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Volumn 162, Issue 1-2, 2000, Pages 57-67

A PPARγ mutant serves as a dominant negative inhibitor of PPAR signaling and is localized in the nucleus

Author keywords

Antidiabetic agents; Dominant negative mutant; Nuclear receptors; Peroxisome proliferator activated receptors; Thiazolidinediones

Indexed keywords

ANTIDIABETIC AGENT; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR; RETINOID X RECEPTOR; CELL RECEPTOR; COMPLEMENTARY DNA; LIGAND; RETINOIC ACID RECEPTOR; TRANSCRIPTION FACTOR;

EID: 0034712589     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0303-7207(00)00211-2     Document Type: Article
Times cited : (34)

References (47)
  • 1
    • 0026726806 scopus 로고
    • Hormone and antihormone induce distinct conformational changes which are central to steroid receptor activation
    • Allan G.F., Xiaohua L., Tsai S.Y., Weigel N.L., Edwards D.P., Tsai M.-J., O'Malley B.W. Hormone and antihormone induce distinct conformational changes which are central to steroid receptor activation. J. Biol. Chem. 267:1992;19513-19520.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19513-19520
    • Allan, G.F.1    Xiaohua, L.2    Tsai, S.Y.3    Weigel, N.L.4    Edwards, D.P.5    Tsai, M.-J.6    O'Malley, B.W.7
  • 2
    • 0028233763 scopus 로고
    • Characterization of the ligand-dependent transactivation domain of thyroid hormone receptor
    • Barettino D., Ruiz M.V., Stunnenberg H.G. Characterization of the ligand-dependent transactivation domain of thyroid hormone receptor. EMBO J. 13:1994;3009-3049.
    • (1994) EMBO J. , vol.13 , pp. 3009-3049
    • Barettino, D.1    Ruiz, M.V.2    Stunnenberg, H.G.3
  • 3
    • 0029745382 scopus 로고    scopus 로고
    • Thiazolidinediones produce a conformational change in peroxisomal proliferator-activated receptor-γ: Binding and activation correlate with antidiabetic actions in db/db mice
    • Berger J., Bailey P., Biswas C., Cullinan C.A., Doebber T.W., Hayes N.S., Saperstein R., Smith R.G., Leibowitz M.D. Thiazolidinediones produce a conformational change in peroxisomal proliferator-activated receptor-γ: binding and activation correlate with antidiabetic actions in db/db mice. Endocrinology. 137:1996;4189-4195.
    • (1996) Endocrinology , vol.137 , pp. 4189-4195
    • Berger, J.1    Bailey, P.2    Biswas, C.3    Cullinan, C.A.4    Doebber, T.W.5    Hayes, N.S.6    Saperstein, R.7    Smith, R.G.8    Leibowitz, M.D.9
  • 5
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α
    • Bourguet W., Ruff M., Chambon P., Gronemeyer H., Moras D. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α Nature. 375:1995;377-382.
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, P.3    Gronemeyer, H.4    Moras, D.5
  • 6
    • 0030047806 scopus 로고
    • Differential expression of peroxisome proliferator-activated receptors: Tissue distribution of PPARα, β and γ in the adult rat
    • Braissant O., Foufelle F., Scotto C., Dauca M., Wahli W. Differential expression of peroxisome proliferator-activated receptors: tissue distribution of PPARα, β and γ in the adult rat. Endocrinology. 137:1995;354-366.
    • (1995) Endocrinology , vol.137 , pp. 354-366
    • Braissant, O.1    Foufelle, F.2    Scotto, C.3    Dauca, M.4    Wahli, W.5
  • 8
    • 0030747895 scopus 로고    scopus 로고
    • Tissue distribution and quantification of the expression of mRNAs of peroxisome proliferator-activated receptors and liver×receptor-α In humans
    • Didier A., Rieusset J., Fajas L., Vallier P., Frering V., Riou J.P., Staels B., Auwerx J., LaVille M., Vidal H. Tissue distribution and quantification of the expression of mRNAs of peroxisome proliferator-activated receptors and liver×receptor-α in humans. Diabetes. 46:1997;1319-1327.
