Nuclear and cytoplasmic glycosylation

International Review of Cytology

Volumn 181, Issue , 1998, Pages 43-74

  Snow, Doris M ^a   Hart, Gerald W ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Glycosylation; N acetylglucosamine; O GlcNac; Phosphorylation

Indexed keywords

CYTOSKELETON PROTEIN; HEAT SHOCK PROTEIN; HYDROXYL GROUP; NUCLEOPORIN; RNA POLYMERASE II; SERINE; THREONINE; TRANSCRIPTION FACTOR; VIRUS PROTEIN;

CELL NUCLEUS; CYTOPLASM; HUMAN; NONHUMAN; ONCOGENE; PRIORITY JOURNAL; PROTEIN GLYCOSYLATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; REVIEW; TUMOR SUPPRESSOR GENE;

EID: 0031956040     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0074-7696(08)60416-7     Document Type: Review

References (151)

1. Akey, C. W. (1992). The nuclear pore complex. Citrr. Opin. Struct. Dial. 2, 258-263.
2. Akey, C. W., and Goldfarb, D. S. (1989). Protein import through the nuclear pore complex is a multistep process. J. Cell Biol. 109, 971-982.
3. Akey, C. W., and Radermacher, M. (1993). Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy. J. Cell Biol. 122, 1-19.
4. Arnold, C. S., Johnson, G. V., Cole, R. N., Dong, D., Lee, M., and Hart, G. W. (1996). The microtubule-associated protein tau is extensively modified with O-linked N-acetylglucos-amine. J. Biol. Chem. 271, 28741-28744.
5. Auger, D., Bounelis, P., and Marchase, R. B. (1993). Phosphoglucomutase is a cytoplasmic glycoprotein implicated in the regulated secretory pathway. In "Molecular Mechanisms of Membrane Traffic" (D. J. Morre, K. E. Howell, and J. J. M. Bergeron, eds.), NATO ASI Series H, Vol. 74, pp. 289-292.
6. Barker, R., Olsen, K. W., Shaper, J. H., and Hill, R. L. (1972). Agarose derivatives of uridine diphosphate and N-acetylglucosamine for the purification of a galactosyltransferase. J. Biol. Chem. 247, 7135-7147.
7. Chakraborty, A., Saha, D., Bose, A., Chatterjee, M., and Gupta, N. K. (1994). Regulation of eIF-2 alpha-subunit phosphorylation in reticulocyte lysate. Biochemistry 33, 6700-6706.
8. Chou, C.F., and Omary, M. B. (1994). Mitotic arrest with anti-microtubule agents or okadaic acid is associated with increased glycoprotein terminal GlcNAc's./. Cell Sci. 107,1833-1843.
9. Chou, C.-F., and Omary, M. B. (1993). Mitotic arrest-associated enhancement of O-linked glycosylation and phosphorylation of human keratins 8 and 18.7. Biol. Chem. 268,4465-4472.
10. Chou, C.-F., Smith, A. J., and Omary, M. B. (1992). Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18. J. Biol. Chem. 267, 3901-3906.
11. Chou, T.-Y., Dang, C. V., and Hart, G. W. (1995a). Glycosylation of the c-Myc transactivation domain. Proc. Natl. Acad. Sci. USA 92, 4417-4421.
12. Chou, T.-Y., Hart, G. W., and Dang, C. V. (1995b). c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas. J. Biol. Chem. 270 (32), 18961-18965.
13. Cole, R. N., and Hart, G. W. (1997). O-GlcNAc glycosylation sites bracket phosphorylation sites in synapsin I. Submitted for publication.
14. Coer, F. L, and Hart, G. W. (1996). Investigating the role of O-GlcNAc on RNA polymerase II. FASEB J. 10, A1119.
15. Cordes, V., Waizenegge, R. I., and Krohne, G. (1991). Nuclear pore complex glycoprotein p62 of Xenopus laevis and mouse: cDNA cloning and identification of its glycosylated region. Enr. J. Cell Biol. 55, 31-47.
16. Cordes, V. C, and Krohne, G. (1993). Sequential O-glycosylation of nuclear pore complex protein gp62 in vitro. Eur. J. Cell Biol. 60, 185-195.
17. Daniels, M. C, Kansal, P., Smith, T. M., Paterson, A. J., Kudlow, J. E., and McCIain, D. A. (1993). Glucose regulation of transforming growth factor-alpha expression is mediated by products of the hexosamine biosynthesis pathway. Mol. Endocrinol. 7, 1041-1048.
18. Daniels, M. C, Ciaraldi, T. P., Nikoulina, S., Henry, R. R., and McCIain, D. A. (1996). Glutamine:fructose-6-phosphate amidotransferase activity in cultured human skeletal muscle cells: Relationship to glucose disposal rate in control and non-insulin-dependent diabetes mellitus subjects and regulation by glucose and insulin. J. Clin. Invest. 97, 1235-1241.
19. Datta, B., Chakrabarti, D., Roy, A. L., and Gupta, N. K. (1988). Roles of a 67-kDa polypeptide in reversal of protein synthesis inhibition in heme-deficient reticulocyte lysate. Proc. Natl. Acad. Sci. USA 85, 3324-3328.
20. 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.
21. Davis, L. I., and Blobel, G. (1986). Identification and characterization of a nuclear pore complex protein. Cell 45, 699-709.
22. Dieckmann-Schuppert, A., Bause, E., and Schwarz, R. T. (1993). Studies on O-glycans of Plasmodium-falciparum-infected human erythrocytes. Evidence for O-GlcNAc and O-GlcNAc-transferase in malaria parasites. Ear. J. Biochem. 216, 779-788.
23. Ding, M., and Vandre, D. D. (1996). High molecular weight microtubule-associated proteins contain O-Iinked-N-acetylglucosamine. J. Biol. Chem. 271, 12555-12561.
24. Dong, D. L., and Hart, G. W. (1994). Purification and characterization of an O-GlcNAc Selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol. J. Biol. Chem. 269, 19321-19330.
25. Dong, D. L., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993). Glycosylation of mammalian neurofilaments. Localization of multiple O-linked N-acetyglucosamine moieties on neurofilament polypeptides L and M. J. Biol. Chem. 268, 16679-16687.
26. Dong, D. L., Xu, Z. S., Hart, G. W., and Cleveland, D. W. (1996). Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H. J. Biol. Chem. 271, 20845-20852.
27. D'Onofrio, M., Starr, C. M., Park, M. K., Holt, G. D., Haltiwanger, R. S., Hart, G. W., and Hanover, J. A. (1988). Partial cDNA sequence encoding a nuclear pore protein modified by O-linked N-acetylglucosamine. Proc. Natl. Acad. Sci. USA 85, 9595-9599.
28. Duverger, E., Carpentier, V., Roche, A.-C, and Monsigny, M. (1993). Sugar-dependent nuclear import of glycoconjugates from the cytosol. Exp. Cell Res. 207, 197-201.
29. Duverger, E., Pellerin-Mendes, C., Mayer, R., Roche, A.-C., and Monsigny, M. (1995). Nuclear import of glycoconjugates is distinct from the classical NLS pathway. J. Cell Sci. 108,1325-1332.
30. Duverger, E., Roche, A.-C., and Monsigny, M. (1996). N-acetylglucosamine-dependent nuclear import of neoglycoproteins. Glycobiology 6, 381-386.
31. Featherstone, C., Darby, M. K., and Gerace, L. (1988). A monoclonal antibody against the nuclear pore complex inhibits nucleocytoplasmic transport of protein and RNA in vivo. J. Cell Biol. 107, 1289-1297.
32. Finlay, D. R., and Forbes, D. J. (1990). Reconstitution of biochemically altered nuclear pores: Transport can be eliminated and restored. Cell 60, 17-29.
33. Finlay, D. R., Newmeyer, D. D., Price, T. M., and Forbes, D. J. (1987). Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores. J. Cell Biol. 104, 189-200.
34. Finlay, D. R., Meier, E., Bradley, P., Horecka, J., and Forbes, D. J. (1991). A complex of nuclear pore proteins required for pore function. J. Cell Biol. 114, 169-183.
