Protein O-GlcNAcylation in diabetes and diabetic complications

References

• IDF Diabetes Atlas (5th Edition). International Diabetes Federation, Brussels, Belgium (2012).
   Google Scholar
• Whiting DR, Guariguata L, Weil C, Shaw, J. IDF diabetes atlas: global estimates of the prevalence of diabetes for 2011 and 2030. Diabetes Res. Clin. Pract. 94, 311–321 (2011).
   PubMed Web of Science ®Google Scholar
• Daneman D. Type 1 diabetes. Lancet 367, 847–858 (2006).
   PubMed Web of Science ®Google Scholar
• Stumvoll M, Goldstein BJ, Haeften TW van, Type 2 diabetes: principles of pathogenesis and therapy. Lancet 365, 1333–1346 (2005).
   PubMed Web of Science ®Google Scholar
• DeFronzo RA. The triumvirate: (-cell muscle, liver: a collusion) responsible for NIDDM. Diabetes 37, 677–687 (1988).
   Google Scholar
• Rossetti L, Giaccari A, DeFronzo RA. Glucose toxicity. Diabetes Care 13, 610–630 (1990).
   PubMed Web of Science ®Google Scholar
• Robertson RP, Harmon J, Tran PO et al. Glucose toxicity in beta-cells: Type 2 diabetes, good radicals gone bad, and the glutathione connection. Diabetes 52, 581–587 (2003).
   PubMed Web of Science ®Google Scholar
• Rossetti L, Smith D, Shulman GI et al. Correction of hyperglycemia with phlorizin normalizes tissue sensitivity to insulin in diabetic rats. J. Clin. Invest. 79, 1510–1515 (1987).
   PubMed Web of Science ®Google Scholar
• Garvey WT, Olefsky JM, Matthaei S et al. Glucose and insulin co-regulate the glucose transport system in primary cultured adipocytes. J. Biol. Chem. 262, 189–197 (1987).
   Google Scholar
• Brownlee M. Biochemistry and molecular cell biology of diabetic complications. Nature 414, 813–820 (2001).
   PubMed Web of Science ®Google Scholar
• Brownlee M. The pathobiology of diabetic complications: a unifying mechanism. Diabetes 54, 1615–1625 (2005).
   PubMed Web of Science ®Google Scholar
• Torres CR, Hart GW. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. J. Biol. Chem. 259, 3308–3317 (1984).
   PubMed Web of Science ®Google Scholar
• Holt GD, Hart GW. 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).
   PubMed Web of Science ®Google Scholar
• Hart GW, Slawson C, Ramirez Correa GA et al. Cross talk between GlcNAcylation and phosphorylation: Roles in signaling, transcription, and chronic disease. Annu. Rev. Biochem. 80, 825–858 (2011).
   PubMed Web of Science ®Google Scholar
• Bond MB, Hanover JA. O-GlcNAc Cycling: A link between metabolism and chronic disease. Annu. Rev. Nutr. 33, 13.1–13.25 (2013).
   Google Scholar
• Marshall S, Bacote V, Traxinger RR. 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).
   PubMed Web of Science ®Google Scholar
• Haltiwanger RS, Holt, GD, Hart GW. Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine: peptide beta-N-acetyl-glucosaminyltransferase. J. Biol. Chem. 265, 2563–2568 (1990).
   PubMed Web of Science ®Google Scholar
• Buse MG. Hexosamines, insulin resistance, and the complications of diabetes: current status. Am. J. Physiol. Endocrinol. Metab. 290, E1–E8 (2006).
   PubMed Web of Science ®Google Scholar
• Dias WB, Hart GW. O-GlcNAc modification in diabetes and Alzheimer’s disease. Mol. Biosyst. 3, 766–772 (2007).
   PubMed Web of Science ®Google Scholar
• Copeland RJ, Bullen JW, Hart GW. Cross-talk between GlcNAcylation and phosphorylation: roles in insulin resistance and glucose toxicity. Am. J. Physiol. Endocrinol. Metab. 295, E17–E28 (2008).
   PubMed Web of Science ®Google Scholar
• Slawson C, Copeland RJ, Hart GW. O-GlcNAc signaling: a metabolic link between diabetes and cancer? Trends Biochem. Sci. 35, 547–555 (2010).
   PubMed Web of Science ®Google Scholar
• Konrad RJ, Zhang FX, Hale JE et al. Alloxan is an inhibitor of the enzyme O-linked N-acetylglucosamine transferase. Biochem. Biophys. Res. Commun. 293, 207–212 (2002).
