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Volumn 410, Issue 4, 2011, Pages 749-753

Multiple post-translational modifications in hepatocyte nuclear factor 4α

Author keywords

Acetylation; Hepatocyte nuclear factor 4 ; Post translational modification

Indexed keywords

HEPATOCYTE NUCLEAR FACTOR 4ALPHA; LYSINE;

EID: 79960338300     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.06.033     Document Type: Article
Times cited : (34)

References (36)
  • 1
    • 52449132322 scopus 로고    scopus 로고
    • Is there a code embedded in proteins that is based on post-translational modifications?
    • Sims R.J., Reinberg D. Is there a code embedded in proteins that is based on post-translational modifications?. Nat. Rev. Mol. Cell. Biol. 2008, 9:815-820.
    • (2008) Nat. Rev. Mol. Cell. Biol. , vol.9 , pp. 815-820
    • Sims, R.J.1    Reinberg, D.2
  • 2
    • 28044433451 scopus 로고    scopus 로고
    • Protein posttranslational modifications: the chemistry of proteome diversifications
    • Walsh C.T., Garneau-Tsodikova S., Gatto G.J. Protein posttranslational modifications: the chemistry of proteome diversifications. Angew. Chem. Int. Ed. Engl. 2005, 44:7342-7372.
    • (2005) Angew. Chem. Int. Ed. Engl. , vol.44 , pp. 7342-7372
    • Walsh, C.T.1    Garneau-Tsodikova, S.2    Gatto, G.J.3
  • 3
    • 35848970747 scopus 로고    scopus 로고
    • Mapping protein post-translational modifications with mass spectrometry
    • Witze E.S., Old W.M., Resing K.A., Ahn N.G. Mapping protein post-translational modifications with mass spectrometry. Nat. Methods 2007, 4:798-806.
    • (2007) Nat. Methods , vol.4 , pp. 798-806
    • Witze, E.S.1    Old, W.M.2    Resing, K.A.3    Ahn, N.G.4
  • 4
    • 39749099462 scopus 로고    scopus 로고
    • Strategy for comprehensive identification of post-translational modifications in cellular proteins, including low abundant modifications: application to glyceraldehyde-3-phosphate dehydrogenase
    • Seo J., Jeong J., Kim Y.M., Hwang N., Paek E., Lee K.J. Strategy for comprehensive identification of post-translational modifications in cellular proteins, including low abundant modifications: application to glyceraldehyde-3-phosphate dehydrogenase. J. Proteome Res. 2008, 7:587-602.
    • (2008) J. Proteome Res. , vol.7 , pp. 587-602
    • Seo, J.1    Jeong, J.2    Kim, Y.M.3    Hwang, N.4    Paek, E.5    Lee, K.J.6
  • 5
    • 5644247544 scopus 로고    scopus 로고
    • Strategies for shotgun identification of post-translational modifications by mass spectrometry
    • Cantin G.T., Yates J.R. Strategies for shotgun identification of post-translational modifications by mass spectrometry. J. Chromatogr. A 2004, 1053:7-14.
    • (2004) J. Chromatogr. A , vol.1053 , pp. 7-14
    • Cantin, G.T.1    Yates, J.R.2
  • 6
    • 71549136813 scopus 로고    scopus 로고
    • Identification and quantification of protein posttranslational modifications
    • Farley A.R., Link A.J. Identification and quantification of protein posttranslational modifications. Methods Enzymol. 2009, 463:725-763.
    • (2009) Methods Enzymol. , vol.463 , pp. 725-763
    • Farley, A.R.1    Link, A.J.2
  • 8
    • 0033305499 scopus 로고    scopus 로고
    • Orphan nuclear receptors: from gene to function
    • Giguere V. Orphan nuclear receptors: from gene to function. Endocr. Rev. 1999, 20:689-725.
    • (1999) Endocr. Rev. , vol.20 , pp. 689-725
    • Giguere, V.1
  • 9
    • 42249106086 scopus 로고    scopus 로고
    • Regulation of hepatocyte nuclear factor 4 alpha-mediated transcription
    • Gonzalez F.J. Regulation of hepatocyte nuclear factor 4 alpha-mediated transcription. Drug Metab. Pharmacokinet. 2008, 23:2-7.
    • (2008) Drug Metab. Pharmacokinet. , vol.23 , pp. 2-7
    • Gonzalez, F.J.1
  • 11
    • 33748357551 scopus 로고    scopus 로고
