Reporter Gene ◽  
Vitamin D Receptor ◽  
Active Form ◽  
Metabolic Labeling ◽  
Dihydroxyvitamin D3 ◽  
Steroid Receptor Coactivator ◽  
Functional Consequences ◽  
Dependent Interaction

Abstract 1,25-Dihydroxyvitamin D3 [1,25-(OH)2D3] promotes intestinal absorption of calcium primarily by binding to the vitamin D receptor (VDR) and regulating gene expression. 1,25-(OH)2D3 also exerts rapid actions at the cell membrane that include increasing intracellular calcium levels and activating protein kinase cascades. To explore potential cross talk between calcium signaling elicited by the nongenomic actions of 1,25-(OH)2D3 and the genomic pathway mediated by VDR, we examined the effects of activated Ca2+/calmodulin-dependent kinases (CaMKs) on 1,25-(OH)2D3/VDR-mediated transcription. Expression of a constitutively active form of CaMKIV dramatically stimulated 1,25-(OH)2D3-activated reporter gene expression in COS-7, HeLa, and ROS17/2.8 cell lines. Metabolic labeling studies indicated that CaMKIV increased VDR phosphorylation levels. In addition, CaMKIV increased the independent transcription activity of the VDR coactivator SRC (steroid receptor coactivator) 1, and promoted ligand-dependent interaction between VDR and SRC coactivator proteins in mammalian two-hybrid studies. The functional consequences of this multifaceted mechanism of CaMKIV action were revealed by reporter gene studies, which showed that CaMKIV and select SRC coactivators synergistically enhanced VDR-mediated transcription. These studies support a model in which CaMKIV signaling stimulates VDR-mediated transcription by increasing phosphorylation levels of VDR and enhancing autonomous SRC activity, resulting in higher 1,25-(OH)2D3-dependent interaction between VDR and SRC coactivators.

Association of vitamin D receptor genotypes with early onset rheumatoid arthritis

2001 ◽  
Vol 28 (1) ◽  
pp. 89-93 ◽  
Author(s):  
J. R. Garcia-Lozano ◽  
M. F. Gonzalez-Escribano ◽  
A. Valenzuela ◽  
A. Garcia ◽  
A. Nunez-Roldan
Keyword(s):  
Rheumatoid Arthritis ◽  
Vitamin D ◽  
Vitamin D Receptor ◽  
Early Onset

803: Interactions Between Ultraviolet Radiation and Polymorphisms in the Vitamin D Receptor Gene Mediate Prostate Cancer Susceptibility

2006 ◽  
Vol 175 (4S) ◽  
pp. 260-260
Author(s):  
Nicholas J. Rukin ◽  
Samuel J. Moon ◽  
Dhaval Bodiwala ◽  
Christopher J. Luscombe ◽  
Mark F. Saxby ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Vitamin D ◽  
Ultraviolet Radiation ◽  
Vitamin D Receptor ◽  
Cancer Susceptibility ◽  
Receptor Gene ◽  
Vitamin D Receptor Gene ◽  
Prostate Cancer Susceptibility
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