   PubMed Web of Science ®Google Scholar
• Kang E-S, Han D, Park J et al. O-GlcNAc modulation at Akt1 Ser473 correlates with apoptosis of murine pancreatic beta cells. Exp. Cell Res. 314, 2238–2248 (2008).
   Google Scholar
• Dorfmueller HC, Borodkin VS, Blair DE et al. Substrate and product analogues as human O-GlcNAc transferase inhibitors. Amino Acids. 40, 781–792 (2011).
   PubMed Web of Science ®Google Scholar
• Gloster TM, Zandberg WF, Heinonen JE et al. Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells. Nat. Chem. Biol. 7, 174–181 (2011).
   PubMed Web of Science ®Google Scholar
• Haltiwanger RS, Grove K, Philipsberg GA. Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-d-gluco-pyranosylidene)amino-N-phenylcarbamate. J. Biol. Chem. 273, 3611–3617 (1998).
   PubMed Web of Science ®Google Scholar
• Macauley MS, Bubb AK, Martinez-Fleites C et al. Elevation of global O-GlcNAc levels in 3T3-L1 adipocytes by selective inhibition of O-GlcNAcase does not induce insulin resistance. J. Biol. Chem. 283, 34687–34695 (2008).
   Google Scholar
• Yuzwa SA, Macauley MS, Heinonen JE et al. A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phos-phorylation of tau in vivo. Nat. Chem. Biol. 4, 483–490 (2008).
   PubMed Web of Science ®Google Scholar
• Andres-Bergos J, Tardio L, Larranaga-Vera A et al. The increase in O-linked N-acetylglucosamine protein modification stimulates chondrogenic differentiation both in vitro and in vivo. J. Biol. Chem. 287, 33615–33628 (2012).
   Google Scholar
• Macauley MS, He Y, Gloster TM et al. Inhibition of O-GlcNAcase using a potent and cell-permeable inhibitor does not induce insulin resistance in 3T3-L1 adipocytes. Chem. Biol. 17, 937–948 (2010).
   Google Scholar
• Macauley MS, Shan X, Yuzwa SA et al. Elevation of global O-GlcNAc in rodents using a selective O-GlcNAcase inhibitor does not cause insulin resistance or perturb glucohomeostasis. Chem. Biol. 17, 949–958 (2010).
   PubMed Web of Science ®Google Scholar
• Dorfmueller HC, Borodkin VS, Schimpl M et al. Cell-penetrant, nanomolar O-GlcNAcase inhibitors selective against lysosomal hexosaminidases. Chem. Biol. 17, 1250–1255 (2010).
   Google Scholar
• Reed MJ, Meszaros K, Entes LJ et al. A new rat model of Type 2 diabetes: The fat-fed, streptozotocin-treated rat. Metabolism 49, 1390–1394 (2000).
   PubMed Web of Science ®Google Scholar
• Roos MD, Xie W, Su K et al. Streptozotocin, an analog of N-acetylglucosamine, blocks the removal of O-GlcNAc from intracellular proteins. Proc. Assoc. Am. Physicians. 110, 422–432 (1998).
   PubMedGoogle Scholar
• O’Donnell N, Zachara NE, Hart GW et al. Ogt-dependent X-chromosome-linked protein glycosylation is a requisite modifi-cation in somatic cell function and embryo viability. Mol. Cell Biol. 24, 1680–1690 (2004).
   PubMedGoogle Scholar
• Watson LJ, Facundo HT, Ngoh GA et al. O-linked β-N-acetyl-glucosamine transferase is indispensable in the failing heart. Proc. Natl Acad. Sci. USA 107, 17797–17802 (2010).
   PubMed Web of Science ®Google Scholar
• Hanover JA, Forsythe ME, Hennessey PT et al. A Caenorhabditis elegans model of insulin resistance: altered macronutrient storage and dauer formation in an OGT-1 knockout. Proc. Natl Acad. Sci . USA 102, 11266–11271 (2005).
   PubMedGoogle Scholar
• Mondoux MA, Love DC, Ghosh SK et al. O-Linked-N-Acetylglucosamine cycling and insulin signaling are required for the glucose stress response in Caenorhabditis elegans. Genetics 188, 369–382 (2011).
   Google Scholar
• Sinclair DAR, Syrzycka M, Macauley MS et al. Drosophila O-GlcNAc transferase (OGT) is encoded by the Polycomb group (PcG) gene, super sex combs (sxc). Proc. Natl Acad. Sci. USA 106, 13427–13432 (2009).
   PubMedGoogle Scholar
• Sekine O, Love DC, Rubenstein DS et al. Blocking O-linked GlcNAc cycling in Drosophila insulin-producing cells perturbs glucose-insulin homeostasis. J. Biol. Chem. 285, 38684–38691 (2010).