35. Forbes, D. J. (1992). Structure and function of the nuclear pore complex. Annu. Rev. Cell Biol. 8, 495-527.
36. Fu, L., Bounelis, P., Dey, N., Browne, B. L., Marchase, R. B., and Bedwell, D. M. (1995). The posttranslational modification of phosphoglucomutase is regulated by galactose induction and glucose repression in Saccharomyces cerevisiae. J. Bacterial. 177, 3087-3094.
37. Gabel, C. A., Den, H., and Ambron, R. T. (1989). Characterization of protein-linked glycoconjugates produced by identified neurons of Aplysia californica. J. Neurobiol. 20, 530-548.
38. Goebl, M., and Yanagida, M. (1991). The TPR snap helix: A novel protein repeat motif from mitosis to transcription. Trends Biochem. Sci. 16, 173-177.
39. Gonzalez, S. A., and Burrone, O. R. (1991). Rotavirus NS26 is modified by addition of single O-linked residues of Af-acetylglucosamine. Virology 182, 8-16.
40. Gonzalez-Yanes, B., Cicero, J. M., Brown, R. D., and West, C. M. (1992). Characterization of a cytosolic fucosylation pathway in Dictyostelium. J. Biol. Chem. 267, 9595-9605.
41. Gowda, D. C., Gupta, P., and Davidson, E. A. (1997). Glycosylphosphatidylinositol anchors represent the major carbohydrate modification in proteins of intraerythrocytic stage Plasmodium falciparum. J. Biol. Chem. 272, 6428-6439.
42. Greis, K. D., and Hart, G. W. (1995). Nuclear and cytosolic glycoproteins. In "Glycoproteins" ( J. Monstreuil, H. Schachter, and J. F. G. Vliegenthart, eds.), Vol. II., in press. Eisevier, Amsterdam.
43. Greis, K. D., Gibson, W., and Hart, G. W. (1994). Site-specific glycosylation of the human cytomegalovirus tegument basic phosphoprotein (UL32) at serine 921 and serine 952. J. Virol. 68, 8339-8349.
44. Greis, K. D., Hayes, B. K., Corner, F. L, Kirk, M., Barnes, S., Lowary, T. L., and Hart, G. W. (1996). Selective detection and site-analysis of O-GlcNAc-modified glycopeptides by beta-elimination and tandem electrospray mass spectrometry. Anal. Biochem. 23-4,38-49.
45. Griffith, L. S., and Schmilz, B. (1995). O-linked N-acetylglucosamine is upregulated in Alzheimer brains. Biochem. Biophys. Res. Commun. 213, 424-431.
46. Griffith, L. S., Mathes, M., and Schmilz, B. (1995). Beta-amyloid precursor protein is modified with O-linked N-acetylglucosamine. J. Neurosci. Res. 41, 270-278.
47. Gupta, N. K. (1996). Mammalian peptide chain initiation: Thirty years of research. Ind. J. Biochem. Biophys. 33, 239-252.
48. Hagmann, J., Grob, M., and Burger, M. M. (1992). The cytoskeletal protein talin is O-glycosylaled. J. Biol. Chem. 267, 14424-14428.
49. Haltiwanger, R. S., and Philipsberg, G. A. (1997). Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosaine and accumulation of incompletely processed N-glycans on proteins from HT29 cells. J. Biol. Chem. 272, 8752-8758.
50. Haltiwanger, R. S., Blomberg, M. A., and Hart, G. W. (1992a). 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.
51. Haltiwanger, R. S., Kelly, W. G., Roquemore, E. P., Blomberg, M. A., Dong, L.-Y. D., Kreppel, L., Chou, T.-Y., and Hart, G. W. (1992b). Glycosylation of nuclear and cytoplasmic proteins is ubiquitous and dynamic. Biochem. Soc. Trans. 20, 264-269.
52. Handman, E., Barnett, L. D., Osborn, A. H., Coding, J. W., and Murray, P. J. (1993). Identification, characterisation and genomic cloning of a O-linked N-acetylglucosaminecontaining cytoplasmic Leishmania glycoprotein. Mol. Biochem. Parasitai. 62, 61-72.
