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Volumn 5, Issue 2, 2006, Pages 313-323

Identification of the major site of O-linked β-N-acetylglucosamine modification in the C terminus of insulin receptor substrate-1

Author keywords

[No Author keywords available]

Indexed keywords

BETA N ACETYLGLUCOSAMINE; GLUCOSE; INSULIN; INSULIN RECEPTOR SUBSTRATE 1; MONOSACCHARIDE; N ACETYL BETA GLUCOSAMINIDASE; SERINE; THREONINE; UNCLASSIFIED DRUG;

EID: 33644698706     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M500314-MCP200     Document Type: Article
Times cited : (79)

References (41)
  • 1
    • 0030943923 scopus 로고    scopus 로고
    • Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins
    • Hart, G. W. (1997) Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins. Annu. Rev. Biochem. 66, 315-335
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 315-335
    • Hart, G.W.1
  • 2
    • 0035800086 scopus 로고    scopus 로고
    • Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II
    • Comer, F. I., and Hart, G. W. (2001) Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II. Biochemistry 40, 7845-7852
    • (2001) Biochemistry , vol.40 , pp. 7845-7852
    • Comer, F.I.1    Hart, G.W.2
  • 3
    • 0141884304 scopus 로고    scopus 로고
    • Dynamic interplay between O-GlcNAc and O-phosphate: The sweet side of protein regulation
    • Slawson, C., and Hart, G. W. (2003) Dynamic interplay between O-GlcNAc and O-phosphate: the sweet side of protein regulation. Curr. Opin. Struct. Biol. 13, 631-636
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 631-636
    • Slawson, C.1    Hart, G.W.2
  • 4
    • 0037432341 scopus 로고    scopus 로고
    • Dynamic nuclear and cytoplasmic glycosylation: Enzymes of O-GlcNAc cycling
    • Iyer, S. P., and Hart, G. W. (2003) Dynamic nuclear and cytoplasmic glycosylation: enzymes of O-GlcNAc cycling. Biochemistry 42, 2493-2499
    • (2003) Biochemistry , vol.42 , pp. 2493-2499
    • Iyer, S.P.1    Hart, G.W.2
  • 5
    • 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. U. S. A. 97, 5735-5739
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , 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
  • 6
    • 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
  • 7
    • 0036181947 scopus 로고    scopus 로고
    • Hexosamines as mediators of nutrient sensing and regulation in diabetes
    • McClain, D. A. (2002) Hexosamines as mediators of nutrient sensing and regulation in diabetes. J. Diabetes Complicat. 16, 72-80
    • (2002) J. Diabetes Complicat. , vol.16 , pp. 72-80
    • McClain, D.A.1
  • 8
    • 24744457321 scopus 로고    scopus 로고
    • O-Glycosylation of the tail domain of neurofilament protein M in human neurons and in spinal cord tissue of a rat model of amyotrophic lateral sclerosis (ALS)
    • Ludemann, N., Clement, A., Hans, V. H., Leschik, J., Behl, C., and Brandt, R. (2005) O-Glycosylation of the tail domain of neurofilament protein M in human neurons and in spinal cord tissue of a rat model of amyotrophic lateral sclerosis (ALS). J. Biol. Chem. 280, 31648-31658
    • (2005) J. Biol. Chem. , vol.280 , pp. 31648-31658
    • Ludemann, N.1    Clement, A.2    Hans, V.H.3    Leschik, J.4    Behl, C.5    Brandt, R.6
  • 9
    • 19044377730 scopus 로고    scopus 로고
    • Adenovirus-mediated overexpression of O-GlcNAcase improves contractile function in the diabetic heart
    • Hu, Y., Belke, D., Suarez, J., Swanson, E., Clark, R., Hoshijima, M., and Dillmann, W. H. (2005) Adenovirus-mediated overexpression of O-GlcNAcase improves contractile function in the diabetic heart. Circ. Res. 96, 1006-1013
    • (2005) Circ. Res. , vol.96 , pp. 1006-1013
    • Hu, Y.1    Belke, D.2    Suarez, J.3    Swanson, E.4    Clark, R.5    Hoshijima, M.6    Dillmann, W.H.7
  • 10
    • 3242739968 scopus 로고    scopus 로고
    • O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease
    • Liu, F., Iqbal, K., Grundke-Iqbal, I., Hart, G. W., and Gong, C. X. (2004) O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer's disease. Proc. Natl. Acad. Sci. U. S. A. 101, 10804-10809
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 10804-10809
