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

• Journal List
• Proc Natl Acad Sci U S A
• v.92(6); 1995 Mar 14
• PMC42430

Proc Natl Acad Sci U S A. 1995 Mar 14; 92(6): 2096–2100.

Center for Biotechnology, Karolinska Institute, NOVUM, Huddinge, Sweden.

Abstract

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.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (1.5M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.

Images in this article

Click on the image to see a larger version.

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

• Evans RM. The steroid and thyroid hormone receptor superfamily. Science. 1988 May 13;240(4854):889–895. [PMC free article] [PubMed] [Google Scholar]
• O'Malley B. The steroid receptor superfamily: more excitement predicted for the future. Mol Endocrinol. 1990 Mar;4(3):363–369. [PubMed] [Google Scholar]
• Umesono K, Murakami KK, Thompson CC, Evans RM. Direct repeats as selective response elements for the thyroid hormone, retinoic acid, and vitamin D3 receptors. Cell. 1991 Jun 28;65(7):1255–1266. [PMC free article] [PubMed] [Google Scholar]
• Yu VC, Delsert C, Andersen B, Holloway JM, Devary OV, När AM, Kim SY, Boutin JM, Glass CK, Rosenfeld MG. RXR beta: a coregulator that enhances binding of retinoic acid, thyroid hormone, and vitamin D receptors to their cognate response elements. Cell. 1991 Dec 20;67(6):1251–1266. [PubMed] [Google Scholar]
• Bugge TH, Pohl J, Lonnoy O, Stunnenberg HG. RXR alpha, a promiscuous partner of retinoic acid and thyroid hormone receptors. EMBO J. 1992 Apr;11(4):1409–1418. [PMC free article] [PubMed] [Google Scholar]
• Heyman RA, Mangelsdorf DJ, Dyck JA, Stein RB, Eichele G, Evans RM, Thaller C. 9-cis retinoic acid is a high affinity ligand for the retinoid X receptor. Cell. 1992 Jan 24;68(2):397–406. [PubMed] [Google Scholar]
• Levin AA, Sturzenbecker LJ, Kazmer S, Bosakowski T, Huselton C, Allenby G, Speck J, Kratzeisen C, Rosenberger M, Lovey A, et al. 9-cis retinoic acid stereoisomer binds and activates the nuclear receptor RXR alpha. Nature. 1992 Jan 23;355(6358):359–361. [PubMed] [Google Scholar]
• Mader S, Leroy P, Chen JY, Chambon P. Multiple parameters control the selectivity of nuclear receptors for their response elements. Selectivity and promiscuity in response element recognition by retinoic acid receptors and retinoid X receptors. J Biol Chem. 1993 Jan 5;268(1):591–600. [PubMed] [Google Scholar]
• Göttlicher M, Widmark E, Li Q, Gustafsson JA. Fatty acids activate a chimera of the clofibric acid-activated receptor and the glucocorticoid receptor. Proc Natl Acad Sci U S A. 1992 May 15;89(10):4653–4657. [PMC free article] [PubMed] [Google Scholar]
• Dagerlind A, Friberg K, Bean AJ, Hökfelt T. Sensitive mRNA detection using unfixed tissue: combined radioactive and non-radioactive in situ hybridization histochemistry. Histochemistry. 1992 Aug;98(1):39–49. [PubMed] [Google Scholar]
• Andersson S, Davis DL, Dahlbäck H, Jörnvall H, Russell DW. Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme. J Biol Chem. 1989 May 15;264(14):8222–8229. [PubMed] [Google Scholar]
• Berger J, Hauber J, Hauber R, Geiger R, Cullen BR. Secreted placental alkaline phosphatase: a powerful new quantitative indicator of gene expression in eukaryotic cells. Gene. 1988 Jun 15;66(1):1–10. [PubMed] [Google Scholar]
• Gearing KL, Göttlicher M, Teboul M, Widmark E, Gustafsson JA. Interaction of the peroxisome-proliferator-activated receptor and retinoid X receptor. Proc Natl Acad Sci U S A. 1993 Feb 15;90(4):1440–1444. [PMC free article] [PubMed] [Google Scholar]
• Rogers S, Wells R, Rechsteiner M. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science. 1986 Oct 17;234(4774):364–368. [PubMed] [Google Scholar]
• Davis IJ, Hazel TG, Lau LF. Transcriptional activation by Nur77, a growth factor-inducible member of the steroid hormone receptor superfamily. Mol Endocrinol. 1991 Jun;5(6):854–859. [PubMed] [Google Scholar]
• Hazel TG, Nathans D, Lau LF. A gene inducible by serum growth factors encodes a member of the steroid and thyroid hormone receptor superfamily. Proc Natl Acad Sci U S A. 1988 Nov;85(22):8444–8448. [PMC free article] [PubMed] [Google Scholar]
• Nakai A, Kartha S, Sakurai A, Toback FG, DeGroot LJ. A human early response gene homologous to murine nur77 and rat NGFI-B, and related to the nuclear receptor superfamily. Mol Endocrinol. 1990 Oct;4(10):1438–1443. [PubMed] [Google Scholar]