    • Mutations in the genes encoding the transcription factors hepatocyte nuclear factor 1 alpha (HNF1A) and 4 alpha (HNF4A) in maturity-onset diabetes of the young
    • Ellard S., Colclough K. Mutations in the genes encoding the transcription factors hepatocyte nuclear factor 1 alpha (HNF1A) and 4 alpha (HNF4A) in maturity-onset diabetes of the young. Hum. Mutat. 2006, 27:854-869.
    • (2006) Hum. Mutat. , vol.27 , pp. 854-869
    • Ellard, S.1    Colclough, K.2
  • 12
    • 0025690311 scopus 로고
    • Liver-enriched transcription factor HNF-4 is a novel member of the steroid hormone receptor superfamily
    • Sladek F.M., Zhong W.M., Lai E., Darnell J.E. Liver-enriched transcription factor HNF-4 is a novel member of the steroid hormone receptor superfamily. Genes Dev. 1990, 4:2353-2365.
    • (1990) Genes Dev. , vol.4 , pp. 2353-2365
    • Sladek, F.M.1    Zhong, W.M.2    Lai, E.3    Darnell, J.E.4
  • 14
    • 0031054568 scopus 로고    scopus 로고
    • Murine gastrulation requires HNF-4 regulated gene expression in the visceral endoderm: tetraploid rescue of HNF-4(-/-) embryos
    • Duncan S.A., Nagy A., Chan W. Murine gastrulation requires HNF-4 regulated gene expression in the visceral endoderm: tetraploid rescue of HNF-4(-/-) embryos. Development 1997, 124:279-287.
    • (1997) Development , vol.124 , pp. 279-287
    • Duncan, S.A.1    Nagy, A.2    Chan, W.3
  • 15
    • 0035141324 scopus 로고    scopus 로고
    • Hepatocyte nuclear factor 4alpha (nuclear receptor 2A1) is essential for maintenance of hepatic gene expression and lipid homeostasis
    • Hayhurst G.P., Lee Y.H., Lambert G., Ward J.M., Gonzalez F.J. Hepatocyte nuclear factor 4alpha (nuclear receptor 2A1) is essential for maintenance of hepatic gene expression and lipid homeostasis. Mol. Cell. Biol. 2001, 21:1393-1403.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1393-1403
    • Hayhurst, G.P.1    Lee, Y.H.2    Lambert, G.3    Ward, J.M.4    Gonzalez, F.J.5
  • 16
    • 1842478960 scopus 로고    scopus 로고
    • Identification of a liver-specific uridine phosphorylase that is regulated by multiple lipid-sensing nuclear receptors
    • Zhang Y., Repa J.J., Inoue Y., Hayhurst G.P., Gonzalez F.J., Mangelsdorf D.J. Identification of a liver-specific uridine phosphorylase that is regulated by multiple lipid-sensing nuclear receptors. Mol. Endocrinol. 2004, 18:851-862.
    • (2004) Mol. Endocrinol. , vol.18 , pp. 851-862
    • Zhang, Y.1    Repa, J.J.2    Inoue, Y.3    Hayhurst, G.P.4    Gonzalez, F.J.5    Mangelsdorf, D.J.6
  • 17
    • 0037067687 scopus 로고    scopus 로고
    • Defective ureagenesis in mice carrying a liver-specific disruption of hepatocyte nuclear factor 4alpha (HNF4α). HNF4α regulates ornithine transcarbamylase in vivo
    • Inoue Y., Hayhurst G.P., Inoue J., Mori M., Gonzalez F.J. Defective ureagenesis in mice carrying a liver-specific disruption of hepatocyte nuclear factor 4alpha (HNF4α). HNF4α regulates ornithine transcarbamylase in vivo. J. Biol. Chem. 2002, 277:25257-25265.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25257-25265
    • Inoue, Y.1    Hayhurst, G.P.2    Inoue, J.3    Mori, M.4    Gonzalez, F.J.5
  • 19
    • 60649099790 scopus 로고    scopus 로고
    • Drosophila HNF4 regulates lipid mobilization and beta-oxidation
    • Palanker L., Tennessen J.M., Lam G., Thummel C.S. Drosophila HNF4 regulates lipid mobilization and beta-oxidation. Cell. Metab. 2009, 9:228-239.
    • (2009) Cell. Metab. , vol.9 , pp. 228-239
    • Palanker, L.1    Tennessen, J.M.2    Lam, G.3    Thummel, C.S.4
  • 24
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1
    • Rodgers J.T., Lerin C., Haas W., Gygi S.P., Spiegelman B.M., Puigserver P. Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature 2005, 434:113-118.
    • (2005) Nature , vol.434 , pp. 113-118
    • Rodgers, J.T.1    Lerin, C.2    Haas, W.3    Gygi, S.P.4    Spiegelman, B.M.5    Puigserver, P.6
  • 26
