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Volumn 116, Issue 4, 2003, Pages 647-654

Mitochondrial and nucleocytoplasmic targeting of O-linked GlcNAc transferase

Author keywords

Glycan dependent signaling; Mitochondria; O GlcNAc; OGT

Indexed keywords

ANTISERUM; EPITOPE; ISOPROTEIN; N ACETYLGLUCOSAMINYLTRANSFERASE;

EID: 0037442984     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00246     Document Type: Review
Times cited : (174)

References (42)
  • 1
    • 0033499354 scopus 로고    scopus 로고
    • Localization of the O-linked N-acetylglucosamine transferase in rat pancreas
    • Akimoto, Y., Kreppel, L. K., Hirano, H. and Hart, G. W. (1999). Localization of the O-linked N-acetylglucosamine transferase in rat pancreas. Diabetes 48, 2407-2413.
    • (1999) Diabetes , vol.48 , pp. 2407-2413
    • Akimoto, Y.1    Kreppel, L.K.2    Hirano, H.3    Hart, G.W.4
  • 2
    • 0033786657 scopus 로고    scopus 로고
    • Increased O-GlcNAc transferase in pancreas of rats with streptozotocin-induced diabetes
    • Akimoto, Y., Kreppel, L. K., Hirano, H. and Hart, G. W. (2000). Increased O-GlcNAc transferase in pancreas of rats with streptozotocin-induced diabetes. Diabetologia 43, 1239-1247.
    • (2000) Diabetologia , vol.43 , pp. 1239-1247
    • Akimoto, Y.1    Kreppel, L.K.2    Hirano, H.3    Hart, G.W.4
  • 3
    • 0033065587 scopus 로고    scopus 로고
    • Leptin receptor long-form splice-variant protein expression in neuron cell bodies of the brain and co-localization with neuropeptide Y mRNA in the arcuate nucleus
    • Baskin, D. G., Schwartz, M. W., Seeley, R. J., Woods, S. C., Porte, A J., Breininger, J. F., Jonak, Z., Schaefer, J., Krouse, M., Burghardt, C. et al. (1999). Leptin receptor long-form splice-variant protein expression in neuron cell bodies of the brain and co-localization with neuropeptide Y mRNA in the arcuate nucleus. J. Histochem. Cytochem. 47, 353-362.
    • (1999) J. Histochem. Cytochem. , vol.47 , pp. 353-362
    • Baskin, D.G.1    Schwartz, M.W.2    Seeley, R.J.3    Woods, S.C.4    Porte, AJ.5    Breininger, J.F.6    Jonak, Z.7    Schaefer, J.8    Krouse, M.9    Burghardt, C.10
  • 4
    • 0344496513 scopus 로고    scopus 로고
    • The tetratricopeptide repeat: A structural motif mediating protein-protein interactions
    • Blatch, G. L. and Lassle, M. (1999). The tetratricopeptide repeat: a structural motif mediating protein-protein interactions. Bioessays 21, 932-939.
    • (1999) Bioessays , vol.21 , pp. 932-939
    • Blatch, G.L.1    Lassle, M.2
  • 6
    • 0035208654 scopus 로고    scopus 로고
    • Cytosolic O-glycosylation is abundant in nerve terminals
    • Cole, R. N. and Hart, G. W. (2001). Cytosolic O-glycosylation is abundant in nerve terminals. J. Neurochem. 79, 1080-1089.
    • (2001) J. Neurochem. , vol.79 , pp. 1080-1089
    • Cole, R.N.1    Hart, G.W.2
  • 7
    • 0032734974 scopus 로고    scopus 로고
    • O-GlcNAc and the control of gene expression
    • Comer, F. I. and Hart, G. W. (1999). O-GlcNAc and the control of gene expression. Biochim. Biophys. Acta. 1473, 161-171.