   Google Scholar
• Oki T, Yamazaki K, Kuromitsu J et al. cDNA cloning and mapping of a novel subtype of glutamine:fructose-6-phosphate amido-transferase (GFAT2) in human and mouse. Genomics 57, 227–234 (1999).
   PubMed Web of Science ®Google Scholar
• DeHaven JE, Robinson KA, Nelson BA et al. A novel variant of glutamine: fructose-6-phosphate amidotransferase-1 (GFAT1) mRNA is selectively expressed in striated muscle. Diabetes 50, 2419–2424 (2001).
   PubMed Web of Science ®Google Scholar
• Zhou J, Huynh QK, Hoffman RT et al. Regulation of glutamine:fructose-6-phosphate amidotransferase by cAMP-dependent protein kinase. Diabetes 47, 1836–1840 (1998).
   Google Scholar
• Chang Q, Su K, Baker JR et al. Phosphorylation of human glutamine:fructose-6-phosphate amidotransferase by cAMP-dependent protein kinase at serine 205 blocks the enzyme activity. J. Biol. Chem. 275, 21981–21987 (2000).
   PubMed Web of Science ®Google Scholar
• Li Y, Roux C, Lazereg S et al. Identification of a novel serine phosphorylation site in human glutamine:fructose-6-phosphate amidotransferase isoform 1. Biochemistry 46, 13163–13169 (2007).
   Google Scholar
• Broschat KO, Gorka C, Page JD et al. Kinetic characterization of human glutamine-fructose-6-phosphate amidotransferase I: potent feedback inhibition by glucosamine 6-phosphate. J. Biol. Chem. 277, 14764–14770 (2002).
   PubMed Web of Science ®Google Scholar
• Kornfeld R. Studies on L-glutamine D-fructose 6-phosphate amidotransferase. I. Feedback inhibition by uridine diphosphate-N-acetylglucosamine. J. Biol. Chem. 242, 3135–3141 (1967).
   PubMed Web of Science ®Google Scholar
• Henry RR, Wallace P, Olefsky JM. Effects of weight loss on mechanisms of hyperglycemia in obese non-insulin dependent diabetes mellitus. Diabetes 35, 990–998 (1986).
   PubMed Web of Science ®Google Scholar
• Yki-Jarvinen H, Helve E, Koivisto VA. Hyperglycemia decreases glucose uptake in Type 1 diabetes. Diabetes 36, 892–896 (1987).
   PubMed Web of Science ®Google Scholar
• Kahn B, Schulman GI, DeFronzo RA et al. Normalization of blood glucose in diabetic rats with phlorizin treatment reverses insulin-resistant glucose transport in adipose cells without restoring glucose transporter gene expression. J. Clin. Invest. 87, 561–570 (1991).
   PubMed Web of Science ®Google Scholar
• McClain DA, Lubas WA, Cooksey RC et al. Altered glycan-dependent signaling induces insulin resistance and hyper-leptinemia. Proc. Natl Acad. Sci. USA 99, 10695–10699 (2002).
   PubMed Web of Science ®Google Scholar
• Herbert L, Daniels M, Zhou J et al. Over-expression of glutamine:fructose-6-phosphate amidotransferase in transgenic mice leads to insulin resistance. J. Clin. Invest. 98, 930–936 (1996).
   PubMed Web of Science ®Google Scholar
• Yki-Jarvinen H, Virkamaki A, Daniels MD et al. Insulin and glucosamine infusions increase O-linked N-acetyl-glucosamine in skeletal muscle proteins in vivo. Metabolism 47, 449–455 (1998).
   PubMed Web of Science ®Google Scholar
• Manning G, Whyte DB, Martinez R et al. The protein kinase complement of the human genome. Science 298, 1912–1934 (2002).
   PubMed Web of Science ®Google Scholar
• Muller U, Steinberger D, Nemeth AH. Clinical and molecular genetics of primary dystonias. Neurogenetics 1, 165–177 (1998).
   Google Scholar
• Lubas WA, Frank DW, Krause M et al. O-linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats. J. Biol. Chem. 272, 9316–9324 (1997).
   PubMed Web of Science ®Google Scholar
• Jacobsen SE, Binkowski KA, Olszewski NE. SPINDLY, a tetratricopeptide repeat protein involved in gibberellin signal transduction in Arabidopsis. Proc. Natl Acad. Sci. USA 93, 9292–9296 (1996).
