Conserved amino acids in the ligand-binding and τ(i) domains of the peroxisome proliferator-activated receptor α are necessary for heterodimerization with RXR

Molecular and Cellular Endocrinology

Volumn 147, Issue 1-2, 1999, Pages 37-47

  Gorla Bajszczak, Agnieszka ^a   Juge Aubry, Cristiana ^a   Pernin, Agnès ^a   Burger, Albert G ^a   Meier, Christoph A ^a  

^a GENEVA UNIVERSITY HOSPITALS   (Switzerland)

Author keywords

Peroxisome proliferator activated receptor; Retinoid X receptor; Transcription

Indexed keywords

AMINO ACID; ARGININE; CELL NUCLEUS RECEPTOR; LEUCINE; LEUCINE ZIPPER PROTEIN; LIGAND; MUTANT PROTEIN; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR; RETINOID X RECEPTOR;

ADIPOCYTE; ARTICLE; CELL DIFFERENTIATION; CONTROLLED STUDY; HUMAN; HUMAN CELL; INFLAMMATION; LIGAND BINDING; LIPID METABOLISM; PEROXISOME; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; SITE DIRECTED MUTAGENESIS;

ACYL-COA OXIDASE; ALKANE 1-MONOOXYGENASE; AMINO ACID SEQUENCE; ASPARTIC ACID; CONSERVED SEQUENCE; CYTOCHROME P-450 ENZYME SYSTEM; DIMERIZATION; DNA; DNA-BINDING PROTEINS; LEUCINE; LEUCINE ZIPPERS; LIGANDS; MIXED FUNCTION OXYGENASES; MOLECULAR SEQUENCE DATA; MUTATION; OXIDOREDUCTASES; PROMOTER REGIONS (GENETICS); PROTEIN BINDING; PYRIMIDINES; RECEPTORS, CYTOPLASMIC AND NUCLEAR; RECEPTORS, RETINOIC ACID; RESPONSE ELEMENTS; RETINOID X RECEPTORS; TRANS-ACTIVATORS; TRANSCRIPTION FACTORS;

EID: 0033601842     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0303-7207(98)00217-2     Document Type: Article

References (33)

