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Volumn 25, Issue 4, 2011, Pages 227-236

The role of intracellular protein O-glycosylation in cell adhesion and disease

Author keywords

Cancer; Cell adhesion; Diabetes; O GlcNAc; O glycosylation

Indexed keywords

CELL PROTEIN; KERATIN; MYC PROTEIN; N ACETYLGLUCOSAMINE; PREGNANCY SPECIFIC BETA1 GLYCOPROTEIN; PROTEIN SERINE THREONINE KINASE;

EID: 80052302909     PISSN: 16748301     EISSN: 16748301     Source Type: Journal    
DOI: 10.1016/S1674-8301(11)60031-6     Document Type: Review
Times cited : (22)

References (100)
  • 1
    • 0035077832 scopus 로고    scopus 로고
    • O-glycosylation of the mucin type
    • Hanisch FG O-glycosylation of the mucin type. Biol Chem 2001, 382:143-149.
    • (2001) Biol Chem , vol.382 , pp. 143-149
    • Hanisch, F.G.1
  • 2
    • 0036816556 scopus 로고    scopus 로고
    • Glycosylation of proteins in plants and in-vertebrates
    • Wilson IBH Glycosylation of proteins in plants and in-vertebrates. Curr Opin Struct Biol 2002, 12:569-577.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 569-577
    • Wilson, I.B.H.1
  • 3
    • 0034442818 scopus 로고    scopus 로고
    • A journey to the world of glycobiology
    • Kobata A A journey to the world of glycobiology. Glycoconj J 2001, 17:443-464.
    • (2001) Glycoconj J , vol.17 , pp. 443-464
    • Kobata, A.1
  • 5
    • 0018929328 scopus 로고
    • High molecular weight surface glycoproteins of murine lymphocytes
    • Hoessli DC, Vassalli P High molecular weight surface glycoproteins of murine lymphocytes. J Immunol 1980, 125:1758-1763.
    • (1980) J Immunol , vol.125 , pp. 1758-1763
    • Hoessli, D.C.1    Vassalli, P.2
  • 6
    • 0029813776 scopus 로고    scopus 로고
    • Cell surface carbohydrates as prognostic markers in human carcinomas
    • Dabelsteen E Cell surface carbohydrates as prognostic markers in human carcinomas. J Pathol 1996, 179:358-369.
    • (1996) J Pathol , vol.179 , pp. 358-369
    • Dabelsteen, E.1
  • 8
    • 0029118548 scopus 로고
    • Adhesion molecules on human myeloma cells: significant changes in expression related to malignancy, tumor spreading, and immortalization
    • Pellat-deceunynck C, Barillé S, Puthier D Adhesion molecules on human myeloma cells: significant changes in expression related to malignancy, tumor spreading, and immortalization. Cancer Res 1995, 3647-3653.
    • (1995) Cancer Res , pp. 3647-3653
    • Pellat-deceunynck, C.1    Barillé, S.2    Puthier, D.3
  • 9
    • 0021280147 scopus 로고
    • Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc
    • 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.
    • (1984) J Biol Chem , vol.259 , pp. 3308-3317
    • Torres, C.R.1    Hart, G.W.2
  • 10
    • 0023758426 scopus 로고
    • Nuclear and cytoplasmic glycosylation: novel saccharide linkages in unexpected places
    • Hart GW, Holt GD, Haltiwanger RS Nuclear and cytoplasmic glycosylation: novel saccharide linkages in unexpected places. Trends Biochem Sci 1988, 13:380-384.
    • (1988) Trends Biochem Sci , vol.13 , pp. 380-384
    • Hart, G.W.1    Holt, G.D.2    Haltiwanger, R.S.3
  • 11
    • 0023037076 scopus 로고
    • The subcellular distribution of terminal N-acetylglucosamine moieties. Localization of a novel protein-saccharide linkage, O-linked GlcNAc
    • Holt GD, Hart GW The subcellular distribution of terminal N-acetylglucosamine moieties. Localization of a novel protein-saccharide linkage, O-linked GlcNAc. J Biol Chem 1986, 261:8049-8057.
    • (1986) J Biol Chem , vol.261 , pp. 8049-8057
    • Holt, G.D.1    Hart, G.W.2
  • 12
    • 0023225084 scopus 로고
    • Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine
    • 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.
    • (1987) J Cell Biol , vol.104 , pp. 1157-1164
    • Holt, G.D.1    Snow, C.M.2    Senior, A.3    Haltiwanger, R.S.4    Gerace, L.5    Hart, G.W.6
  • 13
    • 0029657990 scopus 로고    scopus 로고
    • O-GlcNAcylation of key nuclear and cytoskeletal proteins: reciprocity with O-phosphorylation and putative roles in protein multimerization
    • Hart GW, Kreppel LK, Comer FI, Arnold CS, Snow DM, Ye Z, et al. O-GlcNAcylation of key nuclear and cytoskeletal proteins: reciprocity with O-phosphorylation and putative roles in protein multimerization. Glycobiology 1996, 6:711-716.
    • (1996) Glycobiology , vol.6 , pp. 711-716
    • Hart, G.W.1    Kreppel, L.K.2    Comer, F.I.3    Arnold, C.S.4    Snow, D.M.5    Ye, Z.6
  • 14
    • 0030944105 scopus 로고    scopus 로고
    • O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats
    • Lubas WA, Frank DW, Krause M, Hanover JA O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats. J Biol Chem 1997, 272:9316-9324.
