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Volumn 112, Issue 51, 2015, Pages 15648-15653

Discovery of a nucleocytoplasmic O-mannose glycoproteome in yeast

Author keywords

Glycoproteomics; Mass spectrometry; O glycosylation; Signaling; Yeast

Indexed keywords

ALPHA MANNOSIDASE; CADHERIN; GLYCOGEN PHOSPHORYLASE; GLYCOPROTEIN; HISTONE H2B; MANNITOL PLUS SORBITOL; MITOCHONDRIAL PROTEIN; NUCLEOCYTOPLASMIC O MANNOSE; PROTEOME; UNCLASSIFIED DRUG; MANNOSE; N ACETYLGLUCOSAMINE;

EID: 84952674063     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1511743112     Document Type: Article
Times cited : (62)

References (39)
  • 1
    • 34247583996 scopus 로고    scopus 로고
    • Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins
    • Hart GW, Housley MP, Slawson C (2007) Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins. Nature 446(7139):1017-1022.
    • (2007) Nature , vol.446 , Issue.7139 , pp. 1017-1022
    • Hart, G.W.1    Housley, M.P.2    Slawson, C.3
  • 2
    • 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 (1984) Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. J Biol Chem 259(5):3308-3317.
    • (1984) J Biol Chem , vol.259 , Issue.5 , pp. 3308-3317
    • Torres, C.R.1    Hart, G.W.2
  • 3
    • 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 (1986) The subcellular distribution of terminal N-acetylglucosamine moieties. Localization of a novel protein-saccharide linkage, O-linked GlcNAc. J Biol Chem 261(17):8049-8057.
    • (1986) J Biol Chem , vol.261 , Issue.17 , pp. 8049-8057
    • Holt, G.D.1    Hart, G.W.2
  • 4
    • 0026795976 scopus 로고
    • Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine: Polypeptide beta-N-acetylglucosaminyltransferase
    • Haltiwanger RS, Blomberg MA, Hart GW (1992) Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine: polypeptide beta-N-acetylglucosaminyltransferase. J Biol Chem 267(13):9005-9013.
    • (1992) J Biol Chem , vol.267 , Issue.13 , pp. 9005-9013
    • Haltiwanger, R.S.1    Blomberg, M.A.2    Hart, G.W.3
  • 5
    • 0028085881 scopus 로고
    • Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol
    • Dong DL, Hart GW (1994) Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol. J Biol Chem 269(30):19321-19330.
    • (1994) J Biol Chem , vol.269 , Issue.30 , pp. 19321-19330
    • Dong, D.L.1    Hart, G.W.2
  • 6
    • 79959381299 scopus 로고    scopus 로고
    • Cross talk between O-GlcNAcylation and phosphorylation: Roles in signaling, transcription, and chronic disease
    • Hart GW, Slawson C, Ramirez-Correa G, Lagerlof O (2011) Cross talk between O-GlcNAcylation and phosphorylation: Roles in signaling, transcription, and chronic disease. Annu Rev Biochem 80:825-858.
    • (2011) Annu Rev Biochem , vol.80 , pp. 825-858
    • Hart, G.W.1    Slawson, C.2    Ramirez-Correa, G.3    Lagerlof, O.4
  • 7
    • 84928254126 scopus 로고    scopus 로고
    • A little sugar goes a long way: The cell biology of O-GlcNAc
    • Bond MR, Hanover JA (2015) A little sugar goes a long way: The cell biology of O-GlcNAc. J Cell Biol 208(7):869-880.
    • (2015) J Cell Biol , vol.208 , Issue.7 , pp. 869-880
    • Bond, M.R.1    Hanover, J.A.2
  • 8
    • 84905723395 scopus 로고    scopus 로고
    • Nutrient regulation of signaling, transcription, and cell physiology by O-GlcNAcylation
    • Hardivillé S, Hart GW (2014) Nutrient regulation of signaling, transcription, and cell physiology by O-GlcNAcylation. Cell Metab 20(2):208-213.
    • (2014) Cell Metab , vol.20 , Issue.2 , pp. 208-213
    • Hardivillé, S.1    Hart, G.W.2
  • 9
    • 77953138098 scopus 로고    scopus 로고
    • Site-specific interplay between O-GlcNAcylation and phosphorylation in cellular regulation
