Vitamin D receptor B1 and exon 1d: functional and evolutionary analysis
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.
|Authors||Gardiner, E. M.;Esteban, L. M.;Fong, C.;Allison, S. J.;Flanagan, J. L.;Kouzmenko, A. P.;Eisman, J. A. :|
|Publisher Name||JOURNAL OF STEROID BIOCHEMISTRY AND MOLECULAR BIOLOGY|
|Published Date||2004-01-01 00:00:00|
|URL link to publisher's version||http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15225777|
|OpenAccess link to author's accepted manuscript version||https://publications.gimr.garvan.org.au/open-access/1781|