Intracellular protein O-GlcNAc modification integrates nutrient status with transcriptional and metabolic regulation

Advances in Cancer Research

Volumn 126, Issue , 2015, Pages 137-166

  Nagel, Alexis K ^a   Ball, Lauren E ^a  

^a MEDICAL UNIVERSITY OF SOUTH CAROLINA   (United States)

Author keywords

Cancer; Hexosamine biosynthetic pathway; Metabolic reprogramming; MGEA5; O GlcNAc modification; O GlcNAc transferase; O GlcNAcase

Indexed keywords

CELL PROTEIN; ENZYME; GLUCOSE; HEXOSAMINE; N ACETYL BETA GLUCOSAMINIDASE; N ACETYLGLUCOSAMINE; N ACETYLGLUCOSAMINE TRANSFERASE; O LINKED N ACETYLGLUCOSAMINE; TRANSCRIPTION FACTOR; TRANSFERASE; TUNICAMYCIN; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE; N ACETYLGLUCOSAMINYLTRANSFERASE; O-GLCNAC TRANSFERASE;

ARTICLE; BIOSYNTHESIS; BREAST CANCER; CANCER CELL; CANCER CELL LINE; CANCER PATIENT; CELL FUNCTION; COLON CANCER; ENZYME ACTIVITY; ENZYME METABOLISM; ENZYME STRUCTURE; EPIGENETICS; GLUCOSE HOMEOSTASIS; GLUCOSE METABOLISM; HISTONE ACETYLATION; HUMAN; IN VITRO STUDY; IN VIVO STUDY; LUNG CANCER; METABOLIC REGULATION; NEOPLASM; NONHUMAN; NUTRIENT; PANCREAS CANCER; PRIORITY JOURNAL; PROSTATE CANCER; PROTEIN GLYCOSYLATION; PROTEIN PROCESSING; PUBLICATION; TRANSCRIPTION REGULATION; TUMOR GROWTH; ANIMAL; FOOD; GENETICS; GLYCOSYLATION; METABOLISM;

ACETYLGLUCOSAMINE; ANIMALS; EPIGENOMICS; FOOD; GLYCOSYLATION; HUMANS; METABOLIC NETWORKS AND PATHWAYS; N-ACETYLGLUCOSAMINYLTRANSFERASES; NEOPLASMS; PROTEIN PROCESSING, POST-TRANSLATIONAL;

EID: 84923308012     PISSN: 0065230X     EISSN: 21625557     Source Type: Book Series    
DOI: 10.1016/bs.acr.2014.12.003     Document Type: Chapter

References (174)

1. Alfaro J.F., Gong C.X., Monroe M.E., Aldrich J.T., Clauss T.R., Purvine S.O., et al. Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-specific O-GlcNAc transferase targets. Proceedings of the National Academy of Sciences of the United States of America 2012, 109:7280-7285.
2. Andres-Bergos J., Tardio L., Larranaga-Vera A., Gomez R., Herrero-Beaumont G., Largo R. The increase in O-linked N-acetylglucosamine protein modification stimulates chondrogenic differentiation both in vitro and in vivo. The Journal of Biological Chemistry 2012, 287:33615-33628.
3. Anthonisen E.H., Berven L., Holm S., Nygard M., Nebb H.I., Gronning-Wang L.M. Nuclear receptor liver X receptor is O-GlcNAc-modified in response to glucose. The Journal of Biological Chemistry 2010, 285:1607-1615.
4. Blasius M., Forment J.V., Thakkar N., Wagner S.A., Choudhary C., Jackson S.P. A phospho-proteomic screen identifies substrates of the checkpoint kinase Chk1. Genome Biology 2011, 12:R78.
5. Braidman I., Carroll M., Dance N., Robinson D., Poenaru L., Weber A., et al. Characterisation of human N-acetyl-beta-hexosaminidase C. FEBS Letters 1974, 41:181-184.
6. Broschat K.O., Gorka C., Page J.D., Martin-Berger C.L., Davies M.S., Huang Hc H.C., et al. Kinetic characterization of human glutamine-fructose-6-phosphate amidotransferase I: Potent feedback inhibition by glucosamine 6-phosphate. The Journal of Biological Chemistry 2002, 277:14764-14770.
7. Bullen J.W., Balsbaugh J.L., Chanda D., Shabanowitz J., Hunt D.F., Neumann D., et al. Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK). The Journal of Biological Chemistry 2014, 289:10592-10606.
8. Butkinaree C., Cheung W.D., Park S., Park K., Barber M., Hart G.W. Characterization of beta-N-acetylglucosaminidase cleavage by caspase-3 during apoptosis. The Journal of Biological Chemistry 2008, 283:23557-23566.
9. Butkinaree C., Park K., Hart G.W. O-linked beta-N-acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress. Biochimica et Biophysica Acta 2010, 1800:96-106.
10. Caldwell S.A., Jackson S.R., Shahriari K.S., Lynch T.P., Sethi G., Walker S., et al. Nutrient sensor O-GlcNAc transferase regulates breast cancer tumorigenesis through targeting of the oncogenic transcription factor FoxM1. Oncogene 2010, 29:2831-2842.
11. Capotosti F., Guernier S., Lammers F., Waridel P., Cai Y., Jin J., et al. O-GlcNAc transferase catalyzes site-specific proteolysis of HCF-1. Cell 2011, 144:376-388.
12. Carlson S.M., Chouinard C.R., Labadorf A., Lam C.J., Schmelzle K., Fraenkel E., et al. Large-scale discovery of ERK2 substrates identifies ERK-mediated transcriptional regulation by ETV3. Science Signaling 2011, 4:rs11.