   PubMed Web of Science ®Google Scholar
• Hanover JA, Yu S, Lubas WB et al. Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc transferase encoded by a single mammalian gene. Arch. Biochem. Biophys 409, 287–297 (2003).
   PubMed Web of Science ®Google Scholar
• Lazarus MB, Yunsun Nam, Jiang J et al. Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 469, 564–568 (2011).
   PubMed Web of Science ®Google Scholar
• Jinek M, Rehwinkel J, Lazarus BD et al. The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha. Nat. Struct. Mol. Biol. 11, 1001–1007 (2004).
   PubMed Web of Science ®Google Scholar
• Kreppel LK, Hart GW. Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats. J. Biol. Chem. 274, 32015–32022 (1999).
   PubMed Web of Science ®Google Scholar
• Haltiwanger RS, Blomberg MA, Hart GW. 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).
   PubMed Web of Science ®Google Scholar
• Lazarus MB, Jiang J, Gloster TM, et al. Structural snapshots of the reaction coordinate for O-GlcNAc transferase. Nat. Chem. Biol. 8, 966–968 (2012).
   Google Scholar
• Schimpl M, Zheng X, Borodkin VS et al. O-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysis. Nat. Chem. Biol. 8, 969–974 (2012).
   Google Scholar
• Hart GW, Akimoto Y. The O-GlcNAc modification. In: Essentials of Glycobiology (2nd Edition). Varki ACR, Esko JD, Freeze HH, Stanley P, Bertozzi CR, Hart GW, Etzler ME (Eds). Cold Spring Harbor Laboratory Press, Cold Spring, Harbor NY, USA (2009).
   Google Scholar
• Kreppel LK, Blomberg MA, Hart GW. 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).
   PubMed Web of Science ®Google Scholar
• Whelan SA, Lane DM, Hart GW. Regulation of the O-GlcNAc transferase by insulin signaling. J. Biol. Chem. 283, 21411–21417 (2008).
   Google Scholar
• Akimoto Y, Hart GW, Wells L et al. Elevation of the post-translational modification of proteins by O-linked N-acetylglucosamine leads to deterioration of the glucose-stimulated insulin secretion in the pancreas of diabetic Goto-Kakizaki rats. Glycobiology 17, 127–140 (2007).
   Google Scholar
• Yang X, Ongusaha P, Miles P et al. Phosphoinositide signaling links O-GlcNAc transferase to insulin resistance. Nature 451, 964–970 (2008).
   PubMed Web of Science ®Google Scholar
• Clark RJ, McDonough PM, Swanson E et al. Diabetes and the accompanying hyperglycemia impairs cardiomyocyte calcium cycling through increased nuclear GlcNAcylation. J. Biol. Chem. 278, 44230–44237 (2003).
   PubMed Web of Science ®Google Scholar
• Lenzen S, Munday R. Thiol-group reactivity, hydrophilicity and stability of alloxan, its reduction products and its N-methyl derivatives and a comparison with ninhydrin. Biochem. Pharmacol. 42, 1385–1391 (1991).
   PubMed Web of Science ®Google Scholar
• Robinson KA, Ball LE, Buse MG. Reduction of O-GlcNAc protein modification does not prevent insulin resistance in 3T3-L1 adipocytes. Am. J. Physiol. Endocrinol. Metab. 292, E884–E890 (2007).
   Google Scholar
• Shafi R, Lyer SP, Ellies LG et al. 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).
   PubMed Web of Science ®Google Scholar
• Kazemi Z, Chang H, Haserodt S et al. O-Linked Beta-N-acetylglucosamine (O-GlcNAc) regulates stress-induced heat shock protein expression in a GSK-3β-dependent manner. J. Biol. Chem. 285, 39096–39107 (2010).
   PubMed Web of Science ®Google Scholar
• de la Monte SM, Tong M, Lester-Coll N et al. Therapeutic rescue of neurodegeneration in experimental Type 3 diabetes: relevance to Alzheimer’s disease. J. Alzheimers Dis. 10, 89–109 (2006).
   PubMed Web of Science ®Google Scholar
• Butkinaree C, Cheung WD, Park S et al. Characterization of beta-N-acetylglucosaminidase cleavage by caspase-3 during apoptosis. J. Biol. Chem. 283, 23557–23566 (2008).
   Google Scholar
• Comtesse N, Maldener E, Meese E. Identification of a nuclear variant of MGEA5, a cytoplasmic hyaluronidase and a beta-N-acetylglucosaminidase. Biochem. Biophys. Res. Commun. 283, 634–640 (2001).