    • (1999) Biochim. Biophys. Acta. , vol.1473 , pp. 161-171
    • Comer, F.I.1    Hart, G.W.2
  • 8
    • 0024399051 scopus 로고
    • Glycosylation of eukaryotic peptide chain initiation factor 2 (eIF-2)-associated 67-kDa polypeptide (p67) and its possible role in the inhibition of eIF-2 kinase-catalyzed phosphorylation of the eIF-2 alpha-subunit
    • Datta, B., Ray, M. K., Chakrabarti, D., Wylie, D. E. and Gupta, N. K. (1989). Glycosylation of eukaryotic peptide chain initiation factor 2 (eIF-2)-associated 67-kDa polypeptide (p67) and its possible role in the inhibition of eIF-2 kinase-catalyzed phosphorylation of the eIF-2 alpha-subunit. J. Biol. Chem. 264, 20620-20624.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20620-20624
    • Datta, B.1    Ray, M.K.2    Chakrabarti, D.3    Wylie, D.E.4    Gupta, N.K.5
  • 9
    • 0034710891 scopus 로고    scopus 로고
    • Hyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation
    • Du, X. L., Edelstein, D., Rossetti, L., Fantus, I. G., Goldberg, H., Ziyadeh, F., Wu, J. and Brownlee, M. (2000). Hyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation. Proc. Natl. Acad. Sci. USA 97, 12222-12226.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12222-12226
    • Du, X.L.1    Edelstein, D.2    Rossetti, L.3    Fantus, I.G.4    Goldberg, H.5    Ziyadeh, F.6    Wu, J.7    Brownlee, M.8
  • 10
    • 0035180299 scopus 로고    scopus 로고
    • Hyperglycemia inhibits endothelial nitric oxide synthase activity by posttranslational modification at the Akt site
    • Du, X. L., Edelstein, D., Dimmeler, S., Ju, Q., Sui, C. and Brownlee, M. (2001). Hyperglycemia inhibits endothelial nitric oxide synthase activity by posttranslational modification at the Akt site. J. Clin. Invest. 108, 1341-1348.
    • (2001) J. Clin. Invest. , vol.108 , pp. 1341-1348
    • Du, X.L.1    Edelstein, D.2    Dimmeler, S.3    Ju, Q.4    Sui, C.5    Brownlee, M.6
  • 11
    • 0026795976 scopus 로고
    • Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine: Polypeptide beta-N-acetylglucosaminyltransferase
    • Haltiwanger, R. S., Blomberg, M. A. and Hart, G. W. (1992). Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine: polypeptide beta-N-acetylglucosaminyltransferase. J. Biol. Chem. 267, 9005-9013.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9005-9013
    • Haltiwanger, R.S.1    Blomberg, M.A.2    Hart, G.W.3
  • 12
    • 0034854157 scopus 로고    scopus 로고
    • Glycan-dependent signaling: O-linked N-acetylglucosamine
    • Hanover, J. A. (2001). Glycan-dependent signaling: O-linked N-acetylglucosamine. FASEB J. 15, 1865-1876.
    • (2001) FASEB J. , vol.15 , pp. 1865-1876
    • Hanover, J.A.1
  • 13
    • 0023655430 scopus 로고
    • O-linked N-acetylglucosamine is attached to proteins of the nuclear pore. Evidence for cytoplasmic and nucleoplasmic glycoproteins
    • Hanover, J. A., Cohen, C. K., Willingham, M. C. and Park, M. K. (1987). O-linked N-acetylglucosamine is attached to proteins of the nuclear pore. Evidence for cytoplasmic and nucleoplasmic glycoproteins. J. Biol. Chem. 262, 9887-9894.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9887-9894
    • Hanover, J.A.1    Cohen, C.K.2    Willingham, M.C.3    Park, M.K.4
  • 14
    • 0033080192 scopus 로고    scopus 로고
    • Elevated O-linked N-acetylglucosamine metabolism in pancreatic beta-cells
    • Hanover, J. A., Lai, Z., Lee, G., Lubas, W. A. and Sato, S. M. (1999). Elevated O-linked N-acetylglucosamine metabolism in pancreatic beta-cells. Arch. Biochem. Biophys. 362, 38-45.
