Scientific background: |
VDR (Vitamin D Receptor), also known as Vitamin D Hormone Receptor, is a member of the nuclear receptor family of transcription factors. Labuda et al. (1991) assigned the VDR gene to 12q12-q14 by in situ hybridization. Using mutation analysis, Jurutka et al. (2000) characterized arg18/arg22, VDR residues immediately N-terminal of the first DNA-binding zinc finger, as vital for contact with the general transcription factor IIB (TFIIB). A natural polymorphic variant of VDR, termed F/M4 (missing a FokI restriction site), which lacks only the first 3 amino acids (including glu2), interacted more efficiently with TFIIB and also possessed elevated transcriptional activity compared with the full-length (f/M1) receptor. Shah et al. (2006) stated that the signaling and oncogenic activity of beta-catenin (CTNNB1) can be repressed by activation of VDR. Conversely, high levels of beta-catenin can potentiate the transcriptional activity of 1,25-dihydroxyvitamin D3. |
References: |
1. Jurutka, P. W., Remus, L. S., Whitfield, G. K., Thompson, P. D., Hsieh, J.-C., Zitzer, H., Tavakkoli, P., Galligan, M. A., Dang, H. T. L., Haussler, C. A., Haussler, M. R. The polymorphic N terminus in human vitamin D receptor isoforms influences transcriptional activity by modulating interaction with transcription factor IIB. Molec. Endocr. 14: 401-420, 2000.
2. Labuda, M., Ross, M. V., Fujiwara, T. M., Morgan, K., Ledbetter, D., Hughes, M. R., Glorieux, F. H. Two hereditary defects related to vitamin D metabolism map to the same region of human chromosome 12q.II(Abstract) Cytogenet. Cell Genet. 58: 1978, 1991.
3. Shah, S., Islam, M. N., Dakshanamurthy, S., Rizvi, I., Rao, M., Herrell, R., Zinser, G., Valrance, M., Aranda, A., Moras, D., Norman, A., Welsh, J., Byers, S. W. The molecular basis of vitamin D receptor and beta-catenin crossregulation. Molec. Cell 21: 799-809, 2006. Note: Erratum: Molec. Cell 21: 148 only, 2006.
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