Vitamin D receptor B1 and exon 1d: functional and evolutionary analysis

The Journal of Steroid Biochemistry and Molecular Biology
Edith M GardinerJ A Eisman

Abstract

The vitamin D receptor (VDR) shares a conserved structural and functional organization with other nuclear receptor (NR) superfamily members. For many NRs, N-terminal variant isoforms that display distinct cell-, stage- and promoter-specific actions have been identified. The novel VDR isoform VDRB1, with a 50 amino acid N-terminal extension, is produced from low abundance transcripts that contain exon 1d of the human VDR locus. There is evidence for the conservation of this exon in other mammalian and avian species. The transactivation differences between VDRB1 and the original VDR, clarified here, provide insights into mechanisms that may contribute to functional differences and potentially distinct physiological roles for these two VDR isoforms.

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Citations

May 17, 2012·Pharmacogenetics and Genomics·Audrey H PoonTeri E Klein
Feb 10, 2007·The Journal of Steroid Biochemistry and Molecular Biology·Frédéric JehanMichèle Garabédian
Jul 5, 2005·Biochemical and Biophysical Research Communications·Luis M EstebanEdith M Gardiner
Jul 28, 2005·The Journal of Steroid Biochemistry and Molecular Biology·George P StudzinskiJonathan S Harrison
May 1, 2010·Cancer Biology & Therapy·Radharani MarikChristopher B Umbricht
Jun 14, 2005·American Journal of Physiology. Renal Physiology·Adriana S DussoEduardo Slatopolsky
Jul 23, 2014·Expert Review of Gastroenterology & Hepatology·Simon Ghaly, Ian Lawrance

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