    • 33749238368 scopus 로고    scopus 로고
    • Gaining knowledge from previously unexplained spectra-application of the PTM-Explorer software to detect PTM in HUPO BPP MS/MS data
    • Chamrad D.C., Korting G., Schafer H., Stephan C., Thiele H., Apweiler R., Meyer H.E., Marcus K., Bluggel M. Gaining knowledge from previously unexplained spectra-application of the PTM-Explorer software to detect PTM in HUPO BPP MS/MS data. Proteomics 2006, 6:5048-5058.
    • (2006) Proteomics , vol.6 , pp. 5048-5058
    • Chamrad, D.C.1    Korting, G.2    Schafer, H.3    Stephan, C.4    Thiele, H.5    Apweiler, R.6    Meyer, H.E.7    Marcus, K.8    Bluggel, M.9
  • 27
    • 77149158441 scopus 로고    scopus 로고
    • Unrestricted identification of modified proteins using MS/MS
    • Ahrne E., Muller M., Lisacek F. Unrestricted identification of modified proteins using MS/MS. Proteomics 2010, 10:671-686.
    • (2010) Proteomics , vol.10 , pp. 671-686
    • Ahrne, E.1    Muller, M.2    Lisacek, F.3
  • 28
    • 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. 1997, 17:4208-4219.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4208-4219
    • Viollet, B.1    Kahn, A.2    Raymondjean, M.3
  • 30
    • 0033636892 scopus 로고    scopus 로고
    • Acetylation regulates transcription factor activity at multiple levels
    • Soutoglou E., Katrakili N., Talianidis I. Acetylation regulates transcription factor activity at multiple levels. Mol. Cell. 2000, 5:745-751.
    • (2000) Mol. Cell. , vol.5 , pp. 745-751
    • Soutoglou, E.1    Katrakili, N.2    Talianidis, I.3
  • 31
    • 0242349197 scopus 로고    scopus 로고
    • Regulation of hepatic fasting response by PPARγ coactivator-1alpha (PGC-1): requirement for hepatocyte nuclear factor 4α in gluconeogenesis
    • Rhee J., Inoue Y., Yoon J.C., Puigserver P., Fan M., Gonzalez F.J., Spiegelman B.M. Regulation of hepatic fasting response by PPARγ coactivator-1alpha (PGC-1): requirement for hepatocyte nuclear factor 4α in gluconeogenesis. Proc. Natl. Acad. Sci. USA 2003, 100:4012-4017.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4012-4017
    • Rhee, J.1    Inoue, Y.2    Yoon, J.C.3    Puigserver, P.4    Fan, M.5    Gonzalez, F.J.6    Spiegelman, B.M.7
  • 33
    • 0032850195 scopus 로고    scopus 로고
    • Modulation of transcriptional activation and coactivator interaction by a splicing variation in the F domain of nuclear receptor hepatocyte nuclear factor 4α1
    • Sladek F.M., Ruse M.D., Nepomuceno L., Huang S.M., Stallcup M.R. Modulation of transcriptional activation and coactivator interaction by a splicing variation in the F domain of nuclear receptor hepatocyte nuclear factor 4α1. Mol. Cell. Biol. 1999, 19:6509-6522.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6509-6522
    • Sladek, F.M.1    Ruse, M.D.2    Nepomuceno, L.3    Huang, S.M.4    Stallcup, M.R.5
  • 34
    • 20444475700 scopus 로고    scopus 로고
    • Role of regulatory F-domain in hepatocyte nuclear factor 4α ligand specificity
    • Petrescu A.D., Hertz R., Bar-Tana J., Schroeder F., Kier A.B. Role of regulatory F-domain in hepatocyte nuclear factor 4α ligand specificity. J. Biol. Chem. 2005, 280:16714-16727.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16714-16727
    • Petrescu, A.D.1    Hertz, R.2    Bar-Tana, J.3    Schroeder, F.4    Kier, A.B.5
  • 36
    • 0032077536 scopus 로고    scopus 로고
    • The activation function 2 domain of hepatic nuclear factor 4 is regulated by a short C-terminal proline-rich repressor domain
    • Iyemere V.P., Davies N.H., Brownlee G.G. The activation function 2 domain of hepatic nuclear factor 4 is regulated by a short C-terminal proline-rich repressor domain. Nucleic Acids Res. 1998, 26:2098-2104.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2098-2104
    • Iyemere, V.P.1    Davies, N.H.2    Brownlee, G.G.3


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