    • (1997) J Biol Chem , vol.272 , pp. 9316-9324
    • Lubas, W.A.1    Frank, D.W.2    Krause, M.3    Hanover, J.A.4
  • 16
    • 0034705030 scopus 로고    scopus 로고
    • The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny
    • Shafi R, Iyer SP, Ellies LG, O'Donnell N, Marek KW, 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. Proc Natl Acad Sci U S A 2000, 97:5735-5739.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 5735-5739
    • Shafi, R.1    Iyer, S.P.2    Ellies, L.G.3    O'Donnell, N.4    Marek, K.W.5    Chui, D.6
  • 18
    • 0035971182 scopus 로고    scopus 로고
    • Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain
    • Gao Y, Wells L, Comer FI, Parker GJ, Hart GW Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain. J Biol Chem 2001, 276:9838-9845.
    • (2001) J Biol Chem , vol.276 , pp. 9838-9845
    • Gao, Y.1    Wells, L.2    Comer, F.I.3    Parker, G.J.4    Hart, G.W.5
  • 19
    • 7244261948 scopus 로고    scopus 로고
    • Protein family review Sp1- and Krüppel-like transcription factors
    • Kaczynski J, Cook T, Urrutia R Protein family review Sp1- and Krüppel-like transcription factors. Genome Biol 2003, 1-8.
    • (2003) Genome Biol , pp. 1-8
    • Kaczynski, J.1    Cook, T.2    Urrutia, R.3
  • 20
    • 0037201722 scopus 로고    scopus 로고
    • Regulation of the activity of Sp1-related transcription factors
    • Bouwman P, Philipsen S Regulation of the activity of Sp1-related transcription factors. Mol Cell Endocrinol 2002, 195:27-38.
    • (2002) Mol Cell Endocrinol , vol.195 , pp. 27-38
    • Bouwman, P.1    Philipsen, S.2
  • 21
    • 0024280897 scopus 로고
    • O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation
    • Jackson SP, Tjian R O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation. Cell 1988, 55:125-133.
    • (1988) Cell , vol.55 , pp. 125-133
    • Jackson, S.P.1    Tjian, R.2
  • 22
    • 0030907389 scopus 로고    scopus 로고
    • Reduced O-glycosylation of Sp1 is associated with increased proteasome susceptibility
    • Han I, Kudlow JE Reduced O-glycosylation of Sp1 is associated with increased proteasome susceptibility. Mol Cell Biol 1997, 17:2550-2558.
    • (1997) Mol Cell Biol , vol.17 , pp. 2550-2558
    • Han, I.1    Kudlow, J.E.2
  • 23
    • 33746457809 scopus 로고    scopus 로고
    • Post-translational modification by O-GlcNAc: another way to change protein function
    • Kudlow JE Post-translational modification by O-GlcNAc: another way to change protein function. J Cell Biochem 2006, 98:1062-1075.
    • (2006) J Cell Biochem , vol.98 , pp. 1062-1075
    • Kudlow, J.E.1
  • 24
    • 0346965700 scopus 로고    scopus 로고
    • O-GlcNAc modification is an endogenous inhibitor of the proteasome
    • Zhang F, Su K, Yang X, Bowe DB, Paterson AJ, Kudlow JE O-GlcNAc modification is an endogenous inhibitor of the proteasome. Cell 2003, 115:715-725.
    • (2003) Cell , vol.115 , pp. 715-725
    • Zhang, F.1    Su, K.2    Yang, X.3    Bowe, D.B.4    Paterson, A.J.5    Kudlow, J.E.6
  • 25
    • 0035937586 scopus 로고    scopus 로고
    • Glycosylation of Nucleocytoplasmic Proteins: Signal Transduction and O-GlcNAc
    • Wells L Glycosylation of Nucleocytoplasmic Proteins: Signal Transduction and O-GlcNAc. Science 2001, 291:2376-2378.
    • (2001) Science , vol.291 , pp. 2376-2378
    • Wells, L.1
  • 26
    • 15744393419 scopus 로고    scopus 로고
    • Sp1: regulation of gene expression by phosphorylation
    • Chu S, Ferro TJ Sp1: regulation of gene expression by phosphorylation. Gene 2005, 348:1-11.
    • (2005) Gene , vol.348 , pp. 1-11
    • Chu, S.1    Ferro, T.J.2
  • 27
    • 0032488979 scopus 로고    scopus 로고
    • Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate
    • Haltiwanger RS, Grove K, Philipsberg GA Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate. J Biol Chem 1998, 273:3611-3617.
    • (1998) J Biol Chem , vol.273 , pp. 3611-3617
    • Haltiwanger, R.S.1    Grove, K.2    Philipsberg, G.A.3
  • 28
    • 0033551374 scopus 로고    scopus 로고
    • MYC oncogenes and human neoplastic disease
    • Nesbit CE, Tersak JM, Prochownik EV MYC oncogenes and human neoplastic disease. Oncogene 1999, 18:3004-3016.
    • (1999) Oncogene , vol.18 , pp. 3004-3016
    • Nesbit, C.E.1    Tersak, J.M.2    Prochownik, E.V.3
  • 29
  • 30
    • 0029049198 scopus 로고
    • C-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas
    • Chou TY, 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.
    • (1995) J Biol Chem , vol.270 , pp. 18961
    • Chou, T.Y.1    Hart, G.W.2    Dang, C.V.3
  • 31
    • 0037166352 scopus 로고    scopus 로고
    • Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins: alternative glyco-sylation/phosphorylation of THR-58, a known mutational hot spot of c-Myc in lymphomas, is regulated by mitogens
    • Kamemura K, Hayes BK, Comer FI, Hart GW Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins: alternative glyco-sylation/phosphorylation of THR-58, a known mutational hot spot of c-Myc in lymphomas, is regulated by mitogens. J Biol Chem 2002, 277:19229-19235.
    • (2002) J Biol Chem , vol.277 , pp. 19229-19235
    • Kamemura, K.1    Hayes, B.K.2    Comer, F.I.3    Hart, G.W.4
  • 32
    • 39749124274 scopus 로고    scopus 로고
    • MYC in mammalian epidermis: how can an oncogene stimulate differentiation?
    • Watt FM, Frye M, Benitah SA MYC in mammalian epidermis: how can an oncogene stimulate differentiation?. Nat Rev Cancer 2008, 8:234-242.
    • (2008) Nat Rev Cancer , vol.8 , pp. 234-242
    • Watt, F.M.1    Frye, M.2    Benitah, S.A.3
  • 33
    • 41649118307 scopus 로고    scopus 로고
    • Aberrant Activation of γ-Catenin Promotes Genomic Instability and Oncogenic Effects during Tumor Progression
    • Pan H, Papageorgis P, Abdolmaleky HM, Faller DV, Thiagalingam S Aberrant Activation of γ-Catenin Promotes Genomic Instability and Oncogenic Effects during Tumor Progression. Cancer Biol Ther 2007, 6:1638-1643.
    • (2007) Cancer Biol Ther , vol.6 , pp. 1638-1643
    • Pan, H.1    Papageorgis, P.2    Abdolmaleky, H.M.3    Faller, D.V.4    Thiagalingam, S.5
  • 34
    • 33746494904 scopus 로고    scopus 로고
    • Pemphigus vulgaris identifies plakoglobin as key suppressor of c-Myc in the skin
    • Williamson L, Raess Na, Caldelari R, Zakher A, de Bruin A, Posthaus H, et al. Pemphigus vulgaris identifies plakoglobin as key suppressor of c-Myc in the skin. EMBO J 2006, 25:3298-3309.
    • (2006) EMBO J , vol.25 , pp. 3298-3309
    • Williamson, L.1    Raess, N.2    Caldelari, R.3    Zakher, A.4    de Bruin, A.5    Posthaus, H.6
  • 35
    • 0141844491 scopus 로고    scopus 로고
    • Plakoglobin is O-glycosylated close to the N-terminal destruction box
    • Hatsell S, Medina L, Merola J, Haltiwanger R, Cowin P Plakoglobin is O-glycosylated close to the N-terminal destruction box. J Biol Chem 2003, 278:37745-37752.
    • (2003) J Biol Chem , vol.278 , pp. 37745-37752
    • Hatsell, S.1    Medina, L.2    Merola, J.3    Haltiwanger, R.4    Cowin, P.5
  • 36
    • 0033788835 scopus 로고    scopus 로고
    • Plakoglobin and beta-catenin: protein interactions, regulation and biological roles
    • Zhurinsky J, Shtutman M, Ben-Ze'ev A Plakoglobin and beta-catenin: protein interactions, regulation and biological roles. J Cell Sci 2000, 113:3127-3139.
    • (2000) J Cell Sci , vol.113 , pp. 3127-3139
    • Zhurinsky, J.1    Shtutman, M.2    Ben-Ze'ev, A.3
  • 37
    • 0033392360 scopus 로고    scopus 로고
    • Wnt signalling in mammalian development and cancer
    • Smalley MJ, Dale TC Wnt signalling in mammalian development and cancer. Cancer Metastasis Revi 1999, 18:215-230.
    • (1999) Cancer Metastasis Revi , vol.18 , pp. 215-230
    • Smalley, M.J.1    Dale, T.C.2
  • 38
    • 34250365241 scopus 로고    scopus 로고
    • Desmosomes: a role in cancer?
    • Chidgey M, Dawson C Desmosomes: a role in cancer?. Br J Cancer 2007, 96:1783-1787.
    • (2007) Br J Cancer , vol.96 , pp. 1783-1787
    • Chidgey, M.1    Dawson, C.2
  • 39
    • 33745848407 scopus 로고    scopus 로고
    • Suppression of canonical Wnt/bcatenin signaling by nuclear plakoglobin recapitulates phenotype of arrhythmogenic right ventricular cardiomyopathy
    • Garciagras E, Lombardi R, Giocondo MJ, Willerson JT, Schneider MD, Khoury DS, et al. Suppression of canonical Wnt/bcatenin signaling by nuclear plakoglobin recapitulates phenotype of arrhythmogenic right ventricular cardiomyopathy. Science 2006, 116.
    • (2006) Science , pp. 116
    • Garciagras, E.1    Lombardi, R.2    Giocondo, M.J.3    Willerson, J.T.4    Schneider, M.D.5    Khoury, D.S.6
  • 40
    • 33744953426 scopus 로고    scopus 로고
    • Stabi-lization of plakoglobin and enhanced keratinocyte cell-cell adhesion by intracellular O-glycosylation
    • Hu P, Berkowitz P, Madden VJ, Rubenstein DS Stabi-lization of plakoglobin and enhanced keratinocyte cell-cell adhesion by intracellular O-glycosylation. J Biol Chem 2006, 281:12786-12791.
    • (2006) J Biol Chem , vol.281 , pp. 12786-12791
    • Hu, P.1    Berkowitz, P.2    Madden, V.J.3    Rubenstein, D.S.4
  • 41
    • 0035724582 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of human keratinocyte beta-catenin and pla-koglobin reversibly regulates their binding to E-cadherin and alpha-catenin
    • Hu P, O'Keefe EJ, Rubenstein DS Tyrosine phosphorylation of human keratinocyte beta-catenin and pla-koglobin reversibly regulates their binding to E-cadherin and alpha-catenin. J Invest Dermatol 2001, 117:1059-1067.