   PubMed Web of Science ®Google Scholar
• Soesant Y, Luo B, Parker G et al. Pleiotropic and age-dependent effects of decreased protein modification by O-Linked N-acetylglucosamine on pancreatic beta-cell function and vascularization. J. Biol. Chem. 286, 26118–26126 (2011).
   Google Scholar
• Dentin R, Hedrick S, Xie J et al. Hepatic glucose sensing via the CREB coactivator CRTC2. Science 319, 1402–1405 (2008).
   PubMed Web of Science ®Google Scholar
• Soesanto YA, Luo B, Jones D et al. Regulation of Akt signaling by O-GlcNAc in euglycemia. Am. J. Physiol. Endocrinol. Metab. 295, E974–E980 (2008).
   Google Scholar
• Hu Y, Belke D, Suarez J et al. Adenovirus-mediated over-expression of O-GlcNAcase improves contractile function in the diabetic heart. Circ. Res. 96, 1006–1013 (2005).
   PubMed Web of Science ®Google Scholar
• Forsythe ME, Love DC, Lazarus BD et al. Caenorhabditis elegans ortholog of a diabetes susceptibility locus: oga-1 (O-GlcNAcase) knockout impacts O-GlcNAc cycling, metabolism, and dauer. Proc. Natl Acad. Sci. USA 103, 11952–11957 (2006).
   PubMed Web of Science ®Google Scholar
• Vosseller K, Wells L, Lane MD et al. Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes. Proc. Natl Acad. Sci. USA 99, 5313–5318 (2002).
   PubMed Web of Science ®Google Scholar
• Arias EB, Kim J, Cartee GD. Prolonged incubation in PUGNAc results in increased protein O-Linked glycosylation and insulin resistance in rat skeletal muscle. Diabetes 53, 921–930 (2004).
   PubMed Web of Science ®Google Scholar
• Issad T, Kuo M. O-GlcNAc modification of transcription factors, glucose sensing and glucotoxicity. Trends Endocrinol Metab. 19, 380–389 (2008).
   Web of Science ®Google Scholar
• Ozcan S, Andrali SS, Cantrell, J.E. Modulation of transcription factor function by O-GlcNAc modification. Biochim. Biophys. Acta 1799, 353–364 (2010).
   PubMed Web of Science ®Google Scholar
• Slawson C, Hart GW. O-GlcNAc signalling: implications for cancer cell biology. Nat. Rev. Cancer 11, 678–684 (2011).
   PubMed Web of Science ®Google Scholar
• Liu K, Paterson AJ, Chin E et al. Glucose stimulates protein modification by O-linked GlcNAc in pancreatic b cells: Linkage of O-linked GlcNAc to beta cell death. Proc. Natl Acad. Sci. USA 97, 2820–2825 (2000).
   Google Scholar
• Andrali SS, Qian Q, Ozcan S. Glucose mediates the translocation of NeuroD1 by O-linked glycosylation. J. Biol. Chem. 282, 15589–15596 (2007).
   PubMed Web of Science ®Google Scholar
• Gao Y, Miyazaki J, Hart GW. The transcription factor PDX-1 is posttranslationally 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).
   PubMed Web of Science ®Google Scholar
• Kebede M, Ferdaoussi M, Mancini A et al. Glucose activates free fatty acid receptor 1 gene transcription via phosphatidylinositol-3-kinase-dependent O-GlcNAcylation of pancreas-duodenum homeobox-1. Proc. Natl Acad. Sci. USA 109, 2376–2381 (2012).
   PubMedGoogle Scholar
• Whelan SA, Dias WB, Lakshmanan T et al. Regulation of insulin receptor substrate 1 (IRS-1)/AKT kinase-mediated insulin signaling by O-linked beta-N-acetylglucosamine in 3T3-L1 adipocytes. J. Biol. Chem. 285, 5204–5211 (2010).
   PubMed Web of Science ®Google Scholar
• Parker GJ, Lund KP, Taylor RP et al. Insulin resistance of glycogen synthase mediated by O-linked N-acetylglucosamine. J. Biol. Chem. 278, 10022–10027 (2003).
   Google Scholar
• Teo CF, Wollaston-Hayden EE, Wells L. Hexosamine flux, the O-GlcNAc modification, and the development of insulin resistance in adipocytes. Mol. Cell. Endocrinol. 318, 44–53 (2010).
   Google Scholar
• Housley MP, Rodgers JT, Udeshi ND et al. O-GlcNAc regulates FoxO activation in response to glucose. J. Biol. Chem. 283, 16283–16292 (2008).
   PubMed Web of Science ®Google Scholar
• Housley MP, Udeshi ND, Rodgers JT et al. A PGC-1alpha-O-GlcNAc transferase complex regulates FoxO transcription factor activity in response to glucose. J. Biol. Chem. 284, 5148–5157 (2009).