    • Liu, F.1    Iqbal, K.2    Grundke-Iqbal, I.3    Hart, G.W.4    Gong, C.X.5
  • 11
    • 0037117511 scopus 로고    scopus 로고
    • Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes
    • Vosseller, K., Wells, L., Lane, M. D., and Hart, G. W. (2002) Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes. Proc. Natl. Acad. Sci. U. S. A. 99, 5313-5318
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 5313-5318
    • Vosseller, K.1    Wells, L.2    Lane, M.D.3    Hart, G.W.4
  • 12
    • 0037162342 scopus 로고    scopus 로고
    • Insulin-dependent activation of endothelial nitric oxide synthase is impaired by O-linked glycosylation modification of signaling proteins in human coronary endotheliall cells
    • Federici, M., Menghini, R., Mauriello, A., Hribal, M. L., Ferrelli, F., Lauro, D., Sbraccia, P., Spagnoli, L. G., Sesti G., and Lauro, R. (2002) Insulin-dependent activation of endothelial nitric oxide synthase is impaired by O-linked glycosylation modification of signaling proteins in human coronary endotheliall cells. Circulation 106, 466-472
    • (2002) Circulation , vol.106 , pp. 466-472
    • Federici, M.1    Menghini, R.2    Mauriello, A.3    Hribal, M.L.4    Ferrelli, F.5    Lauro, D.6    Sbraccia, P.7    Spagnoli, L.G.8    Sesti, G.9    Lauro, R.10
  • 13
    • 0344298921 scopus 로고    scopus 로고
    • Activation of the hexosamine pathway by glucosamine in vivo induces insulin resistance of early postreceptor insulin signaling events in skeletal muscle
    • Patti, M. E., Virkamaki, A., Landaker, E. J., Kahn, C. R., and Yki-Jarvinen, H. (1999) Activation of the hexosamine pathway by glucosamine in vivo induces insulin resistance of early postreceptor insulin signaling events in skeletal muscle. Diabetes 48, 1562-1571
    • (1999) Diabetes , vol.48 , pp. 1562-1571
    • Patti, M.E.1    Virkamaki, A.2    Landaker, E.J.3    Kahn, C.R.4    Yki-Jarvinen, H.5
  • 14
    • 0036710280 scopus 로고    scopus 로고
    • IRS proteins and the common path to diabetes
    • White, M. F. (2002) IRS proteins and the common path to diabetes. Am. J. Physiol. 283, E413-E422
    • (2002) Am. J. Physiol. , vol.283
    • White, M.F.1
  • 15
    • 14544271905 scopus 로고    scopus 로고
    • Positive and negative regulation of insulin signaling through IRS-1 phosphorylation
    • Gual, P., Le Marchand-Brustel, Y., and Tanti, J. F. (2005) Positive and negative regulation of insulin signaling through IRS-1 phosphorylation. Biochimie (Paris) 87, 99-109
    • (2005) Biochimie (Paris) , vol.87 , pp. 99-109
    • Gual, P.1    Le Marchand-Brustel, Y.2    Tanti, J.F.3
  • 16
    • 0034329621 scopus 로고    scopus 로고
    • Simultaneous detection and identification of O-GlcNAc-modified glycoproteins using liquid chromatography-tandem mass spectrometry
    • Haynes, P.A., and Aebersold, R. (2000) Simultaneous detection and identification of O-GlcNAc-modified glycoproteins using liquid chromatography-tandem mass spectrometry. Anal. Chem. 72, 5402-5410
    • (2000) Anal. Chem. , vol.72 , pp. 5402-5410
    • Haynes, P.A.1    Aebersold, R.2
  • 17
    • 0344870025 scopus 로고    scopus 로고
    • Identification of novel sites of O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry
    • Chalkley, R. J., and Burlingame, A. L. (2003) Identification of novel sites of O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry. Mol. Cell. Proteomics 2, 182-190
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 182-190
    • Chalkley, R.J.1    Burlingame, A.L.2
  • 18
    • 0030025149 scopus 로고    scopus 로고
    • Selective detection and site-analysis of O-GIc-NAc-modified glycopeptides by β-elimination and tandem electrospray mass spectrometry
    • Greis, K. D., Hayes, B. K., Comer, F. I., Kirk, M., Barnes, S., Lowary, T. L., and Hart, G. W. (1996) Selective detection and site-analysis of O-GIc-NAc-modified glycopeptides by β-elimination and tandem electrospray mass spectrometry. Anal. Biochem. 234, 38-49
    • (1996) Anal. Biochem. , vol.234 , pp. 38-49
    • Greis, K.D.1    Hayes, B.K.2    Comer, F.I.3    Kirk, M.4    Barnes, S.5    Lowary, T.L.6    Hart, G.W.7
  • 19
    • 26844489700 scopus 로고    scopus 로고