    • (2001) J Invest Dermatol , vol.117 , pp. 1059-1067
    • Hu, P.1    O'Keefe, E.J.2    Rubenstein, D.S.3
  • 42
    • 44149099717 scopus 로고    scopus 로고
    • The human keratins: biology and pathology
    • Moll R, Divo M, Langbein L The human keratins: biology and pathology. Histochem Cell Biol 2008, 129:705-733.
    • (2008) Histochem Cell Biol , vol.129 , pp. 705-733
    • Moll, R.1    Divo, M.2    Langbein, L.3
  • 43
    • 0036468732 scopus 로고    scopus 로고
    • 'Hard' and 'soft' principles defining the structure, function and regulation of keratin intermediate filaments
    • Coulombe Pa, Omary MB 'Hard' and 'soft' principles defining the structure, function and regulation of keratin intermediate filaments. Curr Opin Cell Biol 2002, 14:110-122.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 110-122
    • Coulombe, P.1    Omary, M.B.2
  • 44
    • 68549096323 scopus 로고    scopus 로고
    • Insights into the mechanical properties of epithelial cells: the effects of shear stress on the assembly and remodeling of keratin intermediate filaments
    • Flitney EW, Kuczmarski ER, Adam SA, Goldman RD Insights into the mechanical properties of epithelial cells: the effects of shear stress on the assembly and remodeling of keratin intermediate filaments. FASEB J 2009, 23:2110-2119.
    • (2009) FASEB J , vol.23 , pp. 2110-2119
    • Flitney, E.W.1    Kuczmarski, E.R.2    Adam, S.A.3    Goldman, R.D.4
  • 46
    • 77958616531 scopus 로고    scopus 로고
    • O-GlcNAcylation determines the solubility, filament organization and stability of keratins 8 and 18
    • Srikanth B, Vaidya MM, Kalraiya RD O-GlcNAcylation determines the solubility, filament organization and stability of keratins 8 and 18. J Biol Chem 2010, 1-18.
    • (2010) J Biol Chem , pp. 1-18
    • Srikanth, B.1    Vaidya, M.M.2    Kalraiya, R.D.3
  • 47
    • 0026662974 scopus 로고
    • Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18
    • Chou CF, Smith AJ, Omary MB Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18. J Biol Chem 1992, 267:3901-3906.
    • (1992) J Biol Chem , vol.267 , pp. 3901-3906
    • Chou, C.F.1    Smith, A.J.2    Omary, M.B.3
  • 48
    • 77956412905 scopus 로고    scopus 로고
    • Cytoskeletal keratin glycosylation protects epithelial tissue from injury
    • Ku NO, Toivola DM, Strnad P, Omary MB Cytoskeletal keratin glycosylation protects epithelial tissue from injury. Nat Cell Biol 2010, 12:876-885.
    • (2010) Nat Cell Biol , vol.12 , pp. 876-885
    • Ku, N.O.1    Toivola, D.M.2    Strnad, P.3    Omary, M.B.4
  • 49
    • 0033843879 scopus 로고    scopus 로고
    • Cytokeratin 8 protects from hepatotoxicity, and its ratio to cytokeratin 18 determines the ability of hepatocytes to form Mallory bodies
    • Zatloukal K, Stumptner C, Lehner M, Denk H, Baribault H, Eshkind LG, et al. Cytokeratin 8 protects from hepatotoxicity, and its ratio to cytokeratin 18 determines the ability of hepatocytes to form Mallory bodies. Am J Pathol 2000, 156:1263-1274.
    • (2000) Am J Pathol , vol.156 , pp. 1263-1274
    • Zatloukal, K.1    Stumptner, C.2    Lehner, M.3    Denk, H.4    Baribault, H.5    Eshkind, L.G.6
  • 50
    • 77953231144 scopus 로고    scopus 로고
    • N-glycosylation status of E-cadherin controls cytoskeletal dynamics through the organization of distinct beta-catenin- and gamma-catenin-containing AJs
    • Jamal BT, Nita-Lazar M, Gao Z, Amin B, Walker J, Kukuruzinska MA N-glycosylation status of E-cadherin controls cytoskeletal dynamics through the organization of distinct beta-catenin- and gamma-catenin-containing AJs. Cell Health Cytoskelet 2009, 2009:67-80.
    • (2009) Cell Health Cytoskelet , vol.2009 , pp. 67-80
    • Jamal, B.T.1    Nita-Lazar, M.2    Gao, Z.3    Amin, B.4    Walker, J.5    Kukuruzinska, M.A.6
  • 51
    • 33845690437 scopus 로고    scopus 로고
    • Discriminating roles of desmosomal cadherins: beyond desmosomal adhesion
    • Dusek RL, Godsel LM, Green KJ Discriminating roles of desmosomal cadherins: beyond desmosomal adhesion. J Dermatol Sci 2007, 45:7-21.
    • (2007) J Dermatol Sci , vol.45 , pp. 7-21
    • Dusek, R.L.1    Godsel, L.M.2    Green, K.J.3
  • 52
    • 1842733459 scopus 로고    scopus 로고
    • Working out the strength and flexibility of desmosomes
    • Getsios S, Huen AC, Green KJ Working out the strength and flexibility of desmosomes. Nat Rev Mol Cell Biol 2004, 5:271-281.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 271-281
    • Getsios, S.1    Huen, A.C.2    Green, K.J.3
  • 53
    • 35348927451 scopus 로고    scopus 로고
    • Desmosomes: new perspectives on a classic
    • Green KJ, Simpson CL Desmosomes: new perspectives on a classic. J Invest Dermatol 2007, 127:2499-2515.