   PubMed Web of Science ®Google Scholar
• Ruan H, Han X, Li M et al. O-GlcNAc Transferase/host cell factor C1 complex regulates gluconeogenesis by modulating PGC-1a stability. Cell Metab. 16, 226–237 (2012).
   PubMed Web of Science ®Google Scholar
• Guinez C, Filhoulaud G, Rayah-Benhamed F et al. O-GlcNAcylation increases ChREBP protein content and trans-criptional activity in the liver. Diabetes 60, 1399–1413 (2011).
   PubMedGoogle Scholar
• Anthonisen EH, Berven L, Holm S et al. Nuclear receptor liver X receptor is O-GlcNAc-modified in response to glucose. J. Biol. Chem. 285, 1607–1615 (2010).
   PubMedGoogle Scholar
• Arias EB, Cartee GD. Relationship between protein O-linked glycosylation and insulin-stimulated glucose transport in rat skeletal muscle following calorie restriction or exposure to O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarba-mate. Acta Physiol. Scand. 183, 281–289 (2005).
   Google Scholar
• Walgren JL, Vincent TS, Schey KL et al. High glucose and insulin promote O-GlcNAc modification of proteins, including alpha-tubulin. Am. J. Physiol. Endocrinol. Metab. 284, E424–E434 (2003).
   PubMed Web of Science ®Google Scholar
• Hedou J, Cieniewski-Bernard C, Leroy Y et al. O-linked N-acetylglucosaminylation is involved in the Ca2+ activation properties of rat skeletal muscle. J. Biol. Chem. 282, 10360–10369 (2007).
   Google Scholar
• Hedou J, Bastide B, Page A et al. Mapping of O-linked beta-N-acetylglucosamine modification sites in key contractile proteins of rat skeletal muscle. Proteomics 9, 2139–2148 (2009.)
   PubMedGoogle Scholar
• Fulop N, Marchase RB, Chatham JC. Role of protein O-linked N-acetyl-glucosamine in mediating cell function and survival in the cardiovascular system. Cardiovasc. Res. 73, 288–297 (2007).
   Google Scholar
• Laczy B, Hill BG, Wang K et al. Protein O-GlcNAcylation: a new signaling paradigm for the cardiovascular system. Am. J. Physiol. Heart Circ. Physiol. 296, H13–H28 (2009).
   Google Scholar
• Ngoh GA, Facundo HT, Zafir A et al. O-GlcNAc Signaling in the Cardiovascular System. Circ. Res. 107, 171–185 (2010).
   PubMed Web of Science ®Google Scholar
• Zachara NE. The roles of O-linked β-N-acetylglucosamine in cardiovascular physiology and disease. Am. J. Physiol. Heart Circ. Physiol. 302, H1905–H1918 (2012).
   PubMed Web of Science ®Google Scholar
• Jones SP, Zachara NE, Ngoh GA et al. Cardioprotection by N-acetylglucosamine linkage to cellular proteins. Circulation 117, 1172–1182 (2008).
   PubMed Web of Science ®Google Scholar
• Ngoh GA, Watson LJ, Facundo HT et al. Noncanonical glycosyltransferase modulates post-hypoxic cardiac myocyte death and mitochondrial permeability transition. J. Mol. Cell. Cardiol. 45, 313–325 (2008).
   PubMed Web of Science ®Google Scholar
• Hu Y, Suarez J, Fricovsky E et al. Increased enzymatic O-GlcNAcylation of mitochondrial proteins impairs mitochondrial function in cardiac myocytes exposed to high glucose. J. Biol. Chem. 284, 547–555 (2009).
   PubMed Web of Science ®Google Scholar
• Johnsen VL, Belke DD, Hughey CC, et al. Enhanced cardiac protein glycosylation (O-GlcNAc) of selected mitochondrial proteins in rats artificially selected for low running capacity. Physiol. Genomics 45, 17–25 (2013).
   PubMed Web of Science ®Google Scholar
• Ramirez-Correa GA, Jin W, Wang Z et al. O-linked GlcNAc modification of cardiac myofilament proteins: a novel regulator of myocardial contractile function. Circ. Res. 103, 1354–1358 (2008).
   PubMed Web of Science ®Google Scholar
• Goldberg H, Whiteside C, Fantus I. O-linked beta-N-acetylgluco-samine supports p38 MAPK activation by high glucose in glomerular mesangial cells. Am. J. Physiol. Endocrinol. Metab. 301, E713–E726 (2011).