    • (1997) Diabetes , vol.46 , pp. 1319-1327
    • Didier, A.1    Rieusset, J.2    Fajas, L.3    Vallier, P.4    Frering, V.5    Riou, J.P.6    Staels, B.7    Auwerx, J.8    Laville, M.9    Vidal, H.10
  • 9
    • 0031030718 scopus 로고    scopus 로고
    • Ligand-induced peroxisome proliferator-activated receptor α conformational change
    • Dowell P., Peterson V.J., Zabriskie T.M., Leid M. Ligand-induced peroxisome proliferator-activated receptor α conformational change. J. Biol. Chem. 272:1997;2013-2020.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2013-2020
    • Dowell, P.1    Peterson, V.J.2    Zabriskie, T.M.3    Leid, M.4
  • 10
    • 0027278522 scopus 로고
    • Positive regulation of peroxisomal β-oxidation pathway by fatty acids through activation of peroxisome proliferator-activated receptors (PPAR)
    • Dreyer C., Keller H., Mahfoudi A., Laudet V., Krey G., Wahli W. Positive regulation of peroxisomal β-oxidation pathway by fatty acids through activation of peroxisome proliferator-activated receptors (PPAR). Biol. Cell. 77:1993;67-77.
    • (1993) Biol. Cell. , vol.77 , pp. 67-77
    • Dreyer, C.1    Keller, H.2    Mahfoudi, A.3    Laudet, V.4    Krey, G.5    Wahli, W.6
  • 11
    • 0027941792 scopus 로고
    • Activation function of retinoic acid receptor and 9-cis-retinoic acid receptor: Presence of a conserved autonomous constitutive activating domain and of the nature of the response element
    • Durand B., Saunders M., Gaundon C., Roy B., Losson R., Chambon P. Activation function of retinoic acid receptor and 9-cis-retinoic acid receptor: presence of a conserved autonomous constitutive activating domain and of the nature of the response element. EMBO J. 13:1994;5370-5382.
    • (1994) EMBO J. , vol.13 , pp. 5370-5382
    • Durand, B.1    Saunders, M.2    Gaundon, C.3    Roy, B.4    Losson, R.5    Chambon, P.6
  • 13
    • 0028909362 scopus 로고
    • Cloning of a protein that mediates transcriptional effects of fatty acids in preadipocytes
    • Ez-Zoubir A., Bonino F., Ailhaud G., Abumrad N.A., Grimaldi P.A. Cloning of a protein that mediates transcriptional effects of fatty acids in preadipocytes. J. Biol. Chem. 270:1995;2367-2371.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2367-2371
    • Ez-Zoubir, A.1    Bonino, F.2    Ailhaud, G.3    Abumrad, N.A.4    Grimaldi, P.A.5
  • 14
    • 0028972025 scopus 로고
    • 15-Deoxy-Δ12,14 prostaglandin J2 is a ligand for the adipocyte determination factor PPARγ
    • Forman B.M., Tontonoz P., Chen J., Brun R.P., Spiegelman B.M., Evans R.M. 15-Deoxy-Δ12,14 prostaglandin J2 is a ligand for the adipocyte determination factor PPARγ Cell. 83:1995;803-812.
    • (1995) Cell , vol.83 , pp. 803-812
    • Forman, B.M.1    Tontonoz, P.2    Chen, J.3    Brun, R.P.4    Spiegelman, B.M.5    Evans, R.M.6
  • 15
    • 0026551309 scopus 로고
    • Fatty acids activate the clofibric acid activated receptor and the glucocorticoid receptor
    • Gottlicher M., Widmark E., Li Q., Gustafsson J.A. Fatty acids activate the clofibric acid activated receptor and the glucocorticoid receptor. Proc. Natl. Acad. Sci. U.S.A. 89:1992;4653-4657.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 4653-4657
    • Gottlicher, M.1    Widmark, E.2    Li, Q.3    Gustafsson, J.A.4
  • 16
    • 0029152375 scopus 로고
    • Isolation of the human peroxisome proliferator activated receptor gamma cDNA: Expression in hemapoietic cells and chrosomal mapping
    • Greene M.E., Blumberg B., McBride O.W., Yi H.F., Kronquist K., Kwan K., Hsieh L., Greene G., Nimer S.D. Isolation of the human peroxisome proliferator activated receptor gamma cDNA: expression in hemapoietic cells and chrosomal mapping. Gene Exp. 4:1995;281-299.