    • (2007) J Invest Dermatol , vol.127 , pp. 2499-2515
    • Green, K.J.1    Simpson, C.L.2
  • 54
    • 35548987124 scopus 로고    scopus 로고
    • Desmosomes from a structural perspective
    • Stokes DL Desmosomes from a structural perspective. Curr Opin Cell Biol 2007, 19:565-571.
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 565-571
    • Stokes, D.L.1
  • 55
    • 53349133034 scopus 로고    scopus 로고
    • Desmosomes: just cell adhesion or is there more?
    • Schmidt A, Koch PJ Desmosomes: just cell adhesion or is there more?. Cell Adh Migr 2007, 1:28.
    • (2007) Cell Adh Migr , vol.1 , pp. 28
    • Schmidt, A.1    Koch, P.J.2
  • 56
    • 44449092953 scopus 로고    scopus 로고
    • The desmosome and pemphigus
    • Waschke J The desmosome and pemphigus. Histochem Cell Biol 2008, 130:21-54.
    • (2008) Histochem Cell Biol , vol.130 , pp. 21-54
    • Waschke, J.1
  • 57
    • 57149087666 scopus 로고    scopus 로고
    • Autoantibodies in the autoimmune disease pemphigus foliaceus induce blistering via p38 mitogen-activated protein kinase-dependent signaling in the skin
    • Berkowitz P, Chua M, Liu Z, Diaz LA, Rubenstein DS Autoantibodies in the autoimmune disease pemphigus foliaceus induce blistering via p38 mitogen-activated protein kinase-dependent signaling in the skin. Am J Pathol 2008, 173:1628-1636.
    • (2008) Am J Pathol , vol.173 , pp. 1628-1636
    • Berkowitz, P.1    Chua, M.2    Liu, Z.3    Diaz, L.A.4    Rubenstein, D.S.5
  • 58
    • 21244476854 scopus 로고    scopus 로고
    • Desmosome signaling. Inhibition of p38MAPK prevents pemphigus vulgaris IgG-induced cytoskeleton reorganization
    • Berkowitz P, Hu P, Liu Z, Diaz LA, Enghild JJ, Chua MP, et al. Desmosome signaling. Inhibition of p38MAPK prevents pemphigus vulgaris IgG-induced cytoskeleton reorganization. J Biol Chem 2005, 280:23778-23784.
    • (2005) J Biol Chem , vol.280 , pp. 23778-23784
    • Berkowitz, P.1    Hu, P.2    Liu, Z.3    Diaz, L.A.4    Enghild, J.J.5    Chua, M.P.6
  • 59
    • 78650744019 scopus 로고    scopus 로고
    • DSR Advances in pemphigus research, signaling, and acantholysis
    • Bektas M, Runager K, Petersen JS, DSR Advances in pemphigus research, signaling, and acantholysis. G Ital Dermatol Venereol 2010, 145:675-687.
    • (2010) G Ital Dermatol Venereol , vol.145 , pp. 675-687
    • Bektas, M.1    Runager, K.2    Petersen, J.S.3
  • 60
    • 33750320914 scopus 로고    scopus 로고
    • Pemphigus, bullous impetigo, and the staphylococcal scalded-skin syndrome
    • Stanley JR, Amagai M Pemphigus, bullous impetigo, and the staphylococcal scalded-skin syndrome. N Engl J Med 2006, 355:1800-1810.
    • (2006) N Engl J Med , vol.355 , pp. 1800-1810
    • Stanley, J.R.1    Amagai, M.2
  • 61
    • 33748893008 scopus 로고    scopus 로고
    • Are desmoglein autoantibodies essential for the immunopathogenesis of pemphigus vulgaris, or just "witnesses of disease" ?
    • Amagai M, Ahmed AR, Kitajima Y, Bystryn JC, Milner Y, Gniadecki R, et al. Are desmoglein autoantibodies essential for the immunopathogenesis of pemphigus vulgaris, or just "witnesses of disease" ?. Exp Dermatol 2006, 15:815-831.
    • (2006) Exp Dermatol , vol.15 , pp. 815-831
    • Amagai, M.1    Ahmed, A.R.2    Kitajima, Y.3    Bystryn, J.C.4    Milner, Y.5    Gniadecki, R.6
  • 63
    • 33645227215 scopus 로고    scopus 로고
    • Desmoglein endocytosis and desmosome disassembly are coordinated responses to pemphigus autoantibodies
    • Calkins CC, Setzer SV, Jennings JM, Summers S, Tsunoda K, Amagai M, et al. Desmoglein endocytosis and desmosome disassembly are coordinated responses to pemphigus autoantibodies. J Biol Chem 2006, 281:7623-7634.
    • (2006) J Biol Chem , vol.281 , pp. 7623-7634
    • Calkins, C.C.1    Setzer, S.V.2    Jennings, J.M.3    Summers, S.4    Tsunoda, K.5    Amagai, M.6
  • 64
    • 77950590873 scopus 로고    scopus 로고
    • p38MAPK signaling and desmoglein-3 internalization are linked events in pemphigus acantholysis
    • Jolly PS, Berkowitz P, Bektas M, Lee HE, Chua M, Diaz LA, et al. p38MAPK signaling and desmoglein-3 internalization are linked events in pemphigus acantholysis. J Biol Chem 285:8936-41.
    • J Biol Chem , vol.285 , pp. 8936-41
    • Jolly, P.S.1    Berkowitz, P.2    Bektas, M.3    Lee, H.E.4    Chua, M.5    Diaz, L.A.6
  • 65
    • 66449087840 scopus 로고    scopus 로고
    • Biphasic activation of p38MAPK suggests that apoptosis is a downstream event in pemphigus acantholysis
    • Lee HE, Berkowitz P, Jolly PS, Diaz LA, Chua MP, Rubenstein DS Biphasic activation of p38MAPK suggests that apoptosis is a downstream event in pemphigus acantholysis. J Biol Chem 2009, 284:12524.