13. Cetinbas N., Macauley M.S., Stubbs K.A., Drapala R., Vocadlo D.J. Identification of Asp174 and Asp175 as the key catalytic residues of human O-GlcNAcase by functional analysis of site-directed mutants. Biochemistry 2006, 45:3835-3844.
14. Champattanachai V., Netsirisawan P., Chaiyawat P., Phueaouan T., Charoenwattanasatien R., Chokchaichamnankit D., et al. Proteomic analysis and abrogated expression of O-GlcNAcylated proteins associated with primary breast cancer. Proteomics 2013, 13:2088-2099.
15. Chen Q., Chen Y., Bian C., Fujiki R., Yu X. TET2 promotes histone O-GlcNAcylation during gene transcription. Nature 2013, 493:561-564.
16. Cheng X., Hart G.W. Alternative O-glycosylation/O-phosphorylation of serine-16 in murine estrogen receptor beta: Post-translational regulation of turnover and transactivation activity. The Journal of Biological Chemistry 2001, 276:10570-10575.
17. Cheung W.D., Hart G.W. AMP-activated protein kinase and p38 MAPK activate O-GlcNAcylation of neuronal proteins during glucose deprivation. The Journal of Biological Chemistry 2008, 283:13009-13020.
18. Cheung W.D., Sakabe K., Housley M.P., Dias W.B., Hart G.W. O-linked beta-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins. The Journal of Biological Chemistry 2008, 283:33935-33941.
19. Chou T.Y., Hart G.W., Dang C.V. c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas. The Journal of Biological Chemistry 1995, 270:18961-18965.
20. Chu C.S., Lo P.W., Yeh Y.H., Hsu P.H., Peng S.H., Teng Y.C., et al. O-GlcNAcylation regulates EZH2 protein stability and function. Proceedings of the National Academy of Sciences of the United States of America 2014, 111:1355-1360.
21. Comer F.I., Hart G.W. Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II. Biochemistry 2001, 40:7845-7852.
22. Comtesse N., Maldener E., Meese E. Identification of a nuclear variant of MGEA5, a cytoplasmic hyaluronidase and a beta-N-acetylglucosaminidase. Biochemical and Biophysical Research Communications 2001, 283:634-640.
23. DeBerardinis R.J. Is cancer a disease of abnormal cellular metabolism? New angles on an old idea. Genetics in Medicine: Official Journal of the American College of Medical Genetics 2008, 10:767-777.
24. Deberardinis R.J., Sayed N., Ditsworth D., Thompson C.B. Brick by brick: Metabolism and tumor cell growth. Current Opinion in Genetics & Development 2008, 18:54-61.
25. Dentin R., Hedrick S., Xie J., Yates J., Montminy M. Hepatic glucose sensing via the CREB coactivator CRTC2. Science (New York, NY) 2008, 319:1402-1405.
26. Deplus R., Delatte B., Schwinn M.K., Defrance M., Mendez J., Murphy N., et al. TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and SET1/COMPASS. The EMBO Journal 2013, 32:645-655.
27. de Queiroz R.M., Carvalho E., Dias W.B. O-GlcNAcylation: The sweet side of the cancer. Frontiers in Oncology 2014, 4:132.
28. Dias W.B., Cheung W.D., Hart G.W. O-GlcNAcylation of kinases. Biochemical and Biophysical Research Communications 2012, 422:224-228.
29. Dias W.B., Cheung W.D., Wang Z., Hart G.W. Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification. The Journal of Biological Chemistry 2009, 284:21327-21337.
30. Dong D.L., Hart G.W. Purification and characterization of an O-GlcNAc selective N-acetyl-beta-d-glucosaminidase from rat spleen cytosol. The Journal of Biological Chemistry 1994, 269:19321-19330.
31. Dorfmueller H.C., Borodkin V.S., Schimpl M., Shepherd S.M., Shpiro N.A., van Aalten D.M. GlcNAcstatin: A picomolar, selective O-GlcNAcase inhibitor that modulates intracellular O-glcNAcylation levels. Journal of the American Chemical Society 2006, 128:16484-16485.
32. Feng Z., Hui Y., Ling L., Xiaoyan L., Yuqiu W., Peng W., et al. FBXW10 is negatively regulated in transcription and expression level by protein O-GlcNAcylation. Biochemical and Biophysical Research Communications 2013, 438:427-432.
33. Ferrer C.M., Lynch T.P., Sodi V.L., Falcone J.N., Schwab L.P., Peacock D.L., et al. O-GlcNAcylation regulates cancer metabolism and survival stress signaling via regulation of the HIF-1 pathway. Molecular Cell 2014, 54:820-831.
34. Filhoulaud G., Guilmeau S., Dentin R., Girard J., Postic C. Novel insights into ChREBP regulation and function. Trends in Endocrinology and Metabolism: TEM 2013, 24:257-268.
35. Fletcher B.S., Dragstedt C., Notterpek L., Nolan G.P. Functional cloning of SPIN-2, a nuclear anti-apoptotic protein with roles in cell cycle progression. Leukemia 2002, 16:1507-1518.
36. Fong J.J., Nguyen B.L., Bridger R., Medrano E.E., Wells L., Pan S., et al. beta-N-Acetylglucosamine (O-GlcNAc) is a novel regulator of mitosis-specific phosphorylations on histone H3. The Journal of Biological Chemistry 2012, 287:12195-12203.
37. Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., et al. GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis. Nature 2009, 459:455-459.
38. Fujiki R., Hashiba W., Sekine H., Yokoyama A., Chikanishi T., Ito S., et al. GlcNAcylation of histone H2B facilitates its monoubiquitination. Nature 2011, 480:557-560.
39. Gao Y. Mechanism, structure, and inhibition of O-GlcNAc processing enzymes. Current Signal Transduction Therapy 2010, 5:74-91.
40. Gao Y., Wells L., Comer F.I., Parker G.J., Hart G.W. Dynamic O-glycosylation of nuclear and cytosolic proteins: Cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain. The Journal of Biological Chemistry 2001, 276:9838-9845.
41. Gloster T.M., Zandberg W.F., Heinonen J.E., Shen D.L., Deng L., Vocadlo D.J. Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells. Nature Chemical Biology 2011, 7:174-181.
42. Gross B.J., Kraybill B.C., Walker S. Discovery of O-GlcNAc transferase inhibitors. Journal of the American Chemical Society 2005, 127:14588-14589.
43. Gu Y., Gao J., Han C., Zhang X., Liu H., Ma L., et al. O-GlcNAcylation is increased in prostate cancer tissues and enhances malignancy of prostate cancer cells. Molecular Medicine Reports 2014, 10:897-904.
44. Gu Y., Mi W., Ge Y., Liu H., Fan Q., Han C., et al. GlcNAcylation plays an essential role in breast cancer metastasis. Cancer Research 2010, 70:6344-6351.
45. Guinez C., Filhoulaud G., Rayah-Benhamed F., Marmier S., Dubuquoy C., Dentin R., et al. O-GlcNAcylation increases ChREBP protein content and transcriptional activity in the liver. Diabetes 2011, 60:1399-1413.
46. Gut P., Verdin E. The nexus of chromatin regulation and intermediary metabolism. Nature 2013, 502:489-498.
47. Hahne H., Kuster B. Discovery of O-GlcNAc-6-phosphate modified proteins in large-scale phosphoproteomics data. Molecular & Cellular Proteomics: MCP 2012, 11:1063-1069.
48. Halim A., Brinkmalm G., Ruetschi U., Westman-Brinkmalm A., Portelius E., Zetterberg H., et al. Site-specific characterization of threonine, serine, and tyrosine glycosylations of amyloid precursor protein/amyloid beta-peptides in human cerebrospinal fluid. Proceedings of the National Academy of Sciences of the United States of America 2011, 108:11848-11853.
49. Haltiwanger R.S., Blomberg M.A., Hart G.W. Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase. The Journal of Biological Chemistry 1992, 267:9005-9013.
50. Hanahan D., Weinberg R.A. Hallmarks of cancer: The next generation. Cell 2011, 144:646-674.
51. Hanover J.A., Forsythe M.E., Hennessey P.T., Brodigan T.M., Love D.C., Ashwell G., et al. A Caenorhabditis elegans model of insulin resistance: Altered macronutrient storage and dauer formation in an OGT-1 knockout. Proceedings of the National Academy of Sciences of the United States of America 2005, 102:11266-11271.
52. Hanover J.A., Krause M.W., Love D.C. The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine. Biochimica et Biophysica Acta 2010, 1800:80-95.
53. Hanover J.A., Krause M.W., Love D.C. Bittersweet memories: Linking metabolism to epigenetics through O-GlcNAcylation. Nature Reviews. Molecular Cell Biology 2012, 13:312-321.
54. Hanover J.A., Yu S., Lubas W.B., Shin S.H., Ragano-Caracciola M., Kochran J., et al. Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc transferase encoded by a single mammalian gene. Archives of Biochemistry and Biophysics 2003, 409:287-297.
55. Hart G.W., Slawson C., Ramirez-Correa G., Lagerlof O. Cross talk between O-GlcNAcylation and phosphorylation: Roles in signaling, transcription, and chronic disease. Annual Review of Biochemistry 2011, 80:825-858.
56. Hascall V.C., Wang A., Tammi M., Oikari S., Tammi R., Passi A., et al. The dynamic metabolism of hyaluronan regulates the cytosolic concentration of UDP-GlcNAc. Matrix Biology: Journal of the International Society for Matrix Biology 2014, 35:14-17.
57. Hayakawa K., Hirosawa M., Tabei Y., Arai D., Tanaka S., Murakami N., et al. Epigenetic switching by the metabolism-sensing factors in the generation of orexin neurons from mouse embryonic stem cells. The Journal of Biological Chemistry 2013, 288:17099-17110.
58. Heckel D., Comtesse N., Brass N., Blin N., Zang K.D., Meese E. Novel immunogenic antigen homologous to hyaluronidase in meningioma. Human Molecular Genetics 1998, 7:1859-1872.
59. Hornbeck P.V., Kornhauser J.M., Tkachev S., Zhang B., Skrzypek E., Murray B., et al. PhosphoSitePlus: A comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Research 2012, 40:D261-D270.
60. Housley M.P., Rodgers J.T., Udeshi N.D., Kelly T.J., Shabanowitz J., Hunt D.F., et al. O-GlcNAc regulates FoxO activation in response to glucose. The Journal of Biological Chemistry 2008, 283:16283-16292.
61. Housley M.P., Udeshi N.D., Rodgers J.T., Shabanowitz J., Puigserver P., Hunt D.F., et al. A PGC-1alpha-O-GlcNAc transferase complex regulates FoxO transcription factor activity in response to glucose. The Journal of Biological Chemistry 2009, 284:5148-5157.
