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.
Gardiner
Edith M
EM
Bone and Mineral Research Program, Garvan Institute of Medical Research, 384 Victoria Street, Darlinghurst, Sydney, NSW 2010, Australia. e.gardiner@garvan.org.au
Esteban
Luis M
LM
Fong
Colette
C
Allison
Susan J
SJ
Flanagan
Judith L
JL
Kouzmenko
Alexander P
AP
Eisman
John A
JA
D000818:Animals; D001483:Base Sequence; D019556:COS Cells; D017931:DNA Primers; D005091:Exons; D006801:Humans; D008969:Molecular Sequence Data; D018167:Receptors, Calcitriol / Q000235:genetics / Q000502:physiology*; D012689:Sequence Homology, Nucleic Acid
D017931:DNA Primers; D018167:Receptors, Calcitriol