    • (2009) J Biol Chem , vol.284 , pp. 12524
    • Lee, H.E.1    Berkowitz, P.2    Jolly, P.S.3    Diaz, L.A.4    Chua, M.P.5    Rubenstein, D.S.6
  • 67
    • 33644701437 scopus 로고    scopus 로고
    • Normal human melanocyte home-ostasis as a paradigm for understanding melanoma
    • Haass NK, Herlyn M Normal human melanocyte home-ostasis as a paradigm for understanding melanoma. J Investig Dermatol Symp Proc 2005, 10:153-163.
    • (2005) J Investig Dermatol Symp Proc , vol.10 , pp. 153-163
    • Haass, N.K.1    Herlyn, M.2
  • 68
    • 0035819040 scopus 로고    scopus 로고
    • Downregulation of E-cadherin and Desmoglein 1 by autocrine hepatocyte growth factor during melanoma development
    • Li G, Schaider H, Satyamoorthy K, Hanakawa Y, Hashimoto K, Herlyn M Downregulation of E-cadherin and Desmoglein 1 by autocrine hepatocyte growth factor during melanoma development. Oncogene 2001, 20:8125-8135.
    • (2001) Oncogene , vol.20 , pp. 8125-8135
    • Li, G.1    Schaider, H.2    Satyamoorthy, K.3    Hanakawa, Y.4    Hashimoto, K.5    Herlyn, M.6
  • 69
    • 67649586282 scopus 로고    scopus 로고
    • Desmoglein 1-dependent suppression of EGFR signaling promotes epidermal differentiation and morphogenesis
    • Getsios S, Simpson CL, Kojima S-I, Harmon R, Sheu LJ, Dusek RL, et al. Desmoglein 1-dependent suppression of EGFR signaling promotes epidermal differentiation and morphogenesis. J Cell Biol 2009, 185:1243-1258.
    • (2009) J Cell Biol , vol.185 , pp. 1243-1258
    • Getsios, S.1    Simpson, C.L.2    Kojima, S.-I.3    Harmon, R.4    Sheu, L.J.5    Dusek, R.L.6
  • 70
    • 74549114727 scopus 로고    scopus 로고
    • Epidermal growth factor receptor in relation to tumor development: EGFR gene and cancer
    • Mitsudomi T, Yatabe Y. Epidermal growth factor receptor in relation to tumor development: EGFR gene and cancer. FEBS J; 277:301-8.
    • FEBS J , vol.277 , pp. 301-8
    • Mitsudomi, T.1    Yatabe, Y.2
  • 71
    • 0035503219 scopus 로고    scopus 로고
    • Cytoplasmic O-glycosylation prevents cell surface transport of E-cadherin during apoptosis
    • Zhu W, Leber B, Andrews DW Cytoplasmic O-glycosylation prevents cell surface transport of E-cadherin during apoptosis. EMBO J 2001, 20:5999-6007.
    • (2001) EMBO J , vol.20 , pp. 5999-6007
    • Zhu, W.1    Leber, B.2    Andrews, D.W.3
  • 72
    • 0025855139 scopus 로고
    • Discovery of a metabolic pathway mediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resist-ance
    • Marshall S, Bacote V, Traxinger RR Discovery of a metabolic pathway mediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resist-ance. J Biol Chem 1991, 266:4706-4712.
    • (1991) J Biol Chem , vol.266 , pp. 4706-4712
    • Marshall, S.1    Bacote, V.2    Traxinger, R.R.3
  • 73
    • 77956396629 scopus 로고    scopus 로고
    • O-GlcNAc signaling: a metabolic link between diabetes and cancer?
    • Slawson C, Copeland RJ, Hart GW. O-GlcNAc signaling: a metabolic link between diabetes and cancer? Trends Biochem Sci; 35:547-55.
    • Trends Biochem Sci , vol.35 , pp. 547-55
    • Slawson, C.1    Copeland, R.J.2    Hart, G.W.3
  • 74
    • 33644873810 scopus 로고    scopus 로고
    • Hexosamines, insulin resistance, and the complications of diabetes: current status
    • Buse M Hexosamines, insulin resistance, and the complications of diabetes: current status. Am J Physiol Endocrinol Metab 2006, 290:1-15.
    • (2006) Am J Physiol Endocrinol Metab , vol.290 , pp. 1-15
    • Buse, M.1
  • 75
    • 63649085232 scopus 로고    scopus 로고
    • Up-regulation of O-GlcNAc transferase with glucose deprivation in HepG2 cells is mediated by decreased hexosamine pathway flux
    • Taylor RP, Geisler TS, Chambers JH, McClain DA Up-regulation of O-GlcNAc transferase with glucose deprivation in HepG2 cells is mediated by decreased hexosamine pathway flux. J Biol Chem 2009, 284:3425-3432.
    • (2009) J Biol Chem , vol.284 , pp. 3425-3432
    • Taylor, R.P.1    Geisler, T.S.2    Chambers, J.H.3    McClain, D.A.4
  • 76
    • 0037300799 scopus 로고    scopus 로고
    • Cellular and Molecular Life Sciences A role for N-acetylglucosamine as a nutrient sensor and mediator of insulin resistance
    • Wells L, Vosseller K, Hart GW Cellular and Molecular Life Sciences A role for N-acetylglucosamine as a nutrient sensor and mediator of insulin resistance. Proteomics 2003, 60:222-228.
    • (2003) Proteomics , vol.60 , pp. 222-228
    • Wells, L.1    Vosseller, K.2    Hart, G.W.3
  • 77
    • 3042613480 scopus 로고    scopus 로고
    • O-GlcNAc a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress
    • Zachara NE, Hart GW O-GlcNAc a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress. Biochim Biophys Acta 2004, 1673:13-28.