62. Huang X., Pan Q., Sun D., Chen W., Shen A., Huang M., et al. O-GlcNAcylation of cofilin promotes breast cancer cell invasion. The Journal of Biological Chemistry 2013, 288:36418-36425.
63. Huet G., Hennebicq-Reig S., de Bolos C., Ulloa F., Lesuffleur T., Barbat A., et al. GalNAc-alpha-O-benzyl inhibits NeuAcalpha2-3 glycosylation and blocks the intracellular transport of apical glycoproteins and mucus in differentiated HT-29 cells. The Journal of Cell Biology 1998, 141:1311-1322.
64. Itkonen H.M., Engedal N., Babaie E., Luhr M., Guldvik I.J., Minner S., et al. UAP1 is overexpressed in prostate cancer and is protective against inhibitors of N-linked glycosylation. Oncogene 2014, 10.1038/onc.2014.307.
65. Itkonen H.M., Minner S., Guldvik I.J., Sandmann M.J., Tsourlakis M.C., Berge V., et al. O-GlcNAc transferase integrates metabolic pathways to regulate the stability of c-MYC in human prostate cancer cells. Cancer Research 2013, 73:5277-5287.
66. Janetzko J., Walker S. The making of a sweet modification: Structure and function of O-GlcNAc transferase. The Journal of Biological Chemistry 2014, 289(50):34424-34432.
67. Jang H., Kim T.W., Yoon S., Choi S.Y., Kang T.W., Kim S.Y., et al. O-GlcNAc regulates pluripotency and reprogramming by directly acting on core components of the pluripotency network. Cell Stem Cell 2012, 11:62-74.
68. Jeon J.H., Suh H.N., Kim M.O., Ryu J.M., Han H.J. Glucosamine-induced OGT activation mediates glucose production through cleaved Notch1 and FoxO1, which coordinately contributed to the regulation of maintenance of self-renewal in mouse embryonic stem cells. Stem Cells and Development 2014, 23:2067-2079.
69. Jinek M., Rehwinkel J., Lazarus B.D., Izaurralde E., Hanover J.A., Conti E. The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha. Nature Structural & Molecular Biology 2004, 11:1001-1007.
70. Jokela T.A., Makkonen K.M., Oikari S., Karna R., Koli E., Hart G.W., et al. Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1. The Journal of Biological Chemistry 2011, 286:33632-33640.
71. Jones D.R., Keune W.J., Anderson K.E., Stephens L.R., Hawkins P.T., Divecha N. The hexosamine biosynthesis pathway and O-GlcNAcylation maintain insulin-stimulated PI3K-PKB phosphorylation and tumour cell growth after short-term glucose deprivation. The FEBS Journal 2014, 281:3591-3608.
72. Kaasik K., Kivimae S., Allen J.J., Chalkley R.J., Huang Y., Baer K., et al. Glucose sensor O-GlcNAcylation coordinates with phosphorylation to regulate circadian clock. Cell Metabolism 2013, 17:291-302.
73. Kamigaito T., Okaneya T., Kawakubo M., Shimojo H., Nishizawa O., Nakayama J. Overexpression of O-GlcNAc by prostate cancer cells is significantly associated with poor prognosis of patients. Prostate Cancer and Prostatic Diseases 2014, 17:18-22.
74. Kang J.G., Park S.Y., Ji S., Jang I., Park S., Kim H.S., et al. O-GlcNAc protein modification in cancer cells increases in response to glucose deprivation through glycogen degradation. The Journal of Biological Chemistry 2009, 284:34777-34784.
75. Kawauchi K., Araki K., Tobiume K., Tanaka N. Loss of p53 enhances catalytic activity of IKKbeta through O-linked beta-N-acetyl glucosamine modification. Proceedings of the National Academy of Sciences of the United States of America 2009, 106:3431-3436.
76. Kazemi Z., Chang H., Haserodt S., McKen C., Zachara N.E. O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates stress-induced heat shock protein expression in a GSK-3beta-dependent manner. The Journal of Biological Chemistry 2010, 285:39096-39107.
77. Kebede M., Ferdaoussi M., Mancini A., Alquier T., Kulkarni R.N., Walker M.D., et al. Glucose activates free fatty acid receptor 1 gene transcription via phosphatidylinositol-3-kinase-dependent O-GlcNAcylation of pancreas-duodenum homeobox-1. Proceedings of the National Academy of Sciences of the United States of America 2012, 109:2376-2381.
78. Keembiyehetty C.N., Krzeslak A., Love D.C., Hanover J.A. A lipid-droplet-targeted O-GlcNAcase isoform is a key regulator of the proteasome. Journal of Cell Science 2011, 124:2851-2860.
79. Kettenbach A.N., Schweppe D.K., Faherty B.K., Pechenick D., Pletnev A.A., Gerber S.A. Quantitative phosphoproteomics identifies substrates and functional modules of Aurora and Polo-like kinase activities in mitotic cells. Science Signaling 2011, 4:rs5.
80. Khidekel N., Ficarro S.B., Clark P.M., Bryan M.C., Swaney D.L., Rexach J.E., et al. Probing the dynamics of O-GlcNAc glycosylation in the brain using quantitative proteomics. Nature Chemical Biology 2007, 3:339-348.
81. Kornfeld S., Kornfeld R., Neufeld E.F., O'Brien P.J. The feedback control of sugar nucleotide biosynthesis in liver. Proceedings of the National Academy of Sciences of the United States of America 1964, 52:371-379.
82. Kreppel L.K., Hart G.W. Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats. The Journal of Biological Chemistry 1999, 274:32015-32022.