    • (1995) Gene Exp. , vol.4 , pp. 281-299
    • Greene, M.E.1    Blumberg, B.2    McBride, O.W.3    Yi, H.F.4    Kronquist, K.5    Kwan, K.6    Hsieh, L.7    Greene, G.8    Nimer, S.D.9
  • 17
    • 0027525576 scopus 로고
    • The peroxisome proliferator activated receptor: Retinoid×receptor heterodimer is activated by fatty acid and fibrate hypolipidaemic drugs
    • Issemann I., Prince R.A., Tugwood J.D., Green S. The peroxisome proliferator activated receptor: retinoid×receptor heterodimer is activated by fatty acid and fibrate hypolipidaemic drugs. J. Mol. Endocrinol. 11:1993;37-47.
    • (1993) J. Mol. Endocrinol. , vol.11 , pp. 37-47
    • Issemann, I.1    Prince, R.A.2    Tugwood, J.D.3    Green, S.4
  • 18
    • 0028966102 scopus 로고
    • The human peroxisome proliferator-activated receptor (PPAR) subtype NUC1 represses the activation of hPPARα and thyroid receptor receptors
    • Jow L., Mukherjee R. The human peroxisome proliferator-activated receptor (PPAR) subtype NUC1 represses the activation of hPPARα and thyroid receptor receptors. J. Biol. Chem. 270:1995;3836-3840.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3836-3840
    • Jow, L.1    Mukherjee, R.2
  • 20
    • 0027139820 scopus 로고
    • Peroxisome proliferator-activated receptors
    • Keller H., Wahli W. Peroxisome proliferator-activated receptors. Trends Endocrinol. Metab. 4:1993;291-296.
    • (1993) Trends Endocrinol. Metab. , vol.4 , pp. 291-296
    • Keller, H.1    Wahli, W.2
  • 21
    • 0027447461 scopus 로고
    • Fatty acids and retinoids control lipid metabolism through activation of peroxisome proliferator-activated receptors-retinoid×receptor heterodimers
    • 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 receptors-retinoid×receptor heterodimers. Proc. Natl. Acad. Sci. U.S.A. 90:1993;2160-2164.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 2160-2164
    • Keller, H.1    Dreyer, C.2    Medin, J.3    Mahfoudi, A.4    Ozato, K.5    Wahli, W.6
  • 22
    • 0026705751 scopus 로고
    • Convergence of 9-cis-retinoic acid and peroxisome proliferator signaling pathways through heterodimer formation of their receptors
    • Kliewer S.A., Umesono K., Noonan D.J., Heyman R.A., Evans R.M. Convergence of 9-cis-retinoic acid and peroxisome proliferator signaling pathways through heterodimer formation of their receptors. Nature. 358:1992;771-774.
    • (1992) Nature , vol.358 , pp. 771-774
    • Kliewer, S.A.1    Umesono, K.2    Noonan, D.J.3    Heyman, R.A.4    Evans, R.M.5
  • 24
    • 0028972026 scopus 로고
    • A prostaglandin J2 metabolite binds peroxisome proliferator-activated receptor γ and promotes adipocyte differentiation
    • Kliewer S.A., Lenhard J.M., Willson T.M., Patel I., Morris D.C., Lehman J.M. A prostaglandin J2 metabolite binds peroxisome proliferator-activated receptor γ and promotes adipocyte differentiation. Cell. 83:1995;813-819.
    • (1995) Cell , vol.83 , pp. 813-819
    • Kliewer, S.A.1    Lenhard, J.M.2    Willson, T.M.3    Patel, I.4    Morris, D.C.5    Lehman, J.M.6
  • 25
    • 0029016829 scopus 로고
    • An antidiabetic thiazolidinedione is a high affinity ligand for peroxisomal proliferator-activated receptor γ
    • Lehmann J.M., Moore L.B., Smith-Oliver T.A., Wilkison W.O., Willson T.M., Kliewer S.A. An antidiabetic thiazolidinedione is a high affinity ligand for peroxisomal proliferator-activated receptor γ J. Biol. Chem. 270:1995;12953-12956.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12953-12956
    • Lehmann, J.M.1    Moore, L.B.2    Smith-Oliver, T.A.3    Wilkison, W.O.4    Willson, T.M.5    Kliewer, S.A.6
  • 27
    • 0030771215 scopus 로고    scopus 로고
    • Evidence for ligand-dependent intramolecular folding of the AF-2 domain in vitamin D receptor-activated transcription and coactivator interaction
    • Masuyama H., Brownfield C.M., St-Arnaud R., MacDonald P.N. Evidence for ligand-dependent intramolecular folding of the AF-2 domain in vitamin D receptor-activated transcription and coactivator interaction. Mol. Endocrinol. 11:1997;1507-1517.
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1507-1517
    • Masuyama, H.1    Brownfield, C.M.2    St-Arnaud, R.3    MacDonald, P.N.4
  • 28
    • 0028031681 scopus 로고
    • Dominant negative retinoid×receptor β inhibits retinoic acid-responsive gene regulation in embryonal carcinoma cells
    • Minucci S., Zand D.J., Dey A., Marks M.S., Nagata T., Grippo J.F., Ozato K. Dominant negative retinoid×receptor β inhibits retinoic acid-responsive gene regulation in embryonal carcinoma cells. Mol. Cell. Biol. 14:1994;360-372.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 360-372
    • Minucci, S.1    Zand, D.J.2    Dey, A.3    Marks, M.S.4    Nagata, T.5    Grippo, J.F.6    Ozato, K.7
  • 29
    • 0029931972 scopus 로고    scopus 로고
    • The orphan nuclear hormone receptor LXR α interacts with the peroxisome proliferator-activated receptor and inhibits peroxisome proliferator signalling
    • Miyata K.S., McCaw S.E., Patel H.V., Rachubinski R.A., Capone J.P. The orphan nuclear hormone receptor LXR α interacts with the peroxisome proliferator-activated receptor and inhibits peroxisome proliferator signalling. J. Biol. Chem. 271:1996;9189-9192.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9189-9192
    • Miyata, K.S.1    McCaw, S.E.2    Patel, H.V.3    Rachubinski, R.A.4    Capone, J.P.5
  • 31
    • 0025726848 scopus 로고
    • Two cis-acting regulatory elements in the peroxisome proliferator-responsive element enhancer region of rat acyl-CoA oxidase gene
    • Osumi T., Wen J.K., Hashimoto T. Two cis-acting regulatory elements in the peroxisome proliferator-responsive element enhancer region of rat acyl-CoA oxidase gene. Biochem. Biophys. Res. Commun. 175:1991;866-871.
    • (1991) Biochem. Biophys. Res. Commun. , vol.175 , pp. 866-871
    • Osumi, T.1    Wen, J.K.2    Hashimoto, T.3
  • 32
    • 0029643780 scopus 로고
    • Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid
    • 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.
    • (1995) Nature , vol.378 , pp. 681-689
    • Renaud, J.-P.1    Rochel, N.2    Ruff, M.3    Vivat, V.4    Chambon, P.5    Gronemeyer, H.6    Moras, D.7
  • 33
    • 0026785388 scopus 로고
    • Identification of a new member of the steroid hormone receptor superfamily that is activated by a peroxisome proliferator and fatty acid
    • Schmidt, A., Endo, N., Rutledge, S.J., Vogel, R., Shinar, D., Rodan, G.A., 1992. Identification of a new member of the steroid hormone receptor superfamily that is activated by a peroxisome proliferator and fatty acid, Mol. Endocrinol. 1634-1641.
    • (1992) Mol. Endocrinol. , pp. 1634-1641
    • Schmidt, A.1    Endo, N.2    Rutledge, S.J.3    Vogel, R.4    Shinar, D.5    Rodan, G.A.6
  • 35
    • 0030602866 scopus 로고    scopus 로고
    • The peroxisome proliferator activated receptors (PPARs) and their effects on lipid metabolism and adipocyte differentiation
    • Schoonjans K., Staels B., Auwerx J. The peroxisome proliferator activated receptors (PPARs) and their effects on lipid metabolism and adipocyte differentiation. Biochim. Biophys. Acta. 1302:1996;93-109.
    • (1996) Biochim. Biophys. Acta , vol.1302 , pp. 93-109
    • Schoonjans, K.1    Staels, B.2    Auwerx, J.3
  • 37
    • 0028641559 scopus 로고
    • Stimulation of adipogenesis in fibroblasts by PPARγ2, a lipid activated transcription factor
    • Tontonoz P., Hu E., Spiegelman B.M. Stimulation of adipogenesis in fibroblasts by PPARγ2, a lipid activated transcription factor. Cell. 79:1994;1147-1156.
