Glycosylation of the nuclear pore

Traffic

Volumn 15, Issue 4, 2014, Pages 347-361

  Li, Bin ^a   Kohler, Jennifer J ^a  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

Diazirine; FG repeat; Hexosamine; Huisgen cycloaddition; Nucleocytoplasmic transport; Nucleoporin; O GlcNAc; Photocrosslinking; Stress; Unstructured proteins

Indexed keywords

CYTOPLASM PROTEIN; GLYCINE; N ACETYLGLUCOSAMINE; PHENYLALANINE;

CELL CYCLE; CROSS LINKING; CYCLOADDITION; GLYCOSYLATION; NUCLEAR PORE; NUCLEOCYTOPLASMIC TRANSPORT; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEOMICS; REVIEW; SACCHAROMYCES CEREVISIAE; SCHIZOSACCHAROMYCES POMBE; METABOLISM;

ACETYLGLUCOSAMINE; GLYCOSYLATION; NUCLEAR PORE; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEOMICS;

EID: 84896704455     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/tra.12150     Document Type: Review

References (124)

1. Hart GW, Housley MP, Slawson C. Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins. Nature 2007;446:1017-1022.
2. 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-acetylglucosaminyltransferase. J Biol Chem 1990;265:2563-2568.
3. Dong DL, Hart GW. Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol. J Biol Chem 1994;269:19321-19330.
4. Vocadlo DJ. O-GlcNAc processing enzymes: catalytic mechanisms, substrate specificity, and enzyme regulation. Curr Opin Chem Biol 2012;16:488-497.
5. Olszewski NE, West CM, Sassi SO, Hartweck LM. O-GlcNAc protein modification in plants: evolution and function. Biochim Biophys Acta 1800;2010:49-56.
6. Shen A, Kamp HD, Gründling A, Higgins DE. A bifunctional O-GlcNAc transferase governs flagellar motility through anti-repression. Genes Dev 2006;20:3283-3295.
7. Selzer J, Hofmann F, Rex G, Wilm M, Mann M, Just I, Aktories K. Clostridium novyi alpha-toxin-catalyzed incorporation of GlcNAc into Rho subfamily proteins. J Biol Chem 1996;271:25173-25177.
8. Matsuura A, Ito M, Sakaidani Y, Kondo T, Murakami K, Furukawa K, Nadano D, Matsuda T, Okajima T. O-linked N-acetylglucosamine is present on the extracellular domain of Notch receptors. J Biol Chem 2008;283:1-10.
9. Sakaidani Y, Nomura T, Matsuura A, Ito M, Suzuki E, Murakami K, Nadano D, Matsuda T, Furukawa K, Okajima T. O-linked-N-acetylglucosamine on extracellular protein domains mediates epithelial cell-matrix interactions. Nat Commun 2011;2:583-589.
10. Wells L, Vosseller K, Hart GW. A role for N-acetylglucosamine as a nutrient sensor and mediator of insulin resistance. Cell Mol Life Sci 2003;60:222-228.
11. Love DC, Hanover JA. The hexosamine signaling pathway: deciphering the "O-GlcNAc Code". Sci STKE 2005;2005:re13.
12. Wellen KE, Thompson CB. A two-way street: reciprocal regulation of metabolism and signalling. Nat Rev Mol Cell Biol 2012;13:270-276.
13. Hanover JA, Krause MW, Love DC. Bittersweet memories: linking metabolism to epigenetics through O-GlcNAcylation. Nat Rev Mol Cell Biol 2012;13:312-321.
14. Bond MR, Hanover JA. O-GlcNAc cycling: a link between metabolism and chronic disease. Annu Rev Nutr 2013;33:205-229.
15. Chou T-Y, Hart GW, Dang CV. c-Myc Is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas. J Biol Chem 1995;270:18961-18965.
16. Cheng X, Hart GW. Alternative O-glycosylation/O-phosphorylation of serine-16 in murine estrogen receptor β: post-translational regulation of turnover and transactivation activity. J Biol Chem 2001;276:10570-10575.
17. Kelly WG, Dahmus ME, Hart GW. RNA polymerase II is a glycoprotein. Modification of the COOH-terminal domain by O-GlcNAc. J Biol Chem 1993;268:10416-10424.
18. Du XL, Edelstein D, Dimmeler S, Ju Q, Sui C, Brownlee M. Hyperglycemia inhibits endothelial nitric oxide synthase activity by posttranslational modification at the Akt site. J Clin Invest 2001;108:1341-1348.
19. Hahne H, Gholami AM, Kuster B. Discovery of O-GlcNAc-modified proteins in published large-scale proteome data. Mol Cell Proteomics 2012;11:843-850.
20. Wang J, Torii M, Liu H, Hart G, Hu Z-Z. dbOGAP - an integrated bioinformatics resource for protein O-GlcNAcylation. BMC Bioinformatics 2011;12:91.
21. Davis LI, Blobel G. Nuclear pore complex contains a family of glycoproteins that includes p62: glycosylation through a previously unidentified cellular pathway. Proc Natl Acad Sci U S A 1987;84:7552-7556.
22. Hanover JA, Cohen CK, Willingham MC, Park MK. O-linked N-acetylglucosamine is attached to proteins of the nuclear pore. Evidence for cytoplasmic and nucleoplasmic glycoproteins. J Biol Chem 1987;262:9887-9894.
23. Holt GD, Snow CM, Senior A, Haltiwanger RS, Gerace L, Hart GW. Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine. J Cell Biol 1987;104:1157-1164.
24. Snow CM, Senior A, Gerace L. Monoclonal antibodies identify a group of nuclear pore complex glycoproteins. J Cell Biol 1987;104:1143-1156.
25. Wang Z, Udeshi ND, Slawson C, Compton PD, Sakabe K, Cheung WD, Shabanowitz J, Hunt DF, Hart GW. Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis. Sci Signal 2010;3:ra2.
26. Favreau C, Worman HJ, Wozniak RW, Frappier T, Courvalin J-C. Cell cycle-dependent phosphorylation of nucleoporins and nuclear pore membrane protein Gp210. Biochemistry 1996;35:8035-8044.
27. Hallberg E, Wozniak R, Blobel G. An integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like region. J Cell Biol 1993;122:513-521.
28. Finlay DR, Newmeyer DD, Price TM, Forbes DJ. Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores. J Cell Biol 1987;104:189-200.
29. Vosseller K, Trinidad JC, Chalkley RJ, Specht CG, Thalhammer A, Lynn AJ, Snedecor JO, Guan S, Medzihradszky KF, Maltby DA, Schoepfer R, Burlingame AL. O-Linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry. Mol Cell Proteomics 2006;5:923-934.
30. Chalkley RJ, Thalhammer A, Schoepfer R, Burlingame AL. Identification of protein O-GlcNAcylation sites using electron transfer dissociation mass spectrometry on native peptides. Proc Natl Acad Sci U S A 2009;106:8894-8899.
31. Comer FI, Vosseller K, Wells L, Accavitti MA, Hart GW. Characterization of a mouse monoclonal antibody specific for O-linked N-acetylglucosamine. Anal Biochem 2001;293:169-177.
32. Teo CF, Ingale S, Wolfert MA, Elsayed GA, Nöt LG, Chatham JC, Wells L, Boons G-J. Glycopeptide-specific monoclonal antibodies suggest new roles for O-GlcNAc. Nat Chem Biol 2010;6:338-343.
33. Zachara N, Molina H, Wong K, Pandey A, Hart G. The dynamic stress-induced O-GlcNAc-ome" highlights functions for O-GlcNAc in regulating DNA damage/repair and other cellular pathways. Amino Acids 2011;40:793-808.
34. Wang Z, Pandey A, Hart GW. Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation. Mol Cell Proteomics 2007;6:1365-1379.
35. Vocadlo DJ, Hang HC, Kim EJ, Hanover JA, Bertozzi CR. A chemical approach for identifying O-GlcNAc-modified proteins in cells. Proc Natl Acad Sci U S A 2003;100:9116-9121.
36. Boyce M, Carrico IS, Ganguli AS, Yu S-H, Hangauer MJ, Hubbard SC, Kohler JJ, Bertozzi CR. Metabolic cross-talk allows labeling of O-linked β-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway. Proc Natl Acad Sci U S A 2011;108:3141-3146.
37. Zaro BW, Yang Y-Y, Hang HC, Pratt MR. Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1. Proc Natl Acad Sci U S A 2011;108:8146-8151.
38. Sprung R, Nandi A, Chen Y, Kim SC, Barma D, Falck JR, Zhao Y. Tagging-via-substrate strategy for probing O-GlcNAc modified proteins. J Proteome Res 2005;4:950-957.
39. Hahne H, Sobotzki N, Nyberg T, Helm D, Borodkin VS, van Aalten DMF, Agnew B, Kuster B. Proteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometry. J Proteome Res 2013;12:927-936.
40. 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 1984;259:3308-3317.
41. Schindler M, Hogan M, Miller R, DeGaetano D. A nuclear specific glycoprotein representative of a unique pattern of glycosylation. J Biol Chem 1987;262:1254-1260.
42. Roquemore EP, Chou T-Y, Hart GW. Detection of O-linked N-acetylglucosamine (O-GlcNAc) on cytoplasmic and nuclear proteins. In: William J, Lennarz GWH, editors. Methods in Enzymology. Academic Press, New York; 1994, pp. 443-460.
43. Ramakrishnan B, Qasba PK. Structure-based design of β1, 4-galactosyltransferase I (β4Gal-T1) with equally efficient N-acetylgalactosaminyltransferase activity: point mutation broadens βGal-T1 donor specificity. J Biol Chem 2002;277:20833-20839.
44. Khidekel N, Arndt S, Lamarre-Vincent N, Lippert A, Poulin-Kerstien KG, Ramakrishnan B, Qasba PK, Hsieh-Wilson LC. A chemoenzymatic approach toward the rapid and sensitive detection of O-GlcNAc posttranslational modifications. J Am Chem Soc 2003;125:16162-16163.
45. Tai H-C, Khidekel N, Ficarro SB, Peters EC, Hsieh-Wilson LC. Parallel identification of O-GlcNAc-modified proteins from cell lysates. J Am Chem Soc 2004;126:10500-10501.
46. Rexach JE, Rogers CJ, Yu S-H, Tao J, Sun YE, Hsieh-Wilson LC. Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags. Nat Chem Biol 2010;6:645-651.
47. Clark PM, Dweck JF, Mason DE, Hart CR, Buck SB, Peters EC, Agnew BJ, Hsieh-Wilson LC. Direct in-gel fluorescence detection and cellular imaging of O-GlcNAc-modified proteins. J Am Chem Soc 2008;130:11576-11577.
48. Wang Z, Udeshi ND, O'Malley M, Shabanowitz J, Hunt DF, Hart GW. Enrichment and site mapping of O-linked N-acetylglucosamine by a combination of chemical/enzymatic tagging, photochemical cleavage, and electron transfer dissociation mass spectrometry. Mol Cell Proteomics 2010;9:153-160.
49. Alfaro J, Gong C, Monroe M, Aldrich J, Clauss T, Purvine S, Wang Z, Camp D, Shabanowitz J, Stanley P, Hart G, Hunt D, Yang F, Smith R. Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-specific O-GlcNAc transferase targets. Proc Natl Acad Sci U S A 2012;109:7280-7285.
50. Cecioni S, Vocadlo DJ. Tools for probing and perturbing O-GlcNAc in cells and in vivo. Curr Opin Chem Biol 2013;17:719-728.
51. Holt GD, Haltiwanger RS, Torres CR, Hart GW. Erythrocytes contain cytoplasmic glycoproteins. O-linked GlcNAc on Band 4.1. J Biol Chem 1987;262:14847-14850.
52. Khidekel N, Ficarro SB, Peters EC, Hsieh-Wilson LC. Exploring the O-GlcNAc proteome: direct identification of O-GlcNAc-modified proteins from the brain. Proc Natl Acad Sci U S A 2004;101:13132-13137.
53. Thirumurugan P, Matosiuk D, Jozwiak K. Click chemistry for drug development and diverse chemical-biology applications. Chem Rev 2013;113:4905-4979.
54. Zachara NE, O'Donnell N, Cheung WD, Mercer JJ, Marth JD, Hart GW. Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress. J Biol Chem 2004;279:30133-30142.
55. 2-modified proteins induced under glucose deprivation. PLoS One 2011;6:e18959.
56. Reason AJ, Blench IP, Haltiwanger RS, Hart GW, Morris HR, Panico M, Dell A. High-sensitivity FAB-MS strategies for O-GlcNAc characterization. Glycobiology 1991;1:585-594.
57. Greis KD, Hayes BK, Comer FI, Kirk M, Barnes S, Lowary TL, Hart GW. Selective detection and site-analysis of O-GlcNAc-modified glycopeptides by β-elimination and tandem electrospray mass spectrometry. Anal Biochem 1996;234:38-49.
58. North SJ, Hitchen PG, Haslam SM, Dell A. Mass spectrometry in the analysis of N-linked and O-linked glycans. Curr Opin Struct Biol 2009;19:498-506.
59. Myers SA, Daou S, Affar EB, 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.
60. Housley MP, Udeshi ND, Rodgers JT, Shabanowitz J, Puigserver P, Hunt DF, Hart GW. A PGC-1α-O-GlcNAc transferase complex regulates FoxO transcription factor activity in response to glucose. J Biol Chem 2009;284:5148-5157.
61. Zhao P, Viner R, Teo CF, Boons G-J, Horn D, Wells L. Combining high-energy C-trap dissociation and electron transfer dissociation for protein O-GlcNAc modification site assignment. J Proteome Res 2011;10:4088-4104.
62. Wells L, Vosseller K, Cole RN, Cronshaw JM, Matunis MJ, Hart GW. Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications. Mol Cell Proteomics 2002;1:791-804.
63. Radu A, Moore MS, Blobel GN. The peptide repeat domain of nucleoporin NUP98 functions as a docking site in transport across the nuclear pore complex. Cell 1995;81:215-222.
64. Wente SR, Rout MP. The nuclear pore complex and nuclear transport. Cold Spring Harb Perspect Biol 2010;2:a000562. doi:10.1101/cshperspect.a000562.
65. Akey CW, Goldfarb DS. Protein import through the nuclear pore complex is a multistep process. J Cell Biol 1989;109:971-982.
66. Finlay DR, Forbes DJ. Reconstitution of biochemically altered nuclear pores: transport can be eliminated and restored. Cell 1990;60:17-29.
67. Miller MW, Hanover JA. Functional nuclear pores reconstituted with beta 1-4 galactose-modified O-linked N-acetylglucosamine glycoproteins. J Biol Chem 1994;269:9289-9297.
68. Shafi R, Lyer SPN, Ellies LG, O'Donnell N, Marek KW, Chui D, Hart GW, Marth JD. The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny. Proc Natl Acad Sci U S A 2000;97:5735-5739.
69. O'Donnell N, Zachara NE, Hart GW, Marth JD. Ogt-dependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viability. Mol Cell Biol 2004;24:1680-1690.
70. Kazemi Z, Chang H, Haserodt S, McKen C, Zachara NE. O-linked β-N-acetylglucosamine (O-GlcNAc) regulates stress-induced heat shock protein expression in a GSK-β-dependent manner. J Biol Chem 2010;285:39096-39107.
71. Hanover JA, Forsythe ME, Hennessey PT, Brodigan TM, Love DC, Ashwell G, Krause M. A Caenorhabditis elegans model of insulin resistance: altered macronutrient storage and dauer formation in an OGT-1 knockout. Proc Natl Acad Sci U S A 2005;102:11266-11271.
72. Heesepeck A, Cole RN, Borkhsenious ON, Hart GW, Raikhel NV. Plant nuclear pore complex proteins are modified by novel oligosaccharides with terminal N-acetylglucosamine. Plant Cell 1995;7:1459-1471.
73. Hartweck LM, Scott CL, Olszewski NE. Two O-linked N-acetylglucosamine transferase genes of Arabidopsis thaliana L. Heynh. have overlapping functions necessary for gamete and seed development. Genetics 2002;161:1279-1291.
74. Jacobsen SE, Olszewski NE. Mutations at the SPINDLY locus of Arabidopsis alter gibberellin signal transduction. Plant Cell 1993;5:887-896.
75. Wilson RN, Somerville CR. Phenotypic suppression of the gibberellin-insensitive mutant (gai) of Arabidopsis. Plant Physiol 1995;108:495-502.
76. Silverstone AL, Tseng T-S, Swain SM, Dill A, Jeong SY, Olszewski NE, Sun T-P. Functional analysis of SPINDLY in gibberellin signaling in Arabidopsis. Plant Physiol 2007;143:987-1000.
77. Steiner E, Efroni I, Gopalraj M, Saathoff K, Tseng T-S, Kieffer M, Eshed Y, Olszewski N, Weiss D. The Arabidopsis O-linked N-acetylglucosamine transferase SPINDLY interacts with class I TCPs to facilitate cytokinin responses in leaves and flowers. Plant Cell 2012;24:96-108.
78. Tseng T-S, Salomé PA, McClung CR, Olszewski NE. SPINDLY and GIGANTEA interact and act in Arabidopsis thaliana pathways involved in light responses, flowering, and rhythms in cotyledon movements. Plant Cell 2004;16:1550-1563.
79. Taoka K-I, Ham B-K, Xoconostle-Cázares B, Rojas MR, Lucas WJ. Reciprocal phosphorylation and glycosylation recognition motifs control NCAPP1 interaction with pumpkin phloem proteins and their cell-to-cell movement. Plant Cell 2007;19:1866-1884.
80. Lee J-Y, Yoo B-C, Lucas WJ. Parallels between nuclear-pore and plasmodesmal trafficking of information molecules. Planta 2000;210:177-187.
81. Kose S, Furuta M, Imamoto N. Hikeshi, a nuclear import carrier for Hsp70s, protects cells from heat shock-induced nuclear damage. Cell 2012;149:578-589.
82. Ngoh GA, Watson LJ, Facundo HT, Jones SP. Augmented O-GlcNAc signaling attenuates oxidative stress and calcium overload in cardiomyocytes. Amino Acids 2011;40:895-911.
83. Ngoh GA, Facundo HT, Hamid T, Dillmann W, Zachara NE, Jones SP. Unique hexosaminidase reduces metabolic survival signal and sensitizes cardiac myocytes to hypoxia/reoxygenation injury. Circ Res 2009;104:41-49.
84. Ngoh GA, Watson LJ, Jones SP. Loss of O-GlcNAc transferase activity sensitizes cardiac myocytes to post-hypoxic death. FASEB J 2008;22.
85. Slawson C, Zachara NE, Vosseller K, Cheung WD, Lane MD, Hart GW. Perturbations in O-linked β-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis. J Biol Chem 2005;280:32944-32956.
86. Miller MW, Caracciolo MR, Berlin WK, Hanover JA. Phosphorylation and glycosylation of nucleoporins. Arch Biochem Biophys 1999;367:51-60.
87. Crampton N, Kodiha M, Shrivastava S, Umar R, Stochaj U. Oxidative stress inhibits nuclear protein export by multiple mechanisms that target FG nucleoporins and Crm1. Mol Biol Cell 2009;20:5106-5116.
88. Jones SP, Zachara NE, Ngoh GA, Hill BG, Teshima Y, Bhatnagar A, Hart GW, Marbán E. Cardioprotection by N-acetylglucosamine linkage to cellular proteins. Circulation 2008;117:1172-1182.
89. Love DC, Ghosh S, Mondoux MA, Fukushige T, Wang P, Wilson MA, Iser WB, Wolkow CA, Krause MW, Hanover JA. Dynamic O-GlcNAc cycling at promoters of Caenorhabditis elegans genes regulating longevity, stress, and immunity. Proc Natl Acad Sci U S A 2010;107:7413-7418.
90. Zou LY, Yang SL, Hu SH, Chaudry IH, Marchase RB, Chatham JC. The protective effects of PUGNAc on cardiac function after trauma-hemorrhage are mediated via increased protein O-GlcNAc levels. Shock 2007;27:402-408.
91. Ngoh GA, Hamid T, Prabhu SD, Jones SP. O-GlcNAc signaling attenuates ER stress-induced cardiomyocyte death. Am J Physiol 2009;297:H1711-H1719.
92. Not LG, Marchase RB, Fulop N, Brocks CA, Chatham JC. Glucosamine administration improves survival rate after severe hemorrhagic shock combined with trauma in rats. Shock 2007;28:345-352.
93. Not LG, Brocks CA, Vamhidy L, Marchase RB, Chatham JC. Increased O-linked beta-N-acetylglucosamine levels on proteins improves survival, reduces inflammation and organ damage 24 hours after trauma-hemorrhage in rats. Crit Care Med 2010;38:562-571.
94. Yang SL, Zou LY, Bounelis P, Chaudry I, Chatham JC, Marchase RB. Glucosamine administration during resuscitation improves organ function after trauma hemorrhage. Shock 2006;25:600-607.
95. Zou LY, Yang SL, Champattanachai V, Hu SH, Chaudry IH, Marchase RB, Chatham JC. Glucosamine improves cardiac function following trauma-hemorrhage by increased protein O-GlcNAcylation and attenuation of NF-kappa B signaling. Am J Physiol 2009;296:H515-H523.
96. Liu J, Marchase RB, Chatham JC. Increased O-GlcNAc levels during reperfusion lead to improved functional recovery and reduced calpain proteolysis. Am J Physiol 2007;293:H1391-H1399.
97. 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 2007;73:288-297.
98. Fulop N, Zhang ZH, Marchase RB, Chatham JC. Glucosamine cardioprotection in perfused rat hearts associated with increased O-linked N-acetylglucosamine protein modification and altered p38 activation. Am J Physiol 2007;292:H2227-H2236.
99. Hwang SY, Shin JH, Hwang JS, Kim SY, Shin JA, Oh ES, Oh S, Kim JB, Lee JK, Han IO. Glucosamine exerts a neuroprotective effect via suppression of inflammation in rat brain ischemia/reperfusion injury. Glia 2010;58:1881-1892.
100. Liu J, Pang Y, Chang T, Bounelis P, Chatham JC, Marchase RB. Increased hexosamine biosynthesis and protein O-GlcNAc levels associated with myocardial protection against calcium paradox and ischemia. J Mol Cell Cardiol 2006;40:303-312.
101. Pang Y, Hunton DL, Bounelis P, Marchase RB. Hyperglycemia inhibits capacitative calcium entry and hypertrophy in neonatal cardiomyocytes. Diabetes 2002;51:3461-3467.
102. Sohn KC, Lee KY, Park JE, Do SI. OGT functions as a catalytic chaperone under heat stress response: a unique defense role of OGT in hyperthermia. Biochem Biophys Res Commun 2004;322:1045-1051.
103. Chatham JC, Marchase RB. The role of protein O-linked beta-N-acetylglucosamine in mediating cardiac stress responses. Biochim Biophys Acta 1800;2010:57-66.
