OR-1, a member of the nuclear receptor superfamily that interacts with the 9-cis-retinoic acid receptor.

M Teboul, E Enmark, Q Li… - Proceedings of the …, 1995 - National Acad Sciences
M Teboul, E Enmark, Q Li, AC Wikström, M Pelto-Huikko, JA Gustafsson
Proceedings of the National Academy of Sciences, 1995National Acad Sciences
We have cloned a member of the nuclear receptor superfamily. The cDNA was isolated from
a rat liver library and encodes a protein of 446 aa with a predicted mass of 50 kDa. This
clone (OR-1) shows no striking homology to any known member of the steroid/thyroid
hormone receptor superfamily. The most related receptor is the ecdysone receptor and the
highest homologies represent< 10% in the amino-terminal domain, between 15-37% in the
carboxyl-terminal domain and 50-62% in the DNA binding domain. The expression of OR-1 …
We have cloned a member of the nuclear receptor superfamily. The cDNA was isolated from a rat liver library and encodes a protein of 446 aa with a predicted mass of 50 kDa. This clone (OR-1) shows no striking homology to any known member of the steroid/thyroid hormone receptor superfamily. The most related receptor is the ecdysone receptor and the highest homologies represent < 10% in the amino-terminal domain, between 15-37% in the carboxyl-terminal domain and 50-62% in the DNA binding domain. The expression of OR-1 appears to be widespread in both fetal and adult rat tissues. Potential DNA response elements composed of a direct repeat of the hexameric motif AGGTCA spaced by 0-6 nt were tested in gel shift experiments. OR-1 was shown to interact with the 9-cis-retinoic acid receptor (retinoid X receptor, RXR) and the OR-1/RXR complex to bind to a direct repeat spaced by 4 nt (DR4). In transfection experiments, OR-1 appears to activate RXR-mediated function through the DR4. Therefore OR-1 might modulate 9-cis-retinoic acid signaling by interacting with RXR.
National Acad Sciences