    • (1999) Arch. Biochem. Biophys. , vol.362 , pp. 38-45
    • Hanover, J.A.1    Lai, Z.2    Lee, G.3    Lubas, W.A.4    Sato, S.M.5
  • 15
    • 0013429715 scopus 로고    scopus 로고
    • Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc Transferase (OGT) encoded by a single mammalian gene
    • (in press)
    • Hanover, J. A., Yu, S., Lubas, W. A., Shin, S. H., Ragano-Caracciola, M., Kochran, J. and Love, D. C. (2002). Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc Transferase (OGT) encoded by a single mammalian gene. Arch Biochem Biophys. (in press).
    • (2002) Arch Biochem Biophys.
    • Hanover, J.A.1    Yu, S.2    Lubas, W.A.3    Shin, S.H.4    Ragano-Caracciola, M.5    Kochran, J.6    Love, D.C.7
  • 17
    • 0023037076 scopus 로고
    • The subcellular distribution of terminal N-acetylglucosamine moieties. Localization of a novel protein-saccharide linkage, O-linked GlcNAc
    • Holt, G. D. and Hart, G. W. (1986). The subcellular distribution of terminal N-acetylglucosamine moieties. Localization of a novel protein-saccharide linkage, O-linked GlcNAc. J. Biol. Chem. 261, 8049-8057.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8049-8057
    • Holt, G.D.1    Hart, G.W.2
  • 18
    • 0024516198 scopus 로고
    • Glycosylation of chromosomal proteins: Localization of O-linked N-acetylglucosamine in Drosophila chromatin
    • Kelly, W. G. and Hart, G. W. (1989). Glycosylation of chromosomal proteins: localization of O-linked N-acetylglucosamine in Drosophila chromatin. Cell 57, 243-251.
    • (1989) Cell , vol.57 , pp. 243-251
    • Kelly, W.G.1    Hart, G.W.2
  • 19
    • 0030959555 scopus 로고    scopus 로고
    • Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats
    • Kreppel, L. K., Blomberg, M. A. and Hart, G. W. (1997). Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats. J. Biol. Chem. 272, 9308-9315.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9308-9315
    • Kreppel, L.K.1    Blomberg, M.A.2    Hart, G.W.3
  • 20
    • 0034646330 scopus 로고    scopus 로고
    • Glucose stimulates protein modification by O-linked GlcNAc in pancreatic beta cells: Linkage of O-linked GlcNAc to beta cell death
    • Liu, K., Paterson, A. J., Chin, E. and Kudlow, J. E. (2000). Glucose stimulates protein modification by O-linked GlcNAc in pancreatic beta cells: linkage of O-linked GlcNAc to beta cell death. Proc. Natl. Acad. Sci. USA 97, 2820-2825.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2820-2825
    • Liu, K.1    Paterson, A.J.2    Chin, E.3    Kudlow, J.E.4
  • 21
    • 0032169412 scopus 로고    scopus 로고
    • Reconstitution of HIV-1 rev nuclear export: Independent requirements for nuclear import and export
    • Love, D. C., Sweitzer, T. D. and Hanover, J. A. (1998). Reconstitution of HIV-1 rev nuclear export: independent requirements for nuclear import and export. Proc. Natl. Acad. Sci. USA 95, 10608-10613.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10608-10613
    • Love, D.C.1    Sweitzer, T.D.2    Hanover, J.A.3
  • 22
    • 0030944105 scopus 로고    scopus 로고
    • O-linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats
    • Lubas, W. A., Frank, D. W., Krause, M. and Hanover, J. A. (1997). O-linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats. J. Biol. Chem. 272, 9316-9324.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9316-9324
    • Lubas, W.A.1    Frank, D.W.2    Krause, M.3    Hanover, J.A.4
  • 23
    • 0034646669 scopus 로고    scopus 로고
    • Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity
    • Lubas, W. A. and Hanover, J. A. (2000). Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity. J. Biol. Chem. 275, 10983-10988.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10983-10988
    • Lubas, W.A.1    Hanover, J.A.2
  • 24
    • 0028916742 scopus 로고
    • Analysis of nuclear pore protein p62 glycosylation
    • Lubas, W. A., Smith, M., Starr, C. M. and Hanover, J. A. (1995). Analysis of nuclear pore protein p62 glycosylation. Biochemistry 34, 1686-1694.