    • Methods for the detection of paxillin post-translational modifications and interacting proteins by mass spectrometry
    • Schroeder, J., Webb, D. J., Shabanowitz, J., Horwitz A. F., and Hunt, D. F. (2005) Methods for the detection of paxillin post-translational modifications and interacting proteins by mass spectrometry. J. Proteome Res. 4, 1832-1841
    • (2005) J. Proteome Res. , vol.4 , pp. 1832-1841
    • Schroeder, J.1    Webb, D.J.2    Shabanowitz, J.3    Horwitz, A.F.4    Hunt, D.F.5
  • 20
    • 0037709390 scopus 로고    scopus 로고
    • The transcription factor PDX-1 is post-translationally modified by O-linked N-acetylglucosamine and this modification is correlated with its DNA binding activity and insulin secretion in min6 beta-cells
    • Gao, Y., Miyazaki, J., and Hart, G. W. (2003) The transcription factor PDX-1 is post-translationally modified by O-linked N-acetylglucosamine and this modification is correlated with its DNA binding activity and insulin secretion in min6 beta-cells. Arch. Biochem. Biophys. 415, 155-163
    • (2003) Arch. Biochem. Biophys. , vol.415 , pp. 155-163
    • Gao, Y.1    Miyazaki, J.2    Hart, G.W.3
  • 21
    • 0001607910 scopus 로고    scopus 로고
    • Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications
    • Wells, L., Vosseller, K., Cole, R. N., Cronshaw, J. M., Matunis, M. J., and Hart, G. W. (2002) Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications. Mol. Cell. Proteomics 1, 791-804
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 791-804
    • Wells, L.1    Vosseller, K.2    Cole, R.N.3    Cronshaw, J.M.4    Matunis, M.J.5    Hart, G.W.6
  • 22
    • 0028346557 scopus 로고
    • Detection of O-linked N-acetylglucosamine (O-GlcNAc) on cytoplasmic and nuclear proteins
    • Roquemore, E. P., Chou, T. Y., and Hart, G. W. (1994) Detection of O-linked N-acetylglucosamine (O-GlcNAc) on cytoplasmic and nuclear proteins. Methods Enzymol. 230, 443-460
    • (1994) Methods Enzymol. , vol.230 , pp. 443-460
    • Roquemore, E.P.1    Chou, T.Y.2    Hart, G.W.3
  • 24
    • 4444337997 scopus 로고    scopus 로고
    • Exploring the O-GlcNAc proteome: Direct identification of O-GlcNAc-modified proteins from the brain
    • Khidekel, N., Ficarro, S. B., Peters, E. C., and Hsieh-Wilson, L. C. (2004) Exploring the O-GlcNAc proteome: direct identification of O-GlcNAc-modified proteins from the brain. Proc. Natl. Acad. Sci. U. S. A. 101, 13132-13137
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 13132-13137
    • Khidekel, N.1    Ficarro, S.B.2    Peters, E.C.3    Hsieh-Wilson, L.C.4
  • 27
    • 0035866603 scopus 로고    scopus 로고
    • Mass spectrometric determination of O-glycosylation sites using β-elimination and partial acid hydrolysis
    • Mirgorodskaya, E., Hassan, H., Clausen, H., and Roepstorff, P. (2001) Mass spectrometric determination of O-glycosylation sites using β-elimination and partial acid hydrolysis. Anal. Chem. 73, 1263-1269
    • (2001) Anal. Chem. , vol.73 , pp. 1263-1269
    • Mirgorodskaya, E.1    Hassan, H.2    Clausen, H.3    Roepstorff, P.4
  • 29
    • 0032488979 scopus 로고    scopus 로고
    • Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-β-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate
    • Haltiwanger, R. S., Grove, K., and Philipsberg, G. A. (1998) Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-β-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate. J. Biol. Chem. 273, 3611-3617
    • (1998) J. Biol. Chem. , vol.273 , pp. 3611-3617
    • Haltiwanger, R.S.1    Grove, K.2    Philipsberg, G.A.3
  • 30
    • 0348014634 scopus 로고    scopus 로고
    • Improved β-elimination-based affinity purification strategy for enrichment of phosphopeptides
    • McLachlin, D. T., and Chait, B. T. (2003) Improved β-elimination-based affinity purification strategy for enrichment of phosphopeptides. Anal. Chem. 75, 6826-6836
    • (2003) Anal. Chem. , vol.75 , pp. 6826-6836
    • McLachlin, D.T.1    Chait, B.T.2
  • 31
    • 0000857494 scopus 로고
    • An approach to correlated tandem mass spectral data of peptides with a sequence in a protein database