104. Fang B, Miller MW. Use of galactosyltransferase to assess the biological function of O-linked N-acetyl-D-glucosamine: a potential role for O-GlcNAc during cell division. Exp Cell Res 2001;263:243-253.
105. Laurell E, Kutay U. Dismantling the NPC permeability barrier at the onset of mitosis. Cell Cycle 2011;10:2243-2245.
106. Laurell E, Beck K, Krupina K, Theerthagiri G, Bodenmiller B, Horvath P, Aebersold R, Antonin W, Kutay U. Phosphorylation of Nup98 by multiple kinases is crucial for NPC disassembly during mitotic entry. Cell 2011;144:539-550.
107. Kodiha M, Stochaj U. Nuclear transport: a switch for the oxidative stress-signaling circuit? J Signal Transduct 2012;2012:208650.
108. Mizuguchi-Hata C, Ogawa Y, Oka M, Yoneda Y. Quantitative regulation of nuclear pore complex proteins by O-GlcNAcylation. Biochim Biophys Acta 1833;2013:2682-2689.
109. Yu S-H, Boyce M, Wands AM, Bond MR, Bertozzi CR, Kohler JJ. Metabolic labeling enables selective photocrosslinking of O-GlcNAc-modified proteins to their binding partners. Proc Natl Acad Sci U S A 2012;109:4834-4839.
110. Pham N, Parker R, Kohler J. Photocrosslinking approaches to interactome mapping. Curr Opin Chem Biol 2013;17:90-101.
111. Rout MP, Aitchison JD, Magnasco MO, Chait BT. Virtual gating and nuclear transport: the hole picture. Trends Cell Biol 2003;13:622-628.
112. Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. Proc Natl Acad Sci U S A 2003;100:2450-2455.
113. Frey S, Görlich D. A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes. Cell 2007;130:512-523.
114. Labokha AA, Gradmann S, Frey S, Hulsmann BB, Urlaub H, Baldus M, Gorlich D. Systematic analysis of barrier-forming FG hydrogels from Xenopus nuclear pore complexes. EMBO J 2013;32:204-218.
115. Strambio-De-Castillia C, Niepel M, Rout MP. The nuclear pore complex: bridging nuclear transport and gene regulation. Nat Rev Mol Cell Biol 2010;11:490-501.
116. Arib G, Akhtar A. Multiple facets of nuclear periphery in gene expression control. Curr Opin Cell Biol 2011;23:346-353.
117. Blobel G. Gene gating: a hypothesis. Proc Natl Acad Sci U S A 1985;82:8527-8529.
118. Casolari JM, Brown CR, Komili S, West J, Hieronymus H, Silver PA. Genome-wide localization of the nuclear transport machinery couples transcriptional status and nuclear organization. Cell 2004;117:427-439.
119. Hou C, Corces VG. Nups take leave of the nuclear envelope to regulate transcription. Cell 2010;140:306-308.
120. Capelson M, Liang Y, Schulte R, Mair W, Wagner U, Hetzer MW. Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. Cell 2010;140:372-383.
121. Kalverda B, Pickersgill H, Shloma VV, Fornerod M. Nucleoporins directly stimulate expression of developmental and cell-cycle genes inside the nucleoplasm. Cell 2010;140:360-371.
122. Vaquerizas JM, Suyama R, Kind J, Miura K, Luscombe NM, Akhtar A. Nuclear pore proteins Nup153 and megator define transcriptionally active regions in the Drosophila genome. PLoS Genet 2010;6:e1000846.
123. Gough SM, Slape CI, Aplan PD. NUP98 gene fusions and hematopoietic malignancies: common themes and new biologic insights. Blood 2011;118:6247-6257.
124. Jackson SP, Tjian R. Purification and analysis of RNA polymerase II transcription factors by using wheat germ agglutinin affinity chromatography. Proc Natl Acad Sci U S A 1989;86:1781-1785.