    • (2004) Biochim Biophys Acta , vol.1673 , pp. 13-28
    • Zachara, N.E.1    Hart, G.W.2
  • 78
    • 40449128605 scopus 로고    scopus 로고
    • Hepatic glucose sensing via the CREB coactivator CRTC2
    • Dentin R, Hedrick S, Xie J, Yates J, Montminy M Hepatic glucose sensing via the CREB coactivator CRTC2. Science 2008, 319:1402-1405.
    • (2008) Science , vol.319 , pp. 1402-1405
    • Dentin, R.1    Hedrick, S.2    Xie, J.3    Yates, J.4    Montminy, M.5
  • 79
    • 0035872219 scopus 로고    scopus 로고
    • The potential mechanism of the diabetogenic action of streptozotocin: inhibition of pancreatic beta-cell O-GlcNAc-selective N-acetyl-beta-D-glucosaminidase
    • Konrad R, Mikolaenko I, Tolar J, Liu K The potential mechanism of the diabetogenic action of streptozotocin: inhibition of pancreatic beta-cell O-GlcNAc-selective N-acetyl-beta-D-glucosaminidase. Biochem J 2001, 356:31-41.
    • (2001) Biochem J , vol.356 , pp. 31-41
    • Konrad, R.1    Mikolaenko, I.2    Tolar, J.3    Liu, K.4
  • 80
    • 0034614349 scopus 로고    scopus 로고
    • Glucose and streptozotocin stimulate p135 O-glycosylation in pancreatic islets
    • Konrad RJ, Janowski KM, Kudlow JE Glucose and streptozotocin stimulate p135 O-glycosylation in pancreatic islets. Biochem Biophys Res Commun 2000, 267:26-32.
    • (2000) Biochem Biophys Res Commun , vol.267 , pp. 26-32
    • Konrad, R.J.1    Janowski, K.M.2    Kudlow, J.E.3
  • 82
    • 0034646330 scopus 로고    scopus 로고
    • Glucose stimulates protein modification by O-linked GlcNAc in pancreatic beta cells: linkage of O-linked GlcNAc to beta cell death
    • Liu K, Paterson J, Chin E, Kudlow JE Glucose stimulates protein modification by O-linked GlcNAc in pancreatic beta cells: linkage of O-linked GlcNAc to beta cell death. Proc Natl Acad Sci U S A 2000, 97:2820-2825.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 2820-2825
    • Liu, K.1    Paterson, J.2    Chin, E.3    Kudlow, J.E.4
  • 83
    • 0033080192 scopus 로고    scopus 로고
    • Elevated O-linked N-acetylglucosamine metabolism in pancreatic beta-cells
    • Hanover JA, Lai Z, Lee G, Lubas Wa, Sato SM Elevated O-linked N-acetylglucosamine metabolism in pancreatic beta-cells. Arch Biochem Biophys 1999, 362:38-45.
    • (1999) Arch Biochem Biophys , vol.362 , pp. 38-45
    • Hanover, J.A.1    Lai, Z.2    Lee, G.3    Lubas, W.4    Sato, S.M.5
  • 85
    • 20144389168 scopus 로고    scopus 로고
    • A Single Nucleotide Polymor-phism in MGEA5 Encoding Associated With Type 2 Diabetes in Mexican Americans
    • Lehman DM, Fu DJ, Freeman AB, Hunt KJ, Leach RJ, Johnson-Pais T, et al. A Single Nucleotide Polymor-phism in MGEA5 Encoding Associated With Type 2 Diabetes in Mexican Americans. Diabetes 2005, 54:1214-1221.
    • (2005) Diabetes , vol.54 , pp. 1214-1221
    • Lehman, D.M.1    Fu, D.J.2    Freeman, A.B.3    Hunt, K.J.4    Leach, R.J.5    Johnson-Pais, T.6
  • 86
    • 0026669469 scopus 로고
    • P-53 Function and Dysfunction Minireview
    • Vogelstein B, Kinzler KW p-53 Function and Dysfunction Minireview. Cell 1992, 70:523-526.
    • (1992) Cell , vol.70 , pp. 523-526
    • Vogelstein, B.1    Kinzler, K.W.2
  • 87
    • 4043181214 scopus 로고    scopus 로고
    • Cancer genes and the pathways they control
    • Vogelstein B, Kinzler KW Cancer genes and the pathways they control. Nat Med 2004, 10:789-799.
    • (2004) Nat Med , vol.10 , pp. 789-799
    • Vogelstein, B.1    Kinzler, K.W.2
  • 88
    • 33749160125 scopus 로고    scopus 로고
    • Modification of p53 with O-linked N-acetylglu-cosamine regulates p53 activity and stability
    • Yang WH, Kim JE, Nam HW, Ju JW, Kim HS, Kim YS, et al. Modification of p53 with O-linked N-acetylglu-cosamine regulates p53 activity and stability. Nat Cell Biol 2006, 8:1074-1083.
    • (2006) Nat Cell Biol , vol.8 , pp. 1074-1083
    • Yang, W.H.1    Kim, J.E.2    Nam, H.W.3    Ju, J.W.4    Kim, H.S.5    Kim, Y.S.6
  • 89
    • 0033079597 scopus 로고    scopus 로고
    • Oncogenic alterations of metabolism
    • Dang CV, Semenza GL Oncogenic alterations of metabolism. Trends Biochem Sci 1999, 24:68-72.