    • Eng, J., McCormack, A. L., and Yates, J. R. (1994) An approach to correlated tandem mass spectral data of peptides with a sequence in a protein database. J. Am. Soc. Mass Spectrom. 5, 976-989
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.1    McCormack, A.L.2    Yates, J.R.3
  • 32
    • 0029688766 scopus 로고    scopus 로고
    • Sherpa: A Macintosh-based expert system for the interpretation of electrospray ionization LC/MS and MS/MS data from protein digests
    • Taylor, J. A., Walsh, K. A., and Johnson, R. S. (1996) Sherpa: a Macintosh-based expert system for the interpretation of electrospray ionization LC/MS and MS/MS data from protein digests. Rapid Commun. Mass Spectrom. 10, 679-687
    • (1996) Rapid Commun. Mass Spectrom. , vol.10 , pp. 679-687
    • Taylor, J.A.1    Walsh, K.A.2    Johnson, R.S.3
  • 34
    • 0035876021 scopus 로고    scopus 로고
    • Characterization of a mouse monoclonal antibody specific for O-linked N-acetylglucosamine
    • Comer, F. I., Vosseller K., Wells, L., Accavitti, M. A., and Hart, G. W. (2001) Characterization of a mouse monoclonal antibody specific for O-linked N-acetylglucosamine. Anal. Biochem. 293, 169-177
    • (2001) Anal. Biochem. , vol.293 , pp. 169-177
    • Comer, F.I.1    Vosseller, K.2    Wells, L.3    Accavitti, M.A.4    Hart, G.W.5
  • 35
    • 24944576051 scopus 로고    scopus 로고
    • Identification of IRS-1 serine/threonine phosphorylation sites using mass spectrometry analysis: Regulatory role of serine 1223
    • Luo, M., Reyna, S., Wang, L., Yi, Z., Carroll, C., Dong, L. Q., Langlais, P., Weintraub, S. T., and Mandarino, L. J. (2005) Identification of IRS-1 serine/threonine phosphorylation sites using mass spectrometry analysis: regulatory role of serine 1223. Endocrinology 146, 4410-4416
    • (2005) Endocrinology , vol.146 , pp. 4410-4416
    • Luo, M.1    Reyna, S.2    Wang, L.3    Yi, Z.4    Carroll, C.5    Dong, L.Q.6    Langlais, P.7    Weintraub, S.T.8    Mandarino, L.J.9
  • 36
    • 13844313887 scopus 로고    scopus 로고
    • Quantitative analysis of both protein expression and serine/threonine post-translational modifications through stable isotope labeling with dithiothreitol
    • Vosseller, K., Hansen, K. C., Chalkley, R. J., Trinidad, J. C., Wells, L., Hart, G. W., and Burlingame, A. L. (2005) Quantitative analysis of both protein expression and serine/threonine post-translational modifications through stable isotope labeling with dithiothreitol. Proteomics 5, 388-398
    • (2005) Proteomics , vol.5 , pp. 388-398
    • Vosseller, K.1    Hansen, K.C.2    Chalkley, R.J.3    Trinidad, J.C.4    Wells, L.5    Hart, G.W.6    Burlingame, A.L.7
  • 37
    • 15644368839 scopus 로고    scopus 로고
    • The COOH-terminal tyrosine phosphorylation sites on IRS-1 bind SHP-2 and negatively regulate insulin signaling
    • Myers, M. G., Jr., Mendez, R., Shi, P., Pierce, J. H., Rhoads, R., and White, M. F. (1998) The COOH-terminal tyrosine phosphorylation sites on IRS-1 bind SHP-2 and negatively regulate insulin signaling. J. Biol. Chem. 273, 26908-26914
    • (1998) J. Biol. Chem. , vol.273 , pp. 26908-26914
    • Myers Jr., M.G.1    Mendez, R.2    Shi, P.3    Pierce, J.H.4    Rhoads, R.5    White, M.F.6
  • 39
    • 1542284652 scopus 로고    scopus 로고
    • Modulation of human insulin receptor substrate-1 tyrosine phosphorylation by protein kinase Cδ
    • Greene, M. W., Morrice, N., Garofalo, R. S., and Roth, R. A. (2004) Modulation of human insulin receptor substrate-1 tyrosine phosphorylation by protein kinase Cδ. Biochem. J. 378, 105-116
    • (2004) Biochem. J. , vol.378 , pp. 105-116
    • Greene, M.W.1    Morrice, N.2    Garofalo, R.S.3    Roth, R.A.4
  • 40
    • 15844389443 scopus 로고    scopus 로고
    • Phosphorylation of insulin receptor substrate-1 on multiple serine residues, 612, 632, 662, and 731, modulates insulin action
    • Mothe, I., and Van Obberghen, E. (1996) Phosphorylation of insulin receptor substrate-1 on multiple serine residues, 612, 632, 662, and 731, modulates insulin action. J. Biol. Chem. 271, 11222-11227
    • (1996) J. Biol. Chem. , vol.271 , pp. 11222-11227
    • Mothe, I.1    Van Obberghen, E.2


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