   PubMed Web of Science ®Google Scholar
• Yao D, Taguchi T, Matsumura T et al. High glucose increases angiopoietin-2 transcription in microvascular endothelial cells through methylglyoxal modification of mSin3A. J. Biol. Chem. 282, 31038–31045 (2007).
   PubMed Web of Science ®Google Scholar
• James LR, Tang D, Ingram A et al. Flux through the hexosamine pathway is a determinant of nuclear factor kappaB-dependent promoter activation. Diabetes 51, 1146–1156 (2002).
   PubMedGoogle Scholar
• Yang WH, Park SY, Nam HW et al. NF-kappaB activation is associated with its O-GlcNAcylation state under hyperglycemic conditions. Proc. Natl Acad. Sci. USA 105, 17345–17350 (2008).
   PubMed Web of Science ®Google Scholar
• Allison DF, Wamsley JJ, Kumar M et al. Modification of RelA by O-linked N-acetylglucosamine links glucose metabolism to NF-κB acetylation and transcription. Proc. Natl Acad. Sci. USA 94, 2927–2932 (2012).
   Google Scholar
• Du XL, Edelstein D, Rossetti L et al. 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).
   PubMed Web of Science ®Google Scholar
• Du XL, Edelstein D, Dimmeler S et al. Hyperglycemia inhibits endothelial nitric oxide synthase activity by posttranslational modification at the Akt site. J. Clin. Invest. 108, 1341–1348 (2001).
   PubMed Web of Science ®Google Scholar
• Musicki B, Kramer MF, Becker RE et al. Inactivation of phosphorylated endothelial nitric oxide synthase (Ser-1177) by O-GlcNAc in diabetes-associated erectile dysfunction. Proc. Natl Acad. Sci. USA 102, 11870–11875 (2005).
   Google Scholar
• Wang Z, Park K, Comer F et al. Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes. Diabetes 58, 309–317 (2009).
   PubMed Web of Science ®Google Scholar
• Hu P, Shimoji S, Hart GW. Site-specific interplay between O-GlcNAcylation and phosphorylation in cellular regulation. FEBS Lett. 584, 2526–2538 (2010).
   Google Scholar
• Butkinaree C, Park K, Hart GW. O-linked N-acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress. Biochem. Biophys. Acta 1800, 96–106 (2010).
   PubMed Web of Science ®Google Scholar
• Zeidan Q, Hart GW. The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways. J. Cell Sci. 123:13–22 (2010).
   PubMed Web of Science ®Google Scholar
• Ande SR, Moulik S, Mishra S. Interaction between O-GlcNAc modification and tyrosine phosphorylation of prohibitin: Implication for a novel binary switch. PLoS One 4, e4586 (2009).
   PubMedGoogle Scholar
• Sakabe K, Hart GW. O-GlcNAc transferase regulates mitotic chromatin dynamics. J. Biol. Chem. 285, 34460–34468 (2010).
   PubMed Web of Science ®Google Scholar
• Sakabe K, Wang Z, Hart GW. β-N-acetylglucosamine (O-GlcNAc) is part of the histone code. Proc. Natl Acad. Sci. USA 107, 19915–19920 (2010).
   PubMed Web of Science ®Google Scholar
• Fujiki R, Hashiba W, Sekine H et al. GlcNAcylation of histone H2B facilitates its monoubiquitination. Nature 480, 557–560 (2011).
   PubMed Web of Science ®Google Scholar
• Comer FI, Vosseller K, Wells L et al. Characterization of a mouse monoclonal antibody specific for O-linked N-acetylglucosamine. Anal. Biochem. 293, 169–177 (2001).
   PubMedGoogle Scholar
• Snow CM, Senior A, Gerace L. Monoclonal antibodies identify a group of nuclear pore complex glycoproteins. J. Cell Biol. 104, 1143–1156 (1987).
   PubMed Web of Science ®Google Scholar
• Wang J, Torij M, Liu H et al. dbOGAP-an integrated bio-informatics resource for protein O-GlcNAcylation. BMC Bioinformatics. 12, 91 (2011).
   Google Scholar
• Syka JE, Coon JJ, Schroeder MJ et al. Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc. Natl Acad. Sci. USA 101, 9528–9533 (2004).
   PubMed Web of Science ®Google Scholar
• Wells L, Vosseller K, Cole RN et al. Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications. Mol. Cell Proteomics 1, 791–804 (2002).
   PubMed Web of Science ®Google Scholar
• Vosseller K, Hansen KC, Chalkley RJ et al. Quantitative analysis of both protein expression and serine/threonine post-translational modifications through stable isotope labeling with dithiothreitol. Proteomics 5, 388–398 (2005).