• Forman BM, Samuels HH. Interactions among a subfamily of nuclear hormone receptors: the regulatory zipper model. Mol Endocrinol. 1990 Sep;4(9):1293–1301. [PubMed] [Google Scholar]
• Chang C, Kokontis J. Identification of a new member of the steroid receptor super-family by cloning and sequence analysis. Biochem Biophys Res Commun. 1988 Sep 15;155(2):971–977. [PubMed] [Google Scholar]
• Zhang XK, Lehmann J, Hoffmann B, Dawson MI, Cameron J, Graupner G, Hermann T, Tran P, Pfahl M. Homodimer formation of retinoid X receptor induced by 9-cis retinoic acid. Nature. 1992 Aug 13;358(6387):587–591. [PubMed] [Google Scholar]
• Hallenbeck PL, Phyillaier M, Nikodem VM. Divergent effects of 9-cis-retinoic acid receptor on positive and negative thyroid hormone receptor-dependent gene expression. J Biol Chem. 1993 Feb 25;268(6):3825–3828. [PubMed] [Google Scholar]
• Barettino D, Bugge TH, Bartunek P, Vivanco Ruiz MD, Sonntag-Buck V, Beug H, Zenke M, Stunnenberg HG. Unliganded T3R, but not its oncogenic variant, v-erbA, suppresses RAR-dependent transactivation by titrating out RXR. EMBO J. 1993 Apr;12(4):1343–1354. [PMC free article] [PubMed] [Google Scholar]
• Cooney AJ, Tsai SY, O'Malley BW, Tsai MJ. Chicken ovalbumin upstream promoter transcription factor (COUP-TF) dimers bind to different GGTCA response elements, allowing COUP-TF to repress hormonal induction of the vitamin D3, thyroid hormone, and retinoic acid receptors. Mol Cell Biol. 1992 Sep;12(9):4153–4163. [PMC free article] [PubMed] [Google Scholar]
• Lydon JP, Power RF, Conneely OM. Differential modes of activation define orphan subclasses within the steroid/thyroid receptor superfamily. Gene Expr. 1992;2(3):273–283. [PMC free article] [PubMed] [Google Scholar]
• Denner LA, Weigel NL, Maxwell BL, Schrader WT, O'Malley BW. Regulation of progesterone receptor-mediated transcription by phosphorylation. Science. 1990 Dec 21;250(4988):1740–1743. [PubMed] [Google Scholar]
• Singh VB, Moudgil VK. Phosphorylation of rat liver glucocorticoid receptor. J Biol Chem. 1985 Mar 25;260(6):3684–3690. [PubMed] [Google Scholar]
• Goldberg Y, Glineur C, Gesquière JC, Ricouart A, Sap J, Vennström B, Ghysdael J. Activation of protein kinase C or cAMP-dependent protein kinase increases phosphorylation of the c-erbA-encoded thyroid hormone receptor and of the v-erbA-encoded protein. EMBO J. 1988 Aug;7(8):2425–2433. [PMC free article] [PubMed] [Google Scholar]
• Hsieh JC, Jurutka PW, Galligan MA, Terpening CM, Haussler CA, Samuels DS, Shimizu Y, Shimizu N, Haussler MR. Human vitamin D receptor is selectively phosphorylated by protein kinase C on serine 51, a residue crucial to its trans-activation function. Proc Natl Acad Sci U S A. 1991 Oct 15;88(20):9315–9319. [PMC free article] [PubMed] [Google Scholar]
• Lin KH, Ashizawa K, Cheng SY. Phosphorylation stimulates the transcriptional activity of the human beta 1 thyroid hormone nuclear receptor. Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7737–7741. [PMC free article] [PubMed] [Google Scholar]
• Power RF, Lydon JP, Conneely OM, O'Malley BW. Dopamine activation of an orphan of the steroid receptor superfamily. Science. 1991 Jun 14;252(5012):1546–1548. [PubMed] [Google Scholar]
• Power RF, Mani SK, Codina J, Conneely OM, O'Malley BW. Dopaminergic and ligand-independent activation of steroid hormone receptors. Science. 1991 Dec 13;254(5038):1636–1639. [PubMed] [Google Scholar]
• Yang Y, Vacchio MS, Ashwell JD. 9-cis-retinoic acid inhibits activation-driven T-cell apoptosis: implications for retinoid X receptor involvement in thymocyte development. Proc Natl Acad Sci U S A. 1993 Jul 1;90(13):6170–6174. [PMC free article] [PubMed] [Google Scholar]
• Shinar DM, Endo N, Rutledge SJ, Vogel R, Rodan GA, Schmidt A. NER, a new member of the gene family encoding the human steroid hormone nuclear receptor. Gene. 1994 Sep 30;147(2):273–276. [PubMed] [Google Scholar]
• Song C, Kokontis JM, Hiipakka RA, Liao S. Ubiquitous receptor: a receptor that modulates gene activation by retinoic acid and thyroid hormone receptors. Proc Natl Acad Sci U S A. 1994 Nov 8;91(23):10809–10813. [PMC free article] [PubMed] [Google Scholar]
• Apfel R, Benbrook D, Lernhardt E, Ortiz MA, Salbert G, Pfahl M. A novel orphan receptor specific for a subset of thyroid hormone-responsive elements and its interaction with the retinoid/thyroid hormone receptor subfamily. Mol Cell Biol. 1994 Oct;14(10):7025–7035. [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences