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Volumn 10, Issue 9, 2002, Pages 1225-1234

Hepatocyte nuclear factor 4 is a transcription factor that constitutively binds fatty acids

Author keywords

Diabetes; Fatty acids; HNF4; MODY; Nuclear receptor; Transcription factor

Indexed keywords

BASIC HELIX LOOP HELIX LEUCINE ZIPPER TRANSCRIPTION FACTOR; DNA BINDING PROTEIN; FATTY ACID; HEPATOCYTE NUCLEAR FACTOR 4; HNF4A PROTEIN, HUMAN; HNF4G PROTEIN, HUMAN; ISOPROTEIN; MLX PROTEIN, HUMAN; PHOSPHOPROTEIN; TRANSCRIPTION FACTOR; CELL NUCLEUS RECEPTOR; CHLOROFORM; FATTY ACID BINDING PROTEIN; LIGAND; METHANOL; PALMITIC ACID;

EID: 0036710140     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(02)00829-8     Document Type: Article
Times cited : (272)

References (49)
  • 1
    • 0035992181 scopus 로고    scopus 로고
    • Genomics versus orphan nuclear receptors: A half-time report
    • Willson T., Moore J. Genomics versus orphan nuclear receptors. a half-time report Mol. Endocrinol. 16:2002;1135-1144
    • (2002) Mol. Endocrinol , vol.16 , pp. 1135-1144
    • Willson, T.1    Moore, J.2
  • 2
    • 0025690311 scopus 로고
    • Liver-enriched transcription factor HNF-4 is a novel member of the steroid hormone receptor superfamily
    • Sladek F.M., Zhong W., Lai E., Darnell J.E. Jr. Liver-enriched transcription factor HNF-4 is a novel member of the steroid hormone receptor superfamily. Genes Dev. 4:1990;2353-2365
    • (1990) Genes Dev , vol.4 , pp. 2353-2365
    • Sladek, F.M.1    Zhong, W.2    Lai, E.3    Darnell, J.E.4
  • 3
    • 0034035239 scopus 로고    scopus 로고
    • Genotype/phenotype relationships in HNF-4α/MODY1: Haploinsufficiency is associated with reduced apolipoprotein (AII), apolipoprotein (CIII), lipoprotein(a), and triglyceride levels
    • Shih D.Q., Dansky H.M., Fleisher M., Assmann G., Fajans S.S., Stoffel M. Genotype/phenotype relationships in HNF-4α/MODY1. haploinsufficiency is associated with reduced apolipoprotein (AII), apolipoprotein (CIII), lipoprotein(a), and triglyceride levels Diabetes. 49:2000;832-837
    • (2000) Diabetes , vol.49 , pp. 832-837
    • Shih, D.Q.1    Dansky, H.M.2    Fleisher, M.3    Assmann, G.4    Fajans, S.S.5    Stoffel, M.6
  • 4
    • 0026589377 scopus 로고
    • Antagonism between apolipoprotein AI regulatory protein 1, Ear3/COUP-TF, and hepatocyte nuclear factor 4 modulates apolipoprotein CIII gene expression in liver and intestinal cells
    • Mietus-Snyder M., Sladek F.M., Ginsburg G.S., Kuo C.F., Ladias J.A.A., Darnell J.E. Jr., Karathanasis S.K. Antagonism between apolipoprotein AI regulatory protein 1, Ear3/COUP-TF, and hepatocyte nuclear factor 4 modulates apolipoprotein CIII gene expression in liver and intestinal cells. Mol. Cell. Biol. 12:1992;1708-1718
    • (1992) Mol. Cell. Biol , vol.12 , pp. 1708-1718
    • Mietus-Snyder, M.1    Sladek, F.M.2    Ginsburg, G.S.3    Kuo, C.F.4    Ladias, J.A.A.5    Darnell, J.E.6    Karathanasis, S.K.7
  • 5
    • 0027229650 scopus 로고
    • HNF-4 increases activity of the rat Apo A1 gene
    • Chan J., Nakabayashi H., Wong N.C.W. HNF-4 increases activity of the rat Apo A1 gene. Nucleic Acids Res. 21:1993;1205-1211
    • (1993) Nucleic Acids Res , vol.21 , pp. 1205-1211
    • Chan, J.1    Nakabayashi, H.2    Wong, N.C.W.3
  • 7
    • 0028246642 scopus 로고
    • Expression of the L-type pyruvate kinase gene and the hepatocyte nuclear factor 4 transcription factor in exocrine and endocrine pancreas
    • Miquerol L., Lopez S., Cartier N., Tulliez M., Raymondjean M., Kahn A. Expression of the L-type pyruvate kinase gene and the hepatocyte nuclear factor 4 transcription factor in exocrine and endocrine pancreas. J. Biol. Chem. 269:1994;8944-8951
    • (1994) J. Biol. Chem , vol.269 , pp. 8944-8951
    • Miquerol, L.1    Lopez, S.2    Cartier, N.3    Tulliez, M.4    Raymondjean, M.5    Kahn, A.6
  • 8
    • 0030695445 scopus 로고    scopus 로고
    • The maturity-onset diabetes of the young (MODY1) transcription factor HNF4α regulates expression of genes required for glucose transport and metabolism
    • Stoffel M., Duncan S.A. The maturity-onset diabetes of the young (MODY1) transcription factor HNF4α regulates expression of genes required for glucose transport and metabolism. Proc. Natl. Acad. Sci. USA. 94:1997;13209-13214
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13209-13214
    • Stoffel, M.1    Duncan, S.A.2
  • 9
    • 0032553439 scopus 로고    scopus 로고
    • SRC-1 and GRIP1 coactivate transcription with hepatocyte nuclear factor 4
    • Wang J.-C., Stafford J.M., Granner D.K. SRC-1 and GRIP1 coactivate transcription with hepatocyte nuclear factor 4. J. Biol. Chem. 273:1998;30847-30850
    • (1998) J. Biol. Chem , vol.273 , pp. 30847-30850
    • Wang, J.-C.1    Stafford, J.M.2    Granner, D.K.3
  • 12
    • 0032473950 scopus 로고    scopus 로고
    • Fatty acyl-CoA thioesters are ligands of hepatic nuclear factor-4α
    • Hertz R., Magenheim J., Berman I., Bar-Tana J. Fatty acyl-CoA thioesters are ligands of hepatic nuclear factor-4α Nature. 392:1998;512-516
    • (1998) Nature , vol.392 , pp. 512-516
    • Hertz, R.1    Magenheim, J.2    Berman, I.3    Bar-Tana, J.4
  • 14
    • 0031852095 scopus 로고    scopus 로고
    • Natural ligands of nuclear receptors have conserved volumes
    • Bogan A.A., Cohen F.E., Scanlan T.S. Natural ligands of nuclear receptors have conserved volumes. Nat. Struct. Biol. 5:1998;679-681
    • (1998) Nat. Struct. Biol , vol.5 , pp. 679-681
    • Bogan, A.A.1    Cohen, F.E.2    Scanlan, T.S.3
  • 15
    • 0032575057 scopus 로고    scopus 로고
    • Atomic structure of progesterone complexed with its receptor
    • Williams S.P., Sigler P.B. Atomic structure of progesterone complexed with its receptor. Nature. 393:1998;392-396
    • (1998) Nature , vol.393 , pp. 392-396
    • Williams, S.P.1    Sigler, P.B.2
  • 16
    • 0034714276 scopus 로고    scopus 로고
    • Structural evidence for ligand specificity in the binding domain of the human androgen receptor. Implications for pathogenic gene mutations
    • Matias P.M., Donner P., Coelho R., Thomaz M., Peixoto C., Macedo S., Otto N., Joschko S., Scholz P., Wegg A.et al. Structural evidence for ligand specificity in the binding domain of the human androgen receptor. Implications for pathogenic gene mutations. J. Biol. Chem. 275:2000;26164-26171
    • (2000) J. Biol. Chem , vol.275 , pp. 26164-26171
    • Matias, P.M.1    Donner, P.2    Coelho, R.3    Thomaz, M.4    Peixoto, C.5    Macedo, S.6    Otto, N.7    Joschko, S.8    Scholz, P.9    Wegg, A.10
  • 17
    • 0033868825 scopus 로고    scopus 로고
    • Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains
    • Bourguet W., Vivat V., Wurtz J.-M., Chambon P., Gronemeyer H., Moras D. Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains. Mol. Cell. 5:2000;289-298
    • (2000) Mol. Cell , vol.5 , pp. 289-298
    • Bourguet, W.1    Vivat, V.2    Wurtz, J.-M.3    Chambon, P.4    Gronemeyer, H.5    Moras, D.6
  • 19
    • 0029113123 scopus 로고
    • Exclusive homodimerization of the orphan receptor hepatocyte nuclear factor 4 defines a new subclass of nuclear receptors
    • Jiang G., Nepomuceno L., Hopkins K., Sladek F.M. Exclusive homodimerization of the orphan receptor hepatocyte nuclear factor 4 defines a new subclass of nuclear receptors. Mol. Cell. Biol. 15:1995;5131-5143
    • (1995) Mol. Cell. Biol , vol.15 , pp. 5131-5143
    • Jiang, G.1    Nepomuceno, L.2    Hopkins, K.3    Sladek, F.M.4
  • 20
    • 0031012836 scopus 로고    scopus 로고
    • The DNA binding domain of hepatocyte nuclear factor 4 mediates cooperative, specific binding to DNA and heterodimerization with the retinoid X receptor α
    • Jiang G., Sladek F.M. The DNA binding domain of hepatocyte nuclear factor 4 mediates cooperative, specific binding to DNA and heterodimerization with the retinoid X receptor α J. Biol. Chem. 272:1997;1218-1225
    • (1997) J. Biol. Chem , vol.272 , pp. 1218-1225
    • Jiang, G.1    Sladek, F.M.2
  • 21
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha
    • 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
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, P.3    Gronemeyer, H.4    Moras, D.5
  • 24
    • 0016817502 scopus 로고
    • Thermal regulation of the membrane lipid composition of Escherichia coli
    • Cronan J.E.J. Thermal regulation of the membrane lipid composition of Escherichia coli. J. Biol. Chem. 250:1975;7074-7077
    • (1975) J. Biol. Chem , vol.250 , pp. 7074-7077
    • Cronan, J.E.J.1
  • 25
    • 84989085007 scopus 로고
    • Carbon-13 NMR spectroscopy. Part XII. Vicinal carbon-hydrogen spin coupling in substituted alkenes. Stereochemical significance and structural effects
    • Vogeli U., Von Philipsborn W. Carbon-13 NMR spectroscopy. Part XII. Vicinal carbon-hydrogen spin coupling in substituted alkenes. Stereochemical significance and structural effects. Org. Magn. Reson. 7:1975;617-627
    • (1975) Org. Magn. Reson , vol.7 , pp. 617-627
    • Vogeli, U.1    Von Philipsborn, W.2
  • 26
    • 0345311216 scopus 로고
    • Proton and carbon-13 assignments from sensitivity-enhanced detection of heteronuclear multiple-bond connectivity by 2D multiple quantum NMR
    • Bax A., Summers M.F. Proton and carbon-13 assignments from sensitivity-enhanced detection of heteronuclear multiple-bond connectivity by 2D multiple quantum NMR. J. Am. Chem. Soc. 108:1986;2093-2094
    • (1986) J. Am. Chem. Soc , vol.108 , pp. 2093-2094
    • Bax, A.1    Summers, M.F.2
  • 27
    • 0001736119 scopus 로고
    • An improved method for two-dimensional heteronuclear relayed-coherence-transfer NMR spectroscopy
    • Bax A., Davis D.G., Sarkar S.K. An improved method for two-dimensional heteronuclear relayed-coherence-transfer NMR spectroscopy. J. Magn. Reson. 63:1985;230-234
    • (1985) J. Magn. Reson , vol.63 , pp. 230-234
    • Bax, A.1    Davis, D.G.2    Sarkar, S.K.3
  • 28
    • 0005178164 scopus 로고
    • Improvement of carbon-detected proton-proton-TOCSY experiments by employing a DEPT transfer
    • Kessler H., Gemmecker G., Koeck K., Osowski R., Schmieder P. Improvement of carbon-detected proton-proton-TOCSY experiments by employing a DEPT transfer. Magn. Reson. Chem. 28:1990;62-67
    • (1990) Magn. Reson. Chem , vol.28 , pp. 62-67
    • Kessler, H.1    Gemmecker, G.2    Koeck, K.3    Osowski, R.4    Schmieder, P.5
  • 29
    • 0035831522 scopus 로고    scopus 로고
    • Crystal structure of the ligand-binding domain of the ultraspiracle protein USP, the OrthoIog of retinoid X receptors in insects
    • Billas I.M.L., Moulinier L., Rochel N., Moras D. Crystal structure of the ligand-binding domain of the ultraspiracle protein USP, the OrthoIog of retinoid X receptors in insects. J. Biol. Chem. 276:2001;7465-7474
    • (2001) J. Biol. Chem , vol.276 , pp. 7465-7474
    • Billas, I.M.L.1    Moulinier, L.2    Rochel, N.3    Moras, D.4
  • 30
    • 0035852767 scopus 로고    scopus 로고
    • The structure of the ultraspiracle ligand-binding domain reveals a nuclear receptor locked in an inactive conformation
    • Clayton G.M., Peak-Chew S.Y., Evans R.M., Schwabe J.W.R. The structure of the ultraspiracle ligand-binding domain reveals a nuclear receptor locked in an inactive conformation. Proc. Natl. Acad. Sci. USA. 98:2001;1549-1554
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1549-1554
    • Clayton, G.M.1    Peak-Chew, S.Y.2    Evans, R.M.3    Schwabe, J.W.R.4
  • 32
    • 0035502971 scopus 로고    scopus 로고
    • X-ray structure of the orphan nuclear receptor RORβ ligand-binding domain in the active conformation
    • Stehlin C., Wurtz J.-M., Steinmetz A., Greiner E., Schule R., Moras D., Renaud J.-P. X-ray structure of the orphan nuclear receptor RORβ ligand-binding domain in the active conformation. EMBO J. 20:2001;5822-5831
    • (2001) EMBO J , vol.20 , pp. 5822-5831
    • Stehlin, C.1    Wurtz, J.-M.2    Steinmetz, A.3    Greiner, E.4    Schule, R.5    Moras, D.6    Renaud, J.-P.7
  • 33
    • 0034086140 scopus 로고    scopus 로고
    • Origins and evolutionary diversification of the nuclear receptor superfamily
    • Owen G., Zelent A. Origins and evolutionary diversification of the nuclear receptor superfamily. Cell. Mol. Life Sci. 57:2000;809-827
    • (2000) Cell. Mol. Life Sci , vol.57 , pp. 809-827
    • Owen, G.1    Zelent, A.2
  • 34
    • 0026726806 scopus 로고
    • Hormone and antihormone induce distinct conformational changes which are central to steroid receptor activation
    • Allan G.F., Leng X., 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    Leng, X.2    Tsai, S.Y.3    Weigel, N.L.4    Edwards, D.P.5    Tsai, M.J.6    O'Malley, B.W.7
  • 36
    • 0034680936 scopus 로고    scopus 로고
    • Hepatocyte nuclear factor 4α regulates the expression of pancreatic β-cell genes implicated in glucose metabolism and nutrient-induced insulin secretion
    • Wang H., Maechler P., Antinozzi P.A., Hagenfeldt K.A., Wollheim C.B. Hepatocyte nuclear factor 4α regulates the expression of pancreatic β-cell genes implicated in glucose metabolism and nutrient-induced insulin secretion. J. Biol. Chem. 275:2000;35953-35959
    • (2000) J. Biol. Chem , vol.275 , pp. 35953-35959
    • Wang, H.1    Maechler, P.2    Antinozzi, P.A.3    Hagenfeldt, K.A.4    Wollheim, C.B.5
  • 37
    • 0035342271 scopus 로고    scopus 로고
    • Suppression of hepatocyte nuclear factor-4α by acyl-CoA thioesters of hypolipidemic peroxisome proliferators
    • Hertz R., Sheena V., Kalderon B., Berman I., Bar-Tana J. Suppression of hepatocyte nuclear factor-4α by acyl-CoA thioesters of hypolipidemic peroxisome proliferators. Biochem. Pharmacol. 61:2001;1057-1062
    • (2001) Biochem. Pharmacol , vol.61 , pp. 1057-1062
    • Hertz, R.1    Sheena, V.2    Kalderon, B.3    Berman, I.4    Bar-Tana, J.5
  • 39
    • 0030877342 scopus 로고    scopus 로고
    • Protein kinase A-dependent phosphorylation modulates DNA-binding activity of hepatocyte nuclear factor 4
    • Viollet B., Kahn A., Raymondjean M. Protein kinase A-dependent phosphorylation modulates DNA-binding activity of hepatocyte nuclear factor 4. Mol. Cell. Biol. 17:1997;4208-4219
    • (1997) Mol. Cell. Biol , vol.17 , pp. 4208-4219
    • Viollet, B.1    Kahn, A.2    Raymondjean, M.3
  • 40
    • 0033986961 scopus 로고    scopus 로고
    • The orphan nuclear receptor SHP inhibits hepatocyte nuclear factor 4 and retinoid X receptor transactivation: Two mechanisms for repression
    • Lee Y.-K., Dell H., Dowhan D.H., Hadzopoulou-Cladaras M., Moore D.D. The orphan nuclear receptor SHP inhibits hepatocyte nuclear factor 4 and retinoid X receptor transactivation. two mechanisms for repression Mol. Cell. Biol. 20:2000;187-195
    • (2000) Mol. Cell. Biol , vol.20 , pp. 187-195
    • Lee, Y.-K.1    Dell, H.2    Dowhan, D.H.3    Hadzopoulou-Cladaras, M.4    Moore, D.D.5
  • 41
    • 0345588573 scopus 로고    scopus 로고
    • Shake-and-bake: Applications and advances
    • for solving protein structures
    • Miller R., Weeks C.M. Shake-and-bake. applications and advances NATO ASI Ser. Ser. C. 507:1998;389-400. [for solving protein structures]
    • (1998) NATO ASI Ser. Ser. C , vol.507 , pp. 389-400
    • Miller, R.1    Weeks, C.M.2
  • 42
  • 43
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams J.P., Leslie A.G.W. Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallogr. D. 52:1996;30-42
    • (1996) Acta Crystallogr. D , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.W.2
  • 47
    • 0027234208 scopus 로고
    • Analysis of the rat hepatocyte nuclear factor (HNF) 1 gene promoter: Synergistic activation by HNF4 and HNF1 proteins
    • Miura N., Tanaka K. Analysis of the rat hepatocyte nuclear factor (HNF) 1 gene promoter. Synergistic activation by HNF4 and HNF1 proteins Nucleic Acids Res. 21:1993;3731-3736
    • (1993) Nucleic Acids Res , vol.21 , pp. 3731-3736
    • Miura, N.1    Tanaka, K.2
  • 48
    • 0023649835 scopus 로고
    • CAT constructions with multiple unique restriction sites for the functional analysis of eukaryotic promoters and regulatory elements
    • Luckow B., Schutz G. CAT constructions with multiple unique restriction sites for the functional analysis of eukaryotic promoters and regulatory elements. Nucleic Acids Res. 15:1987;5490
    • (1987) Nucleic Acids Res , vol.15 , pp. 5490
    • Luckow, B.1    Schutz, G.2
  • 49
    • 0029016829 scopus 로고
    • An antidiabetic thiazolidinedione is a high affinity ligand for peroxisome proliferator-activated receptor γ (PPARγ)
    • 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 peroxisome proliferator-activated receptor γ (PPARγ). 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


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