    • (1995) Biochemistry , vol.34 , pp. 1686-1694
    • Lubas, W.A.1    Smith, M.2    Starr, C.M.3    Hanover, J.A.4
  • 25
    • 0034956729 scopus 로고    scopus 로고
    • Subcellular distribution, calmodulin interaction, and mitochondrial association of the hyaluronan-binding protein RHAMM in rat brain
    • Lynn, B. D., Turley, E. A. and Nagy, J. I. (2001). Subcellular distribution, calmodulin interaction, and mitochondrial association of the hyaluronan-binding protein RHAMM in rat brain. J. Neurosci. Res. 65, 6-16.
    • (2001) J. Neurosci. Res. , vol.65 , pp. 6-16
    • Lynn, B.D.1    Turley, E.A.2    Nagy, J.I.3
  • 26
    • 0025855139 scopus 로고
    • Discovery of a metabolic pathway mediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resistance
    • Marshall, S., Bacote, V. and Traxinger, R. R. (1991). Discovery of a metabolic pathway mediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resistance. J. Biol. Chem. 266, 4706-4712.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4706-4712
    • Marshall, S.1    Bacote, V.2    Traxinger, R.R.3
  • 29
    • 0036134476 scopus 로고    scopus 로고
    • Human O-GlcNAc transferase (OGT): Genomic structure, analysis of splice variants, fine mapping in Xq13.1
    • Nolte, D. and Muller, U. (2002). Human O-GlcNAc transferase (OGT): genomic structure, analysis of splice variants, fine mapping in Xq13.1. Mamm. Genome 13, 62-64.
    • (2002) Mamm. Genome , vol.13 , pp. 62-64
    • Nolte, D.1    Muller, U.2
  • 31
    • 0028802599 scopus 로고
    • The yeast tribrid system-genetic detection of trans-phosphorylated ITAM-SH2-interactions
    • Osborne, M. A., Dalton, S. and Kochan, J. P. (1995). The yeast tribrid system-genetic detection of trans-phosphorylated ITAM-SH2-interactions. Biotechnology (NY) 13, 1474-1478.
    • (1995) Biotechnology (NY) , vol.13 , pp. 1474-1478
    • Osborne, M.A.1    Dalton, S.2    Kochan, J.P.3
  • 32
    • 0034630719 scopus 로고    scopus 로고
    • Structure of O-linked GlcNAc transferase: Mediator of glycan-dependent signaling
    • Roos, M. D. and Hanover, J. A. (2000). Structure of O-linked GlcNAc transferase: mediator of glycan-dependent signaling. Biochem. Biophys. Res. Commun. 271, 275-280.
    • (2000) Biochem. Biophys. Res. Commun. , vol.271 , pp. 275-280
    • Roos, M.D.1    Hanover, J.A.2
  • 33
    • 0034705030 scopus 로고    scopus 로고
    • The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny
    • Shafi, R., Iyer, S. P., Ellies, L. G., O'Donnell, N., Marek, K. W., Chui, D., Hart, G. W. and Marth, J. D. (2000). The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny. Proc. Natl. Acad. Sci. USA 97, 5735-5739.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5735-5739
    • Shafi, R.1    Iyer, S.P.2    Ellies, L.G.3    O'Donnell, N.4    Marek, K.W.5    Chui, D.6    Hart, G.W.7    Marth, J.D.8
  • 34
    • 0025231304 scopus 로고
    • Glycosylation of nuclear pore protein p62. Reticulocyte lysate catalyzes O-linked N-acetylglucosamine addition in vitro
    • Starr, C. M. and Hanover, J. A. (1990). Glycosylation of nuclear pore protein p62. Reticulocyte lysate catalyzes O-linked N-acetylglucosamine addition in vitro. J. Biol. Chem. 265, 6868-6873.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6868-6873
    • Starr, C.M.1    Hanover, J.A.2
  • 35
    • 0033865106 scopus 로고    scopus 로고
    • Transgenic mice with increased hexosamine flux specifically targeted to beta-cells exhibit hyperinsulinemia and peripheral insulin resistance
    • Tang, J., Neidigh, J. L., Cooksey, R. C. and McClain, D. A. (2000). Transgenic mice with increased hexosamine flux specifically targeted to beta-cells exhibit hyperinsulinemia and peripheral insulin resistance. Diabetes 49, 1492-1499.
    • (2000) Diabetes , vol.49 , pp. 1492-1499
    • Tang, J.1    Neidigh, J.L.2    Cooksey, R.C.3    McClain, D.A.4
  • 36
    • 0025781289 scopus 로고
    • Coordinated regulation of glutamine: Fructose-6-phosphate amidotransferase activity by insulin, glucose, and glutamine. Role of hexosamine biosynthesis in enzyme regulation
    • Traxinger, R. R. and Marshall, S. (1991). Coordinated regulation of glutamine:fructose-6-phosphate amidotransferase activity by insulin, glucose, and glutamine. Role of hexosamine biosynthesis in enzyme regulation. J. Biol. Chem. 266, 10148-10154.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10148-10154
    • Traxinger, R.R.1    Marshall, S.2
  • 37
    • 0026713285 scopus 로고
    • Insulin regulation of pyruvate kinase activity in isolated adipocytes. Crucial role of glucose and the hexosamine biosynthesis pathway in the expression of insulin action
    • Traxinger, R. R. and Marshall, S. (1992). Insulin regulation of pyruvate kinase activity in isolated adipocytes. Crucial role of glucose and the hexosamine biosynthesis pathway in the expression of insulin action. J. Biol. Chem. 267, 9718-9723.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9718-9723
    • Traxinger, R.R.1    Marshall, S.2
  • 38
    • 0033664020 scopus 로고    scopus 로고
    • Overexpression of glutamine: Fructose-6-phosphate amidotransferase in the liver of transgenic mice results in enhanced glycogen storage, hyperlipidemia, obesity, and impaired glucose tolerance
    • Veerababu, G., Tang, J., Hoffman, R. T., Daniels, M. C., Hebert, L. F. J., Crook, E. D., Cooksey, R. C. and McClain, D. A. (2000). Overexpression of glutamine: fructose-6-phosphate amidotransferase in the liver of transgenic mice results in enhanced glycogen storage, hyperlipidemia, obesity, and impaired glucose tolerance. Diabetes 49, 2070-2078.
    • (2000) Diabetes , vol.49 , pp. 2070-2078
    • Veerababu, G.1    Tang, J.2    Hoffman, R.T.3    Daniels, M.C.4    Hebert, L.F.J.5    Crook, E.D.6    Cooksey, R.C.7    McClain, D.A.8
  • 39
    • 0035937586 scopus 로고    scopus 로고
    • Glycosylation of nucleocytoplasmic proteins: Signal transduction and O-GlcNAc
    • Wells, L., Vosseller, K. and Hart, G. W. (2001). Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc. Science 291, 2376-2378.
    • (2001) Science , vol.291 , pp. 2376-2378
    • Wells, L.1    Vosseller, K.2    Hart, G.W.3
  • 40
    • 0035976715 scopus 로고    scopus 로고
    • Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily
    • Wrabl, J. O. and Grishin, N. V. (2001). Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily. J. Mol. Biol. 314, 365-374.
    • (2001) J. Mol. Biol. , vol.314 , pp. 365-374
    • Wrabl, J.O.1    Grishin, N.V.2
  • 41
    • 0037067659 scopus 로고    scopus 로고
    • Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: Coupling protein O-GlcNAcylation to transcriptional repression
    • Yang, X., Zhang, F. and Kudlow, J. E. (2002). Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression. Cell 110, 69-80.
    • (2002) Cell , vol.110 , pp. 69-80
    • Yang, X.1    Zhang, F.2    Kudlow, J.E.3
  • 42
    • 0035811072 scopus 로고    scopus 로고
    • O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability
    • Yang, X., Su, K., Roos, M. D., Chang, Q., Paterson, A. J. and Kudlow, J. E. (2001). O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability. Proc. Natl. Acad. Sci. USA 98, 6611-6616.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6611-6616
    • Yang, X.1    Su, K.2    Roos, M.D.3    Chang, Q.4    Paterson, A.J.5    Kudlow, J.E.6


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