    • (1994) Cell , vol.79 , pp. 1147-1156
    • Tontonoz, P.1    Hu, E.2    Spiegelman, B.M.3
  • 38
    • 0028988487 scopus 로고
    • PPARγ2 regulates adipose expression of the phospoenolpyruvate carboxykinase gene
    • Tontonoz P., Hu E., Devine J., Geale E.G., Spiegelman B.M. PPARγ2 regulates adipose expression of the phospoenolpyruvate carboxykinase gene. Mol. Cell. Biol. 15:1995;351-357.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 351-357
    • Tontonoz, P.1    Hu, E.2    Devine, J.3    Geale, E.G.4    Spiegelman, B.M.5
  • 39
    • 0026541591 scopus 로고
    • The mouse peroxisome-proliferator-activated receptor recognizes a response element in the 5′ flanking sequence of the rat acyl CoA oxidase gene
    • Tugwood J.D., Isseman I., Anderson R.G., Bundell K.R., McPheat W.L., Green S. The mouse peroxisome-proliferator-activated receptor recognizes a response element in the 5′ flanking sequence of the rat acyl CoA oxidase gene. EMBO J. 11:1992;433-439.
    • (1992) EMBO J. , vol.11 , pp. 433-439
    • Tugwood, J.D.1    Isseman, I.2    Anderson, R.G.3    Bundell, K.R.4    McPheat, W.L.5    Green, S.6
  • 41
    • 0029954339 scopus 로고    scopus 로고
    • TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors
    • Voegel J.J., Heine M.J.S., Zechel C., Chambon P., Gronemeyer H. TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors. EMBO J. 15:1996;3667-3675.
    • (1996) EMBO J. , vol.15 , pp. 3667-3675
    • Voegel, J.J.1    Heine, M.J.S.2    Zechel, C.3    Chambon, P.4    Gronemeyer, H.5
  • 42
    • 0030877565 scopus 로고    scopus 로고
    • Ligand-independent activation domain in the N-terminus of peroxisome proliferator-activated receptor γ (PPARγ)
    • Werman A., Hollenberg A., Solanes G., Bjorbaek C., Vidal-Puig A.J., Flier J.S. Ligand-independent activation domain in the N-terminus of peroxisome proliferator-activated receptor γ (PPARγ). J. Biol. Chem. 272:1997;20230-20235.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20230-20235
    • Werman, A.1    Hollenberg, A.2    Solanes, G.3    Bjorbaek, C.4    Vidal-Puig, A.J.5    Flier, J.S.6
  • 43
  • 44
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
    • Yang X.J., Ogryzko V.V., Nishikawa J., Howard B.H., Nakatani Y. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature. 382:1996;319-324.
    • (1996) Nature , vol.382 , pp. 319-324
    • Yang, X.J.1    Ogryzko, V.V.2    Nishikawa, J.3    Howard, B.H.4    Nakatani, Y.5
  • 45
    • 0027749599 scopus 로고
    • Cloning of a new member of the peroxisome proliferator-activated receptor gene family from mouse liver
    • Zhu Y., Alvares K., Huang Q., Sambasiva Rao M., Reddy J.K. Cloning of a new member of the peroxisome proliferator-activated receptor gene family from mouse liver. J. Biol. Chem. 268:1993;26817-26820.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26817-26820
    • Zhu, Y.1    Alvares, K.2    Huang, Q.3    Sambasiva Rao, M.4    Reddy, J.K.5
  • 46
    • 0029102676 scopus 로고
    • Structural organization of mouse peroxisome proliferator-activated receptor γ (mPPARγ) gene: Alternative promoter use and different splicing yield two mPPARγ isoforms
    • Zhu Y., Qi C., Korenberg J.R., Chen X.N., Noya D., Sambasiva Rao M., Reddy J.K. Structural organization of mouse peroxisome proliferator-activated receptor γ (mPPARγ) gene: alternative promoter use and different splicing yield two mPPARγ isoforms. Proc. Natl. Acad. Sci. U.S.A. 92:1995;7921-7925.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 7921-7925
    • Zhu, Y.1    Qi, C.2    Korenberg, J.R.3    Chen, X.N.4    Noya, D.5    Sambasiva Rao, M.6    Reddy, J.K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.