53. Hanover, J. A. (1992). The nuclear pore: At the crossroads. FASEB J. 6, 2288-2295.
54. Hart, G. W. (1997). Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins. Anna. Rev. Biochem. 66, 315-335.
55. Hart, G. W., Haltiwanger, R. S., Holt, G. D., and Kelly, W. G. (1989). Glycosylation in the nucleus and cytoplasm. Anna. Rev. Biochem. 58, 841-874.
56. Hart, G. W., Greis, K. D., Dong, L. Y. D., Blomberg, M. A., Chou, T. Y., Jiang, M. S., Roquemore, E. P., Snow, D. M., et al. (1995). O-linked N-acetylglucosamine: The "yinyang" of ser/thr phosphorylation? Nuclear and cytoplasmic glycosylation. Adv. Exp. Med. Biol. 376, 115-123.
57. Hart, G. W., Kreppel, L. K., Corner, F. I., Arnold, C. S., Snow, D. M., Ye, Z., Cheng, X., DellaManna, D., et al. (1996). O-GlcNAcylation of key nuclear and cytoskeletal proteins: Reciprocity with O-phosphorylation and putative roles in protein multimerization. Glycobiology 6, 711-716.
58. Hayes, B. K., Greis, K. D., and Hart, G. W. (1995). Specific isolation of O-linked N-acetylglucosamine glycopeptides from complex mixtures. Anal. Biochem. 228, 115-122.
59. Hiscock, D. R., Yanagishita, M., and Hascall, V. C. (1994). Nuclear localization of glycosaminoglycans in rat ovarian granulosa cells. J. Biol. Chem. 269, 4539-4546.
60. Holt, G. D., Hart, G. W., et al. (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.
61. Holt, G. D., Haltiwanger, R. S., Torres, C. R., and Hart, G. W. (1987a). Erythrocytes contain cytoplasmic glycoproteins. O-linked GlcNAc on Band 4.1. J. Biol. Chem. 262,14847-14850.
62. Holt, G. D., Snow, C. M., Senior, A., Haltiwanger, R. S., Gerace, L., and Hart, G. W. (1987b). Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked Nacetylglucosamine. J. Cell Biol. 104, 1157-1164.
63. Hounsell, E. F., Davies, M. J., and Renouf, D. V. (1996). O-linked protein glycosylation structure and function. Glycoconj. J. 13, 19-26.
64. Inaba, M., and Maede, Y. (1989). O-N-acetyl-o-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways. J. Biol. Client. 264,18149-18155.
65. Ishihara, M., Fedarko, N. S., and Conrad, H. E. (1986). Transport of heparan sulfate into the nuclei of hepatocytes. J. Biol. Chem. 261, 13575-13580.
66. Jackson, S. P., and Tjian, R. (1988). O-glycosylation of eukaryotic transcription factors: Implications for mechanisms of transcriptional regulation. Cell 55, 125-133.
67. Jackson, S. P., and Tjian, R. (19S9). Purification and analysis of RNA polymerase II transcription factors by using wheat germ agglutinin affinity chromatography. Proc. Natl. Acad. Sci. USA 86, 1781-1785.
68. Jacobsen, S. E., Binkowski, K. A., and Olszewski, N. E. (1996). SPINDLY, a tetratricopeptide repeat protein involved in gibberellin signal transduction in Arabidopsis. Proc. Natl. Acad. Sci. USA 93, 9292-9296.
69. Jiang, M., and Hart, G. W. (1997). A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine. J. Biol. Chem. 272, 2421-2428.
70. Just, I., Selzer, J., Wilm, M., von Eichel-Streiber, C, Mann, M., and Aktories, K. (1995a). Glucosylation of Rho proteins by Clostridium difficile toxin B. Nature 375, 500-503.
71. Just, I., Wilm, M., Selzer, J., Rex, G., von Eichel-Streiber, C, Mann, M., and Aktories, K. (1995b). The enterotoxin from Clostridium difficile (ToxA) monoglucosylates the Rho proteins. J. Biol. Chem. 270, 13932-13936.
72. Kadonaga J. T., Courey, A. J., Ladika, J., and Tjian, R. (1988). Distinct regions of Sp1 modulate DNA binding and transcriptional activation. Science 242, 1566-1570.
73. Kaufman, R. J. (1994). Control of gene expression at the level of translation initiation. Citrr. Opin. Biotechnol. 5, 550-557.
74. Kearse, K. P., and Hart, G. W. (1991a). Lymphocyte activation induces rapid changes in nuclear and cytoplasmic glycoproteins. Proc. Natl. Acad. Sci. USA 88, 1701-1705.
75. Kearse, K. P., and Hart, G. W. (1991b). Topology of O-linked W-acetylglucosamine in murine lymphocytes. Arch. Biochem. Biophys. 290, 543-548.
76. 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.
77. Kelly, W. G., Dahmus, M. E., and Hart, G. W. (1993). RNA polymerase II is a glycoprotein. Modification of the COOH-terminal domain by O-GlcNAc./. Biol. Chem. 268,10416-10424.
78. Kelly, W. G., Roquemore, E. P., and Hart, G. W. (1994). Cell-cycle-dependent changes in nuclear glycosylation. Submitted for publication.
79. King, I. A., and Hounsell, E. F. (1989). Cytokeratin 13 contains O-glycosidically linked N-acetylglucosamine residues. J. Biol. Chem. 264,14022-14028.
80. Kornfeld, R., and Kornfeld, S. (1985). Assembly of asparagine-linked oligosaccharides. Anna. Rev. Biochem. 54, 631-664.
81. Kraemer, D., Wozniak, R. W., Blobel, G., and Radu, A. (1994). The human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm. Proc. Natl. Acad. Sci. USA 91, 1519-1523.
82. 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-GIcNAc transferase with multiple tetratricopeptide repeats. J. Biol. Chem. 272, 9308-9315.
83. Krusius, T., Finne, J., Margolis, R. K., and Margolis, R. U. (1986). Identification of an O-glycosidic mannose-linked sialylated tetrasaccharide and kcratan sulfate oligosaccharides in the chondroitin sulfate proteoglycan of brain. J. Biol Chem. 261, 8237-8242.
84. Krusius, T., Reinhold, V. N., Margolis, R. K., and Margolis, R. U. (1987). Structural studies on sialylated and sulphated O-glycosidic mannose-linked oligosaccharides in the chondroitin sulphate proteoglycan of brain. Biochem. J. 245, 229-234.
85. Ku, N.-O., and Omary, M. B. (1995). Identification and mutational analysis of the glycosylation sites of human keratin 18. J. Biol. Chem. 270, 11820-11827.
86. Lamb, J. R-. Tugendreich, S., and Mieter, P. (1995). Tetratrico peptide repeat interactions: To TPR or not to TPR? Trends Biochcm. Sci. 20, 257-259.
87. Levenson, A. S., and Jordan, V. C. (1994). Transfection of human estrogen receptor (ER) cDNA into ER-negative mammalian cell lines. J. Steroid Biochem. Mol. Biol. 51,229-239.
88. Lorenzi, M. (1992). Glucose toxicity in the vascular complications of diabetes: The cellular perspective. Diabetes Metab. Rev. 8, 85-103.
89. 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. Cliem. 272, 9316-9324.
90. Luthi, T., Haltiwanger, R. S., Greengard, P., and Bahler, M. (1991). Synapsins contain O-linked N-acetylglucosamine. J. Neitrochem. 56, 1493-1498.
91. Macaulay, C., Meier, E., and Forbes, D. J. (1995). Differential mitotic phosphorylation of proteins of the nuclear pore complex. J. Biol. Chem. 270, 254-262.
92. Mandelkow, E. M., and Mandelkow, E. (1993). Tau as a marker for Alzheimer's disease. Trends Biochem. Sci. 18, 480-483.
93. Mandelkow, E. M., Biernat, J., Drewes, G., Steiner, B., Lichtenberg-Kraag, B., Wille, H., Gustke, N., and Mandelkow, E. (1993). Microtubule-associated protein tau, paired helical filaments, and phosphorylation. Ann. NY Acad. Sci. 695, 209-216.
94. Marshall, S., Bacote, V., and Traxinger, R.R. (1991a). 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. Cliem. 266, 4706-4712.
95. Marshall, S., Garvey, W. T., and Traxinger, R. R. (1991b). New insights into the metabolic regulation of insulin action and insulin resistance: Role of glucose and amino acids. FASEB J. 5, 3031-3036.
96. McClain, D. A., and Crook, E. D. (1996). Hexosamines and insulin resistance. Diabetes 45, 1003-1009.
97. McClain, D. A., Paterson, A. J., Roos, M. D., Wei, X., and Kudlow, J. E. (1992). Glucose and glucosamine regulate growth factor gene expression in vascular smooth muscle cells. Proc. Natl. Acad. Sci. USA 89, 8150-8154.
98. Medina-Vera, L., and Haltiwanger, R. S. (1994). SV40 large T antigen is modified with O-linked N-acetylglucosamine. Mol. Biol. Cell 5 (S), 340a.
99. Meikrantz, W., Smith, D. M., Sladicka, M. M., and Schlegel, R. A. (1991). Nuclear localization of an O-glycosylated protein phosphotyrosine phosphatase from human cells. J. Cell Sci. 98, 303-307.
100. Miksicek, R. J. (1994). Steroid receptor variants and their potential role in cancer. Semin. Cancer Biol. 5, 369-379.
101. Miller, M. W., and Hanover, J. A. (1994). Functional nuclear pores reconstituted with betal-4 galactose-modified O-linked N-acetylglucosamine glycoproteins.y. Biol. Chem. 269,9289-9297.
102. Monsigny M., Roche, A. C., Sene, C., Maget-Dana, R., and Delmotte, F. (1980). Sugar-lectin interactions: How does wheat-germ agglutinin bind sialoglycoconjugates? Eur. J. Biochem. 104, 147-153.
103. Morley, S. J. (1994). Signal transduction mechanisms in the regulation of protein synthesis. Mol. Biol. Rep. 19, 221-231.
104. Mullis, K. G., Haltiwanger, R. S., Hart, G. W., Marchase, R. B., and Engler, J. A. (1990). Relative accessibility of N-acetylglucosamine in trimers of the adenovirus types 2 and 5 fiber proteins. J. Virol. 64, 5317-5323.
105. Murphy, J. E., Hanover, J. A., Froehlich, M., DuBois, G., and Keen, J. H. (1994). Clathrin assembly protein AP-3 is phosphorylated and glycosylated on the 50-kDa structural domain. J. Biol. Chem. 269, 21346-21352.
106. Newmeyer, D. D., and Forbes, D. J. (1988). Nuclear import can be separated into distinct steps in vitro: Nuclear pore binding and translocation. Cell 52, 641-653.
107. Nyame, K., Cummings, R. D., and Damian, R. T. (1987). Schistosoma mansoni synthesizes glycoproteins containing terminal O-linked N-acetylglucosamine residues. J. Biol. Chem. 262, 7990-7995.
108. Pain, V. m. (1996). Initiation of protein synthesis in eukaryotic cells. Eiir. J. Biochem. 236, 747-771.
109. Pante, N., Bastos, R., McMorrow, L, Burke, B., and Aebi, U. (1994). Interactions and three-dimensional localization of a group of nuclear pore complex proteins. J. Cell Biol. 126, 603-617.
110. Park, M. K., D'Onofrio, M., Willingham, M. C, and Hanover, J. A. (1987). A monoclonal antibody against a family of nuclear pore proteins (nucleoporins): O-linked N-acetylglucos-amine is part of the immunodeterminant. Proc. Natl. Acad. Sci. USA 84, 6462-6466.
111. Petrangeli, E., Lubrano, C, Ortolani, F., Ravenna, L., Vacca, A., Sciacchitano, S., Frati, L., and Gulino, A. (1994). Estrogen receptors: New perspectives in breast cancer management. J. Steroid Biochem. Mol. Biol. 49, 327-331.
112. Privalsky, M. L. (1990). A subpopulation of the avian erythroblastosis virus v-erbA protein, a member of the nuclear hormone receptor family, is glycosylated. J. Virol. 64, 463-466.
113. Ray, M. K., Datta, B., Chakraborty, A., Chattopadhyay, A., Meza-Keuthen, S., and Gupta, N. K. (1992). The eukaryotic initiation factor 2-associated 67-kDa polypeptide (p67) plays a critical role in regulation of protein synthesis initiation in animal cells. Proc. Natl. Acad. Sci. USA 89, 539-543.
114. Reason, A. J., Morris, H. R., Panico, M., Marais, R., Treisman, R. H., Haltiwanger, R. S., Hart, G. W., Kelly, W. G., et al. (1992). Localization of O-GIcNAc modification on the serum response transcription factor. J. Biol. Cliem. 267 (24), 16911-16921.
115. Rechsteiner, M., and Rogers, S. W. (1996). PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21, 267-271.
116. Ridley, A. J., and Hall, A. (1992). The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70, 389-399.
117. Rihs, H. P., and Peters, R. (19S9). Nuclear transport kinetics depend on phosphorylation-site-containing sequences flanking the karyophilic signal of the simian virus 40 T-antigen. EMBO J. S, 1479-1484.
118. Rihs, H. P., Jans, D. A., Fan, H., and Peters, R. (1991). The rate of nuclear cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T-antigen. EMBO J. 10, 633-639.
119. Roquemore, E. P., Dell, A., Morris, H. R., Panico, M., Reason, A. J., Savoy, L. A., Wistow, G. J., Zigler, J. S., Jr., et al. (1992). Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine. J. Biol. Chem. 267, 555-563.
120. Roquemore, E. P., Chou, T.-Y., and Hart, G. W. (1994). Detection of O-linked W-Acetylglucosamine (O-GlcNAc) on cytoplasmic and nuclear proteins. Methods Enzymol. 230,443-460.
121. Roquemore, E. P., Chevrier, M. R., Cotter, R., and Hart, G. W. (1996). Dynamic O-GlcNAcyla-tion of the small heat shock protein alpha B-crystallin. Biochemistry 35, 3578-3586.
122. Rossetti, L. (1995). Glucose toxicity: The implications of hyperglycemia in the pathophysiology of diabetes mellitus. Clin. Invest. Med. 18, 255-260.
123. Sayeski, P. P., and Kudlow, J. E. (1996). Glucose metabolism to glucosamine is necessary for glucose stimulation of transforming growth factor-alpha gene transcription. J. Biol. Chem. 271, 15237-15243.
124. Schaufele, F., West, B. L., and Reudelhuber, T. L. (1990). Overlapping Pit-1 and Spl binding sites are both essential to full rat growth hormone gene promoter activity despite mutually exclusive Pit-1 and Spl binding. J. Biol. Chem. 265, 17189-17196.
125. Selzer, J., Hofmann, F., Rex, G., Wilm, M., Mann, M., Just, I., and Aktories, K. (1996). Clostridium novyi alpha-toxin-catalyzed incorporation of GlcNAc into Rho subfamily proteins. J. Biol. Chem. 271, 25173-25177.
126. Shaw, P., Freeman, J., Bovey, R., and Iggo, R. (1996). Regulation of specific DNA binding by p53: Evidence for a role for O-glycosylation and charged residues at the carboxy-terminus. Oncogene 12, 921-930.
127. Skyler, J. S. (1996). Diabetic complications. The importance of glucose control. Endocrinol. Metab. Clin. North Am. 25, 243-254.
128. Smythe, C, and Cohen, P. (1991). The discovery of glycogenin and the priming mechanism for glycogen biogenesis. Eur. J. Biochem. 200, 625-631.
129. Snow, C. M., Senior A., and Gerace, L. (1987). Monoclonal antibodies identify a group of nuclear pore complex proteins. J. Cell Biol. 104, 1143-1156.
130. Snow, D. M., Shaper, J. H., Shaper, N. L., and Hart, G. W. (1995). Cytosolic galactosyltransfer-ase mediated capping of O-GlcNAc in CHO cells: A model to elucidate function. Mol. Biol. Cell 6, 357a.
131. Soulard, M., Barque, J.-P., Delle Valle, V., Hernandez-Verdun, D., Masson, C, Danon, F., and Larsen, C.-J. (1991). A novel 43-kDa glycoprotein is detected in the nucleus of mammalian cells by autoantibodies from dogs with autoimmune disorders. Exp. Cell Res. 193,59-71.
132. Soulard, M., Delia Valle, V., Siomi, M. C, Pinol-Roma, S., Codogno, P., Bauvy, C, Bellini, M., Lacroix, J. C, et al. (1993). hnRNP G: Sequence and characterization of a glycosylated RNA-binding protein. Nucleic Acids Res. 21, 4210-4217.
133. Stanley, S. L., Jr., Tian, K., Koester, J. P., and Li, E. (1995). The serine-rich Entamoeba histolytica protein is a phosphorylated membrane protein containing O-linked terminal N-acetylglucosamine residues. J. Biol. Client. 270, 4121-4126.
134. Starr, C. M., and Hanover, J. A. (1990). Glycosylation of nuclear pore protein p62. Reticulocyte lysatc catalyzes O-linked N-acetylglucosamine addition in vitro. J. Biol. Chem. 265, 6868-6873.
135. Starr, C. M., D'Onofrio, M., Park, M. K., and Hanover, J. A. (1990). Primary sequence and heterologous expression of nuclear pore glycoprotein p62. J. Cell Biol. 110, 1861-1871.
136. Steinert, P. M., and Roop; D. R. (1988). Molecular and cellular biology of intermediate filaments. Anntt. Rev. Biochem. 57, 593-625.
137. Strous, G. J., and Dekker, J. (1992). Mucin-type glycoproteins. Crit. Rev. Biochem. Mol. Biol. 27, 57-92.
138. Torres, C. R., and Hart, G. W. (1984). Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-GlcNAc. J. Biol. Chem. 259, 3308-3317.
139. Traxinger, R. R., and Marshall, S. (1989). Role of amino acids in modulating glucose-induced desensitization of the glucose transport system. J. Biol. Client. 264, 20910-20916.
140. 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. Bio!. Chem. 266, 10148-10154.
141. Trayer, I. P., and Hill, R. L. (1971). The purification and properties of the A protein of lactose synthetase. J. Biol. Chem. 246, 6666-6675.
142. Vojtek, A., and Cooper, J. A. (1995). Rho family members: Activators of MAP kinase cascades. Cell 82, 527-529.
143. Vostal, J. G., and Krasnewich, D. M. (1996). Dynamic O-linked N-acetylglucosamine glycosylation of platelet vinculin. Mol. Biol. Cell 5 (Suppl.), 263a.
144. Wang, J. L., Laing, J. G., and Anderson, R. L. (1991). Lectins in the cell nucleus. Glycobiology I, 243-252.
145. Wang, J. L., Werner, E. A., Laing, J. G., and Patterson, R. J. (1992). Nuclear and cytoplasmic localization of a lectin-ribonucleoprotein complex. Biochem. Soc. Trans. 20, 269-274.
146. Wek, R. C. (1994). elF-2 kinases: Regulators of general and gene-specific translation initiation. Trends Biochem. Sci. 19, 491-496.
147. Whitford, M., and Faulkner, P. (1992). A structural polypeptide of the baculovirus Autographa californica nuclear polyhedrosis virus contains O-linked N-acetylglucosamine. J. Virol. 66, 3324-3329.
148. Wolff, B., Willingham, M. C., and Hanover, J. A. (1988). Nuclear protein import: Specificity for transport across the nuclear pore. Exp. Cell Res. 178, 318-334.
149. Wu, S., Gupta, S., Chatterjee, N., Hileman, R. E., Kinzy, T. G., Denslow, N. D., Merrick, W. C, Chakrabarti, D., et al. (1993). Cloning and characterization of complementary DNA encoding the eukaryotic initiation factor 2-associated 67-kDa protein (p67). J. Biol. Cliem. 268, 10796.
150. Wu, S., Rehemtulla, A., Gupta, N. K., and Kaufman, R. J. (1996). A eukaryotic translation initiation factor 2-associated 67 kDa glycoprotein partially reverses protein synthesis inhibition by activated double-stranded RNA-dependent protein kinase in intact cells. Biochemistry 35, 8275-8280.
151. Zhang, X., and Bennett, V. (1996). Identification of O-linked N-acetylglucosamine modification of ankyrinG isoforms targeted to nodes of Ranvier. J. Biol. Cliem. 271, 31391-31398.