Phosphorylation at serine 208 of the 1α,25-dihydroxy Vitamin D3 receptor modulates the interaction with transcriptional coactivators
✍ Scribed by Gloria Arriagada; Roberto Paredes; Juan Olate; Andre van Wijnen; Jane B. Lian; Gary S. Stein; Janet L. Stein; Sergio Onate; Martin Montecino
- Book ID
- 116697925
- Publisher
- Elsevier Science
- Year
- 2007
- Tongue
- English
- Weight
- 388 KB
- Volume
- 103
- Category
- Article
- ISSN
- 0960-0760
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract Binding of 1α,25‐dihydroxy vitamin D~3~ to the C‐terminal ligand‐binding domain (LBD) of its receptor (VDR) induces a conformational change that enables interaction of VDR with transcriptional coactivators such as members of the p160/SRC family or the DRIP (vitamin D receptor‐interactin
## Abstract The Runx2 transcription factor is a key regulator of osteoblast differentiation. In response to 1α,25 dihydroxy vitamin D3, Runx2 may interact with the 1α,25 dihydroxy vitamin D3 receptor (VDR) in the promoter of target genes, producing a synergic activation of their transcription. Prev