83. Krzeslak A., Forma E., Bernaciak M., Romanowicz H., Brys M. Gene expression of O-GlcNAc cycling enzymes in human breast cancers. Clinical and Experimental Medicine 2012, 12:61-65.
84. Krzeslak A., Wojcik-Krowiranda K., Forma E., Bienkiewicz A., Brys M. Expression of genes encoding for enzymes associated with O-GlcNAcylation in endometrial carcinomas: Clinicopathologic correlations. Ginekologia Polska 2012, 83:22-26.
85. Laczy B., Marsh S.A., Brocks C.A., Wittmann I., Chatham J.C. Inhibition of O-GlcNAcase in perfused rat hearts by NAG-thiazolines at the time of reperfusion is cardioprotective in an O-GlcNAc-dependent manner. American Journal of Physiology. Heart and Circulatory Physiology 2010, 299:H1715-H1727.
86. Lazarus M.B., Jiang J., Kapuria V., Bhuiyan T., Janetzko J., Zandberg W.F., et al. HCF-1 is cleaved in the active site of O-GlcNAc transferase. Science (New York, NY) 2013, 342:1235-1239.
87. Lazarus B.D., Love D.C., Hanover J.A. Recombinant O-GlcNAc transferase isoforms: Identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates. Glycobiology 2006, 16:415-421.
88. Lazarus M.B., Nam Y., Jiang J., Sliz P., Walker S. Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 2011, 469:564-567.
89. Lee M.M., Nasirikenari M., Manhardt C.T., Ashline D.J., Hanneman A.J., Reinhold V.N., et al. Platelets support extracellular sialylation by supplying the sugar donor substrate. The Journal of Biological Chemistry 2014, 289:8742-8748.
90. Lehman D.M., Fu D.J., Freeman A.B., Hunt K.J., Leach R.J., Johnson-Pais T., et al. A single nucleotide polymorphism in MGEA5 encoding O-GlcNAc-selective N-acetyl-beta-d glucosaminidase is associated with type 2 diabetes in Mexican Americans. Diabetes 2005, 54:1214-1221.
91. Lewis B.A., Hanover J.A. O-GlcNAc and the epigenetic regulation of gene expression. The Journal of Biological Chemistry 2014, 289(50):34440-34448.
92. Li X., Molina H., Huang H., Zhang Y.Y., Liu M., Qian S.W., et al. O-linked N-acetylglucosamine modification on CCAAT enhancer-binding protein beta: Role during adipocyte differentiation. The Journal of Biological Chemistry 2009, 284:19248-19254.
93. Liu X., Li L., Wang Y., Yan H., Ma X., Wang P.G., et al. A peptide panel investigation reveals the acceptor specificity of O-GlcNAc transferase. FASEB Journal: Official Publication of the Federation of American Societies for Experimental Biology 2014, 28(8):3362-3372.
94. Love D.C., Krause M.W., Hanover J.A. O-GlcNAc cycling: Emerging roles in development and epigenetics. Seminars in Cell & Developmental Biology 2010, 21:646-654.
95. Lubas W.A., Hanover J.A. Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity. The Journal of Biological Chemistry 2000, 275:10983-10988.
96. Luchansky S.J., Yarema K.J., Takahashi S., Bertozzi C.R. GlcNAc 2-epimerase can serve a catabolic role in sialic acid metabolism. The Journal of Biological Chemistry 2003, 278:8035-8042.
97. Lynch T.P., Ferrer C.M., Jackson S.R., Shahriari K.S., Vosseller K., Reginato M.J. Critical role of O-linked beta-N-acetylglucosamine transferase in prostate cancer invasion, angiogenesis, and metastasis. The Journal of Biological Chemistry 2012, 287:11070-11081.
98. Ma J., Hart G.W. Protein O-GlcNAcylation in diabetes and diabetic complications. Expert Review of Proteomics 2013, 10:365-380.
99. Ma J., Hart G.W. O-GlcNAc profiling: From proteins to proteomes. Clinical Proteomics 2014, 11:8.
100. Ma Z., Vocadlo D.J., Vosseller K. Hyper-O-GlcNAcylation is anti-apoptotic and maintains constitutive NF-kappaB activity in pancreatic cancer cells. The Journal of Biological Chemistry 2013, 288:15121-15130.
101. Ma Z., Vosseller K. O-GlcNAc in cancer biology. Amino Acids 2013, 45:719-733.
102. Macauley M.S., Whitworth G.E., Debowski A.W., Chin D., Vocadlo D.J. O-GlcNAcase uses substrate-assisted catalysis: Kinetic analysis and development of highly selective mechanism-inspired inhibitors. The Journal of Biological Chemistry 2005, 280:25313-25322.
103. Manzari B., Kudlow J.E., Fardin P., Merello E., Ottaviano C., Puppo M., et al. Induction of macrophage glutamine: Fructose-6-phosphate amidotransferase expression by hypoxia and by picolinic acid. International Journal of Immunopathology and Pharmacology 2007, 20:47-58.
104. Marshall S., Bacote V., Traxinger R.R. Discovery of a metabolic pathway mediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resistance. The Journal of Biological Chemistry 1991, 266:4706-4712.
105. Marshall S., Okuyama R., Rumberger J.M. Turnover and characterization of UDP-N-acetylglucosaminyl transferase in a stably transfected HeLa cell line. Biochemical and Biophysical Research Communications 2005, 332:263-270.