1. Au-Fliegner M., Helmer E., Casanova J., Raaka B. M., Samuels H. H. The conserved ninth C-terminal heptad in thyroid hormone and retinoic acid receptors mediates diverse responses by affecting heterodimer but not homodimer formation. Mol. Cell. Biol. 13:1993;5725-5737.
2. Bardot O., Aldridge T. C., Latruffe N., Green S. PPAR-RXR Heterodimer activates a peroxisome proliferator response element upstream of the bifunctional enzyme gene. Biochem. Biophys. Res. Commun. 192:1993;37-45.
3. Bocos C., Gottlicher M., Gearing K., Banner C., Enmark E., Teboul M., Crickmore A., Gustafsson J. A. Fatty acid activation of peroxisome proliferator-activated receptor (PPAR). J. Steroid Biochem. Mol. Biol. 53:1995;467-473.
4. Bourguet W., Ruff M., Chambon P., Gronemeyer H., Moras D. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha. Nature. 375:1995;377-382.
5. Braissant O., Foufelle F., Scotto C., Dauca M., Wahli W. Differential expression of peroxisome proliferator- activated receptors (PPARs): Tissue distribution of PPAR- alpha, -beta, and -gamma in the adult rat. Endocrinology. 137:1996;354-366.
6. Brun R. P., Tontonoz P., Forman B. M., Ellis R., Chen J., Evans R. M., Spiegelman B. M. Differential activation of adipogenesis by multiple PPAR isoforms. Genes Develop. 10:1996;974-984.
7. Desvergne, B., Wahli W., 1995. PPAR: a key nuclear factor in nutrient/gene interactions. In: Baeurle P.A. (Ed.), Inducible gene expression. Birkhäuser, Boston, pp. 142-176.
8. Devchand P.R., Keller H., Peters J.M., Vazquez M., Gonzalez F.J., Wahli W. The PPAR alpha-leukotriene B-4 pathway to inflammation control. Nature. 384:1996;39-43.
9. Dowell P., Peterson V.J., Zabriskie T.M., Leid M. Ligand-induced peroxisome proliferator-activated receptor alpha conformational change. J. Biol. Chem. 272:1997;2013-2020.
10. Forman B.M., Tontonoz P., Chen J., Brun R.P., Spiegelman B.M., Evans R.M. 15-Deoxy-delta 12, 14-prostaglandin J2 is a ligand for the adipocyte determination factor PPAR gamma. Cell. 83:1995;803-812.
11. Forman B.M., Chen J., Evans R.M. Hypolipidemic drugs, polyunsaturated fatty acids, and eicosanoids are ligands for peroxisome proliferator-activated receptors alpha and delta. Proc. Natl. Acad. Sci. U.S.A. 94:1997;4312-4317.
12. Green S., Wahli W. Peroxisome proliferator-activated receptors: finding the orphan a home. Mol. Cell. Endocrinol. 100:1994;149-153.
13. Juge-Aubry C., Pernin A., Faves T., Burger A.G., Wahli W., Meier C.A., Desvergne B. DNA binding properties of peroxisome proliferator-activated receptor subtypes on various natural peroxisome proliferator response elements. J. Biol. Chem. 272:1997;25252-25259.
14. Juge-Aubry C.E., Gorla-Bajszczak A., Pernin A., Lemberger T., Wahli W., Burger A.G., Meier C.A. Peroxisome proliferator-activated receptor mediates cross-talk with thyroid hormone receptor by competition for retinoid X receptor. Possible role of a leucine zipper-like heptad repeat. J Biol. Chem. 270:1995;18117-18122.
15. Keller H., Dreyer C., Medin J., Mahfoudi A., Ozato K., Wahli W. Fatty acids and retinoids control lipid metabolism through activation of peroxisome proliferator-activated receptor-retinoid X receptor heterodimers. Proc. Natl. Acad. Sci. U.S.A. 90:1993a;2160-2164.
16. Keller H., Wahli W. Peroxisome proliferator-activated receptors-A link between endocrinology and nutrition. Trends Endocrinol. Metab. 4:1993b;291-296.
17. Kliewer S.A., Lenhard J.M., Willson T.M., Patel I., Morris D.C., Lehmann J.M. A prostaglandin J2 metabolite binds peroxisome proliferator-activated receptor gamma and promotes adipocyte differentiation. Cell. 83:1995;813-819.
18. Kliewer S.A., Sundseth S.S., Jones S.A., Brown P.J., Wisley G.B., Koble C.S., Devchand P., Wahli W., Willson T.M., Lenhard J.M., Lehmann J.M. Fatty acids and eicosanoids regulate gene expression through direct interactions with peroxisome proliferator-activated receptors α and γ Proc. Natl. Acad. Sci. USA. 94:1997;4318-4323.
19. Krey G., Braissant O., L'Horset F., Kalkhoven E., Perroud M., Parker M.G., Wahli W. Fatty acids, eciosanoids, and hypolipidemic agents identified as ligands of peroxisome proliferator-activated receptors by coactivator-dependent receptor ligand assay. Mol. Endocrinol. 11:1997;779-791.
20. Lehmann J.M., Moore L.B., Smitholiver T.A., Wilkison W.O., Willson T.M., Kliewer S.A. An antidiabetic thiazolidinedione is a high affinity ligand for peroxisome proliferator-activated receptor gamma (PPAR gamma). J. Biol. Chem. 270:1995;12953-12956.
21. Lemberger T., Desvergne B., Wahli W. Peroxisome proliferator-activated receptors: A nuclear receptor signaling pathway in lipid physiology. Annu. Rev. Cell. Dev. Biol. 12:1996;335.
22. Long S.D., Pekala P.H. Regulation of GLUT4 gene expression by arachidonic acid. Evidence for multiple pathways, one of which requires oxidation to prostaglandin E2. J. Biol. Chem. 271:1996;1138-1144.
23. Meier-Heusler S.C., Zhu X., Juge-Aubry C., Pernin A., Burger A.G., Cheng S.Y., Meier C.A. Modulation of thyroid hormone action by mutant thyroid hormone receptors; c-erbAα2 and peroxisome proliferator-activated receptor: evidence for different mechanisms of inhibition. Mol. Cell. Endocrinol. 107:1995;55-66.
24. Nagaya T., Jameson J.L. Thyroid hormone receptor dimerization is required for dominant negative inhibition by mutations that cause thyroid hormone resistance. J. Biol. Chem. 268:1993;15766-15771.
25. O'Donnell A.L., Koenig R.J. Mutational analysis identifies a new functional domain of the thyroid hormone receptor. Mol. Endocrinol. 4:1990;715-720.
26. O'Donnell A.L., Rosen E.D., Darling D.S., Koenig R.J. Thyroid hormone receptor mutations that interfere with transcriptional activation also interfere with receptor interaction with a nuclear protein. Mol. Endocrinol. 5:1991;94-99.
27. Palmer C.N., Hsu M.H., Griffin H.J., Johnson E.F. Novel sequence determinants in peroxisome proliferator signaling. J. Biol. Chem. 270:1995;16114-16121.
28. Renaud J.P., Rochel N., Ruff M., Vivat V., Chambon P., Gronemeyer H., Moras D. Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid. Nature. 378:1995;681-689.
29. Shalev A., Meier C.A. Peroxisome proliferator-activated receptors: A nuclear hormone receptor involved in adipocyte differentiation and lipid homeostasis. Eur. J. Endocrinology. 134:1996;541-542.
30. Sher T., Yi H.F., McBride O.W., Gonzalez F.J. cDNA cloning, chromosomal mapping, and functional characterization of the human peroxisome proliferator activated receptor. Biochemistry. 32:1993;5598-5604.
31. Wagner R.L., Apriletti J.W., Mcgrath M.E., West B.L., Baxter J.D., Fletterick R.J. A structural role for hormone in the thyroid hormone receptor. Nature. 378:1995;690-697.
32. Wurtz J.M., Bourguet W., Renaud J.P., Vivat V., Chambon P., Moras D., Gronemeyer H. A canonical structure for the ligand-binding domain of nuclear receptors. Nat. Struct. Biol. 3:1996;206.
33. Zhang X.K., Salbert G., Lee M.O., Pfahl M. Mutations that alter ligand-induced switches and dimerization activities in the retinoid X receptor. Mol. Cell. Biol. 14:1994;4311-4323.