    • (1999) Trends Biochem Sci , vol.24 , pp. 68-72
    • Dang, C.V.1    Semenza, G.L.2
  • 90
    • 77952509221 scopus 로고    scopus 로고
    • Glycolysis links p53 function with NF-kappaB signaling: impact on cancer and aging process
    • Salminen A, Kaarniranta K Glycolysis links p53 function with NF-kappaB signaling: impact on cancer and aging process. J Cell Physiol 2010, 224:1-6.
    • (2010) J Cell Physiol , vol.224 , pp. 1-6
    • Salminen, A.1    Kaarniranta, K.2
  • 92
    • 43049139541 scopus 로고    scopus 로고
    • P53 regulates glucose metabolism through an IKK-NF-kappaB pathway and inhibits cell transformation
    • Kawauchi K, Araki K, Tobiume K, Tanaka N p53 regulates glucose metabolism through an IKK-NF-kappaB pathway and inhibits cell transformation. Nat Cell Biol 2008, 10:611-618.
    • (2008) Nat Cell Biol , vol.10 , pp. 611-618
    • Kawauchi, K.1    Araki, K.2    Tobiume, K.3    Tanaka, N.4
  • 93
    • 62549161375 scopus 로고    scopus 로고
    • Loss of p53 enhances catalytic activity of IKKbeta through O-linked beta-N-acetyl glucosamine modification
    • Kawauchi K, Araki K, Tobiume K, Tanaka N Loss of p53 enhances catalytic activity of IKKbeta through O-linked beta-N-acetyl glucosamine modification. Proc Natl Acad Sci U S A 2009, 106:3431-3436.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 3431-3436
    • Kawauchi, K.1    Araki, K.2    Tobiume, K.3    Tanaka, N.4
  • 94
    • 77952429792 scopus 로고    scopus 로고
    • Nutrient sensor O-GlcNAc transferase regulates breast cancer tumorigenesis through targeting of the oncogenic transcription factor FoxM1
    • Caldwell SA, Jackson SR, Shahriari KS, Lynch TP, 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.
    • (2010) Oncogene , vol.29 , pp. 2831-2842
    • Caldwell, S.A.1    Jackson, S.R.2    Shahriari, K.S.3    Lynch, T.P.4    Sethi, G.5    Walker, S.6
  • 95
    • 71749108365 scopus 로고    scopus 로고
    • O-GlcNAc protein modification in cancer cells increases in response to glucose deprivation through glycogen degradation
    • Kang JG, Park SY, Ji S, Jang I, Park S, Kim HS, et al. O-GlcNAc protein modification in cancer cells increases in response to glucose deprivation through glycogen degradation. J Biol Chem 2009, 284:34777-34784.
    • (2009) J Biol Chem , vol.284 , pp. 34777-34784
    • Kang, J.G.1    Park, S.Y.2    Ji, S.3    Jang, I.4    Park, S.5    Kim, H.S.6
  • 96
    • 45149095784 scopus 로고    scopus 로고
    • AMP-activated protein kinase and p38 MAPK activate O-GlcNAcylation of neuronal proteins during glucose deprivation
    • Cheung WD, Hart GW AMP-activated protein kinase and p38 MAPK activate O-GlcNAcylation of neuronal proteins during glucose deprivation. J Biol Chem 2008, 283:13009-13020.
    • (2008) J Biol Chem , vol.283 , pp. 13009-13020
    • Cheung, W.D.1    Hart, G.W.2
  • 97
    • 35348866703 scopus 로고    scopus 로고
    • O-GlcNAc modification in diabetes and Alzheimer's disease
    • Dias WB, Hart GW O-GlcNAc modification in diabetes and Alzheimer's disease. Mol Biosyst 2007, 3:766-772.
    • (2007) Mol Biosyst , vol.3 , pp. 766-772
    • Dias, W.B.1    Hart, G.W.2
  • 98
    • 77949283280 scopus 로고    scopus 로고
    • Dysregulation of the nutrient/stress sensor O-GlcNAcylation is involved in the etiology of cardiovascular disorders, type-2 diabetes and Alzhe-imer's disease
    • Lefebvre T, Dehennaut V, Guinez C, Olivier S, Drougat L, Mir AM, et al. Dysregulation of the nutrient/stress sensor O-GlcNAcylation is involved in the etiology of cardiovascular disorders, type-2 diabetes and Alzhe-imer's disease. Biochim Biophys Acta 2010, 1800:67-79.
    • (2010) Biochim Biophys Acta , vol.1800 , pp. 67-79
    • Lefebvre, T.1    Dehennaut, V.2    Guinez, C.3    Olivier, S.4    Drougat, L.5    Mir, A.M.6
  • 99
    • 47649114560 scopus 로고    scopus 로고
    • A potent mechanism-inspired O-Glc-NAcase inhibitor that blocks phosphorylation of tau in vivo
    • Yuzwa SA, Macauley MS, Heinonen JE, Shan X, Dennis RJ, He Y, et al. A potent mechanism-inspired O-Glc-NAcase inhibitor that blocks phosphorylation of tau in vivo. Nat Chem Biol 2008, 4:483-490.
    • (2008) Nat Chem Biol , vol.4 , pp. 483-490
    • Yuzwa, S.A.1    Macauley, M.S.2    Heinonen, J.E.3    Shan, X.4    Dennis, R.J.5    He, Y.6
  • 100
    • 79251611901 scopus 로고    scopus 로고
    • Structure of human O-GlcNAc transferase and its complex with a peptide substrate
    • Lazarus MB, Nam Y, Jiang J, Sliz P, Walker S. Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature; 469:564-7.
    • Nature , vol.469 , pp. 564-7
    • Lazarus, M.B.1    Nam, Y.2    Jiang, J.3    Sliz, P.4    Walker, S.5


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