   PubMed Web of Science ®Google Scholar
• Overath T, Kuckelkorn U, Henklein P et al. Mapping of O-GlcNAc sites of 20S proteasome subunits and Hsp90 by a novel biotin-cystamine tag. Mol. Cell Proteomics 11, 467–477 (2012).
   Google Scholar
• Hahne H, Moghaddas-Gholami A, Kuster B. Discovery of O-GlcNAc-modified proteins in published large-scale proteome data. Mol. Cell Proteomics 11, 843–850 (2012).
   Google Scholar
• Teo CF, Ingale S, Wolfert M et al. Glycopeptide-specific mono-clonal antibodies suggest new roles for O-GlcNAc. Nat. Chem. Biol. 6, 338–343 (2010).
   Google Scholar
• Zhao P, Viner R, Teo CF et al. Combining high-energy C-trap dissociation and electron transfer dissociation for protein O-GlcNAc modification site assignment. J. Proteome Res. 10, 4088–4104 (2011).
   PubMed Web of Science ®Google Scholar
• Kelly WG, Hart GW. Glycosylation of chromosomal proteins: localization of O-linked N-acetylglucosamine in Drosophila chromatin. Cell 57, 243–251 (1989).
   PubMed Web of Science ®Google Scholar
• Chalkley RJ, Thalhammer A, Schoepfer R et al. Identification of protein O-GlcNAcylation sites using electron transfer dissociation mass spectrometry on native peptides. Proc. Natl Acad. Sci. USA 106, 8894–8899 (2009).
   PubMed Web of Science ®Google Scholar
• Trinidad JC, Barkan DT, Gulledge BF et al. Global identification and characterization of both O-GlcNAcylation and phosphory-lation at the murine synapse. Mol. Cell Proteomics 11, 215–229 (2012).
   PubMedGoogle Scholar
• Khidekel N, Ficarro SB, Clark MC et al. Probing the dynamics of O-GlcNAc glycosylation in the brain using quantitative proteomics. Nat. Chem. Biol. 3, 339–348 (2007).
   PubMed Web of Science ®Google Scholar
• Wang Z, Udeshi ND, O’Malley M et al. Enrichment and sitemapping of O-linked N-acetylglucosamine by a combination of chemical/enzymatic tagging, photochemical cleavage, and electron transfer dissociation mass spectrometry. Mol. Cell Proteomics 9, 153–160 (2010).
   Google Scholar
• Alfaro JF, Gong CX, Monroe ME et al. Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-specific O-GlcNAc transferase targets. Proc. Natl Acad. Sci. USA 109, 7280–7285 (2012).
   PubMed Web of Science ®Google Scholar
• Wang Z, Udeshi ND, Slawson C et al. Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis. Sci. Signal. 3, ra2 (2010).
   PubMed Web of Science ®Google Scholar
• Vocadlo DJ, Hang HC, Kim EJ et al. A chemical approach for identifying O-GlcNAc-modified proteins in cells. Proc. Natl Acad. Sci. USA 100, 9116–9121 (2003).
   PubMed Web of Science ®Google Scholar
• Nandi A, Sprung R, Barma DK et al. Global identification of O-GlcNAc-modified proteins. Anal. Chem. 78, 452–458 (2006).
   Google Scholar
• Zaro BW, Yang YY, Hang HC et al. Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1. Proc. Natl Acad. Sci. USA 108, 8146–8151 (2011).
   Google Scholar
• Hahne H, Sobotzki N, Tamara N et al. Proteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometry. J. Proteome Res. 12 (2), 927–936 (2013).
   PubMed Web of Science ®Google Scholar
• Choudhary C, Mann M. Decoding signaling networks by mass spectrometry-based proteomics. Nat. Rev. Mol. Cell Bio. 11, 427–439 (2010).
   PubMed Web of Science ®Google Scholar
• Topf F, Schvartz D, Gaudet P et al. The Human Diabetes Proteome Project (HDPP): from network biology to targets for therapies and prevention. Transl. Proteomics 1, 3–11 (2013).
   Google Scholar
• Park K, Saudek CD, Hart GW et al. Increased expression of beta-N-acetylglucosaminidase in erythrocytes from individuals with pre-diabetes and diabetes. Diabetes 59, 1845–1850 (2010).
   PubMed Web of Science ®Google Scholar
• Springhorn C, Matsha TE, Erasmus RT et al. Exploring leukocyte O-GlcNAcylation as a novel diagnostic tool for the earlier detection of Type 2 diabetes mellitus. J. Clin. Endocrinol. Metab. 97, 4640–4649 (2012).
   Google Scholar