106. Mazars R., Gonzalez-de-Peredo A., Cayrol C., Lavigne A.C., Vogel J.L., Ortega N., et al. The THAP-zinc finger protein THAP1 associates with coactivator HCF-1 and O-GlcNAc transferase: A link between DYT6 and DYT3 dystonias. The Journal of Biological Chemistry 2010, 285:13364-13371.
107. Mi W., Gu Y., Han C., Liu H., Fan Q., Zhang X., et al. O-GlcNAcylation is a novel regulator of lung and colon cancer malignancy. Biochimica et Biophysica Acta 2011, 1812:514-519.
108. Moremen K.W., Tiemeyer M., Nairn A.V. Vertebrate protein glycosylation: Diversity, synthesis and function. Nature Reviews. Molecular Cell Biology 2012, 13:448-462.
109. Muthusamy S., DeMartino A.M., Watson L.J., Brittian K.R., Zafir A., Dassanayaka S., et al. MicroRNA-539 is up-regulated in failing heart, and suppresses O-GlcNAcase expression. The Journal of Biological Chemistry 2014, 289:29665-29676.
110. Myers S.A., Daou S., Affar el B., Burlingame A. Electron transfer dissociation (ETD): The mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-A study of the O-GlcNAcylated protein host cell factor C1. Proteomics 2013, 13:982-991.
111. Myers S.A., Panning B., Burlingame A.L. Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells. Proceedings of the National Academy of Sciences of the United States of America 2011, 108:9490-9495.
112. Nagel A.K., Ball L.E. O-GlcNAc modification of the runt-related transcription factor 2 (Runx2) links osteogenesis and nutrient metabolism in bone marrow mesenchymal stem cells. Molecular & Cellular Proteomics: MCP 2014, 13:3381-3395.
113. Nagel A.K., Schilling M., Comte-Walters S., Berkaw M.N., Ball L.E. Identification of O-linked N-acetylglucosamine (O-GlcNAc)-modified osteoblast proteins by electron transfer dissociation tandem mass spectrometry reveals proteins critical for bone formation. Molecular & Cellular Proteomics: MCP 2013, 12:945-955.
114. Ngoh G.A., Watson L.J., Facundo H.T., Jones S.P. Augmented O-GlcNAc signaling attenuates oxidative stress and calcium overload in cardiomyocytes. Amino Acids 2011, 40:895-911.
115. Olivier-Van Stichelen S., Dehennaut V., Buzy A., Zachayus J.L., Guinez C., Mir A.M., et al. O-GlcNAcylation stabilizes beta-catenin through direct competition with phosphorylation at threonine 41. FASEB Journal: Official Publication of the Federation of American Societies for Experimental Biology 2014, 28:3325-3338.
116. Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., et al. Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Science Signaling 2010, 3:ra3.
117. Onodera Y., Nam J.M., Bissell M.J. Increased sugar uptake promotes oncogenesis via EPAC/RAP1 and O-GlcNAc pathways. The Journal of Clinical Investigation 2014, 124:367-384.
118. Ortiz-Meoz R.F., Merbl Y., Kirschner M.W., Walker S. Microarray discovery of new OGT substrates: The medulloblastoma oncogene OTX2 is O-GlcNAcylated. Journal of the American Chemical Society 2014, 136:4845-4848.
119. Ozcan S., Andrali S.S., Cantrell J.E. Modulation of transcription factor function by O-GlcNAc modification. Biochimica et Biophysica Acta 2010, 1799:353-364.
120. Park S.Y., Kim H.S., Kim N.H., Ji S., Cha S.Y., Kang J.G., et al. Snail1 is stabilized by O-GlcNAc modification in hyperglycaemic condition. The EMBO Journal 2010, 29:3787-3796.
121. Park S., Pak J., Jang I., Cho J. Inhibition of mTOR affects protein stability of OGT. Biochemical and Biophysical Research Communications 2014, 453:208-212.
122. Parker G., Taylor R., Jones D., McClain D. Hyperglycemia and inhibition of glycogen synthase in streptozotocin-treated mice: Role of O-linked N-acetylglucosamine. The Journal of Biological Chemistry 2004, 279:20636-20642.
123. Penque B.A., Hoggatt A.M., Herring B.P., Elmendorf J.S. Hexosamine biosynthesis impairs insulin action via a cholesterolgenic response. Molecular Endocrinology (Baltimore, MD) 2013, 27:536-547.
124. Phueaouan T., Chaiyawat P., Netsirisawan P., Chokchaichamnankit D., Punyarit P., Srisomsap C., et al. Aberrant O-GlcNAc-modified proteins expressed in primary colorectal cancer. Oncology Reports 2013, 30:2929-2936.
125. Rao F.V., Schuttelkopf A.W., Dorfmueller H.C., Ferenbach A.T., Navratilova I., van Aalten D.M. Structure of a bacterial putative acetyltransferase defines the fold of the human O-GlcNAcase C-terminal domain. Open Biology 2013, 3:130021.
126. Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., et al. System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Science Signaling 2011, 4:rs3.
127. Roos M.D., Han I.O., Paterson A.J., Kudlow J.E. Role of glucosamine synthesis in the stimulation of TGF-alpha gene transcription by glucose and EGF. The American Journal of Physiology 1996, 270:C803-C811.
128. Rozanski W., Krzeslak A., Forma E., Brys M., Blewniewski M., Wozniak P., et al. Prediction of bladder cancer based on urinary content of MGEA5 and OGT mRNA level. Clinical Laboratory 2012, 58:579-583.
129. Sakabe K., Wang Z., Hart G.W. Beta-N-acetylglucosamine (O-GlcNAc) is part of the histone code. Proceedings of the National Academy of Sciences of the United States of America 2010, 107:19915-19920.
130. Sesma J.I., Esther C.R., Kreda S.M., Jones L., O'Neal W., Nishihara S., et al. Endoplasmic reticulum/Golgi nucleotide sugar transporters contribute to the cellular release of UDP-sugar signaling molecules. The Journal of Biological Chemistry 2009, 284:12572-12583.
131. Shafi R., Iyer S.P., Ellies L.G., O'Donnell N., Marek K.W., Chui D., et al. The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny. Proceedings of the National Academy of Sciences of the United States of America 2000, 97:5735-5739.
132. Shan X., Vocadlo D.J., Krieger C. Reduced protein O-glycosylation in the nervous system of the mutant SOD1 transgenic mouse model of amyotrophic lateral sclerosis. Neuroscience Letters 2012, 516:296-301.
133. Sharma K., D'Souza R.C., Tyanova S., Schaab C., Wisniewski J.R., Cox J., et al. Ultradeep human phosphoproteome reveals a distinct regulatory nature of Tyr and Ser/Thr-based signaling. Cell Reports 2014, 8:1583-1594.
134. Sheldon W.L., Macauley M.S., Taylor E.J., Robinson C.E., Charnock S.J., Davies G.J., et al. Functional analysis of a group A streptococcal glycoside hydrolase Spy1600 from family 84 reveals it is a beta-N-acetylglucosaminidase and not a hyaluronidase. The Biochemical Journal 2006, 399:241-247.
135. Shi Y., Tomic J., Wen F., Shaha S., Bahlo A., Harrison R., et al. Aberrant O-GlcNAcylation characterizes chronic lymphocytic leukemia. Leukemia 2010, 24:1588-1598.
136. Shin S.H., Love D.C., Hanover J.A. Elevated O-GlcNAc-dependent signaling through inducible mOGT expression selectively triggers apoptosis. Amino Acids 2011, 40:885-893.
137. Singh J.P., Zhang K., Wu J., Yang X. O-GlcNAc signaling in cancer metabolism and epigenetics. Cancer Letters 2015, 356(2):244-250.
138. Slawson C., Copeland R.J., Hart G.W. O-GlcNAc signaling: A metabolic link between diabetes and cancer?. Trends in Biochemical Sciences 2010, 35:547-555.
139. Solary E., Bernard O.A., Tefferi A., Fuks F., Vainchenker W. The Ten-Eleven Translocation-2 (TET2) gene in hematopoiesis and hematopoietic diseases. Leukemia 2014, 28:485-496.
140. Speakman C.M., Domke T.C., Wongpaiboonwattana W., Sanders K., Mudaliar M., van Aalten D.M., et al. Elevated O-GlcNAc levels activate epigenetically repressed genes and delay mouse ESC differentiation without affecting naive to primed cell transition. Stem Cells (Dayton, Ohio) 2014, 32:2605-2615.
141. Starska K., Forma E., Brzezinska-Blaszczyk E., Lewy-Trenda I., Brys M., Jozwiak P., et al. Gene and protein expression of O-GlcNAc-cycling enzymes in human laryngeal cancer. Clinical and Experimental Medicine 2014, 10.1007/s10238-014-0318-1.
142. Steentoft C., Vakhrushev S.Y., Joshi H.J., Kong Y., Vester-Christensen M.B., Schjoldager K.T., et al. Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology. The EMBO Journal 2013, 32:1478-1488.
143. Steentoft C., Vakhrushev S.Y., Vester-Christensen M.B., Schjoldager K.T., Kong Y., Bennett E.P., et al. Mining the O-glycoproteome using zinc-finger nuclease-glycoengineered SimpleCell lines. Nature Methods 2011, 8:977-982.
144. Tai H.C., Khidekel N., Ficarro S.B., Peters E.C., Hsieh-Wilson L.C. Parallel identification of O-GlcNAc-modified proteins from cell lysates. Journal of the American Chemical Society 2004, 126:10500-10501.
145. Tan E.P., Villar M.T., Lezi E., Lu J., Selfridge J.E., Artigues A., et al. Altering O-linked beta-N-acetylglucosamine cycling disrupts mitochondrial function. The Journal of Biological Chemistry 2014, 289(21):14719-14730.
146. Taylor R.P., Parker G.J., Hazel M.W., Soesanto Y., Fuller W., Yazzie M.J., et al. Glucose deprivation stimulates O-GlcNAc modification of proteins through up-regulation of O-linked N-acetylglucosaminyltransferase. The Journal of Biological Chemistry 2008, 283:6050-6057.
147. Toleman C., Paterson A.J., Whisenhunt T.R., Kudlow J.E. Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities. The Journal of Biological Chemistry 2004, 279:53665-53673.
148. Torres C.R., Hart G.W. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. The Journal of Biological Chemistry 1984, 259:3308-3317.
149. Trinidad J.C., Barkan D.T., Gulledge B.F., Thalhammer A., Sali A., Schoepfer R., et al. Global identification and characterization of both O-GlcNAcylation and phosphorylation at the murine synapse. Molecular & Cellular Proteomics: MCP 2012, 11:215-229.
150. Trinidad J.C., Schoepfer R., Burlingame A.L., Medzihradszky K.F. N- and O-glycosylation in the murine synaptosome. Molecular & Cellular Proteomics: MCP 2013, 12:3474-3488.
151. Vella P., Scelfo A., Jammula S., Chiacchiera F., Williams K., Cuomo A., et al. Tet proteins connect the O-linked N-acetylglucosamine transferase Ogt to chromatin in embryonic stem cells. Molecular Cell 2013, 49:645-656.
152. Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A., Lynn A.J., et al. O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry. Molecular & Cellular Proteomics: MCP 2006, 5:923-934.
153. Wang Z.V., Deng Y., Gao N., Pedrozo Z., Li D.L., Morales C.R., et al. Spliced X-box binding protein 1 couples the unfolded protein response to hexosamine biosynthetic pathway. Cell 2014, 156:1179-1192.
154. Wang S., Huang X., Sun D., Xin X., Pan Q., Peng S., et al. Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates Akt signaling. PLoS One 2012, 7:e37427.
155. Wang Z., Pandey A., Hart G.W. Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation. Molecular & Cellular Proteomics: MCP 2007, 6:1365-1379.
156. Wang Z., Udeshi N.D., Slawson C., Compton P.D., Sakabe K., Cheung W.D., et al. Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis. Science Signaling 2010, 3:ra2.
157. Webster D.M., Teo C.F., Sun Y., Wloga D., Gay S., Klonowski K.D., et al. O-GlcNAc modifications regulate cell survival and epiboly during zebrafish development. BMC Developmental Biology 2009, 9:28.
158. Weigert C., Klopfer K., Kausch C., Brodbeck K., Stumvoll M., Haring H.U., et al. Palmitate-induced activation of the hexosamine pathway in human myotubes: Increased expression of glutamine:fructose-6-phosphate aminotransferase. Diabetes 2003, 52:650-656.
159. Wells L., Gao Y., Mahoney J.A., Vosseller K., Chen C., Rosen A., et al. Dynamic O-glycosylation of nuclear and cytosolic proteins: Further characterization of the nucleocytoplasmic beta-N-acetylglucosaminidase, O-GlcNAcase. The Journal of Biological Chemistry 2002, 277:1755-1761.
160. Whelan S.A., Lane M.D., Hart G.W. Regulation of the O-linked beta-N-acetylglucosamine transferase by insulin signaling. The Journal of Biological Chemistry 2008, 283:21411-21417.
161. Whisenhunt T.R., Yang X., Bowe D.B., Paterson A.J., Van Tine B.A., Kudlow J.E. Disrupting the enzyme complex regulating O-GlcNAcylation blocks signaling and development. Glycobiology 2006, 16:551-563.
162. Yang W.H., Kim J.E., Nam H.W., Ju J.W., Kim H.S., Kim Y.S., et al. Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability. Nature Cell Biology 2006, 8:1074-1083.
163. Yang X., Ongusaha P.P., Miles P.D., Havstad J.C., Zhang F., So W.V., et al. Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance. Nature 2008, 451:964-969.
164. Yang Y.R., Song M., Lee H., Jeon Y., Choi E.J., Jang H.J., et al. O-GlcNAcase is essential for embryonic development and maintenance of genomic stability. Aging Cell 2012, 11:439-448.
165. Yang X., Zhang F., Kudlow J.E. Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: Coupling protein O-GlcNAcylation to transcriptional repression. Cell 2002, 110:69-80.
166. Yehezkel G., Cohen L., Kliger A., Manor E., Khalaila I. O-linked beta-N-acetylglucosaminylation (O-GlcNAcylation) in primary and metastatic colorectal cancer clones and effect of N-acetyl-beta-d-glucosaminidase silencing on cell phenotype and transcriptome. The Journal of Biological Chemistry 2012, 287:28755-28769.
167. Yi W., Clark P.M., Mason D.E., Keenan M.C., Hill C., Goddard W.A., et al. Phosphofructokinase 1 glycosylation regulates cell growth and metabolism. Science (New York, NY) 2012, 337:975-980.
168. Ying H., Kimmelman A.C., Lyssiotis C.A., Hua S., Chu G.C., Fletcher-Sananikone E., et al. Oncogenic Kras maintains pancreatic tumors through regulation of anabolic glucose metabolism. Cell 2012, 149:656-670.
169. Yuzwa S.A., Macauley M.S., Heinonen J.E., Shan X., Dennis R.J., He Y., et al. A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo. Nature Chemical Biology 2008, 4:483-490.
170. Yuzwa S.A., Shan X., Jones B.A., Zhao G., Woodward M.L., Li X., et al. Pharmacological inhibition of O-GlcNAcase (OGA) prevents cognitive decline and amyloid plaque formation in bigenic tau/APP mutant mice. Molecular Neurodegeneration 2014, 9:42.
171. Zachara N.E., O'Donnell N., Cheung W.D., Mercer J.J., Marth J.D., Hart G.W. Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress. A survival response of mammalian cells. The Journal of Biological Chemistry 2004, 279:30133-30142.
172. Zafir A., Readnower R., Long B.W., McCracken J., Aird A., Alvarez A., et al. Protein O-GlcNAcylation is a novel cytoprotective signal in cardiac stem cells. Stem Cells (Dayton, OH) 2013, 31:765-775.
173. Zhang S., Roche K., Nasheuer H.P., Lowndes N.F. Modification of histones by sugar beta-N-acetylglucosamine (GlcNAc) occurs on multiple residues, including histone H3 serine 10, and is cell cycle-regulated. The Journal of Biological Chemistry 2011, 286:37483-37495.
174. Zhu Q., Zhou L., Yang Z., Lai M., Xie H., Wu L., et al. O-GlcNAcylation plays a role in tumor recurrence of hepatocellular carcinoma following liver transplantation. Medical Oncology (Northwood, London, England) 2012, 29:985-993.