    • Hu P, Shimoji S, Hart GW (2010) Site-specific interplay between O-GlcNAcylation and phosphorylation in cellular regulation. FEBS Lett 584(12):2526-2538.
    • (2010) FEBS Lett , vol.584 , Issue.12 , pp. 2526-2538
    • Hu, P.1    Shimoji, S.2    Hart, G.W.3
  • 10
    • 33847778786 scopus 로고    scopus 로고
    • Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry
    • Chi A, et al. (2007) Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry. Proc Natl Acad Sci USA 104(7):2193-2198.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.7 , pp. 2193-2198
    • Chi, A.1
  • 11
    • 84880633496 scopus 로고    scopus 로고
    • Protein O-mannosylation: What we have learned from baker's yeast
    • Loibl M, Strahl S (2013) Protein O-mannosylation: What we have learned from baker's yeast. Biochim Biophys Acta 1833(11):2438-2446.
    • (2013) Biochim Biophys Acta , vol.1833 , Issue.11 , pp. 2438-2446
    • Loibl, M.1    Strahl, S.2
  • 12
    • 67650159384 scopus 로고    scopus 로고
    • Protein O-mannosylation: Conserved from bacteria to humans
    • Lommel M, Strahl S (2009) Protein O-mannosylation: Conserved from bacteria to humans. Glycobiology 19(8):816-828.
    • (2009) Glycobiology , vol.19 , Issue.8 , pp. 816-828
    • Lommel, M.1    Strahl, S.2
  • 13
    • 84941114402 scopus 로고    scopus 로고
    • Glycobiology of α-dystroglycan and muscular dystrophy
    • Endo T (2015) Glycobiology of α-dystroglycan and muscular dystrophy. J Biochem 157(1):1-12.
    • (2015) J Biochem , vol.157 , Issue.1 , pp. 1-12
    • Endo, T.1
  • 14
    • 0029954105 scopus 로고    scopus 로고
    • The PMT gene family: Protein O-glycosylation in Saccharomyces cerevisiae is vital
    • Gentzsch M, Tanner W (1996) The PMT gene family: Protein O-glycosylation in Saccharomyces cerevisiae is vital. EMBO J 15(21):5752-5759.
    • (1996) EMBO J , vol.15 , Issue.21 , pp. 5752-5759
    • Gentzsch, M.1    Tanner, W.2
  • 15
    • 79952453315 scopus 로고    scopus 로고
    • Functional and genomic analyses of blocked protein O-mannosylation in baker's yeast
    • Arroyo J, et al. (2011) Functional and genomic analyses of blocked protein O-mannosylation in baker's yeast. Mol Microbiol 79(6):1529-1546.
    • (2011) Mol Microbiol , vol.79 , Issue.6 , pp. 1529-1546
    • Arroyo, J.1
  • 16
    • 84891368942 scopus 로고    scopus 로고
    • Mining the O-mannose glycoproteome reveals cadherins as major O-mannosylated glycoproteins
    • Vester-Christensen MB, et al. (2013) Mining the O-mannose glycoproteome reveals cadherins as major O-mannosylated glycoproteins. Proc Natl Acad Sci USA 110(52):21018-21023.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.52 , pp. 21018-21023
    • Vester-Christensen, M.B.1
  • 17
    • 0029360464 scopus 로고
    • Plant nuclear pore complex proteins are modified by novel oligosaccharides with terminal N-acetylglucosamine
    • Heese-Peck A, Cole RN, Borkhsenious ON, Hart GW, Raikhel NV (1995) Plant nuclear pore complex proteins are modified by novel oligosaccharides with terminal N-acetylglucosamine. Plant Cell 7(9):1459-1471.
    • (1995) Plant Cell , vol.7 , Issue.9 , pp. 1459-1471
    • Heese-Peck, A.1    Cole, R.N.2    Borkhsenious, O.N.3    Hart, G.W.4    Raikhel, N.V.5
  • 18
    • 57449105428 scopus 로고    scopus 로고
    • PhosphoPep-A database of protein phosphorylation sites in model organisms
    • Bodenmiller B, et al. (2008) PhosphoPep-A database of protein phosphorylation sites in model organisms. Nat Biotechnol 26(12):1339-1340.
    • (2008) Nat Biotechnol , vol.26 , Issue.12 , pp. 1339-1340
    • Bodenmiller, B.1
  • 19
    • 78651277460 scopus 로고    scopus 로고
    • PHOSIDA 2011: The posttranslational modification database
    • Database issue
    • Gnad F, Gunawardena J, Mann M (2011) PHOSIDA 2011: The posttranslational modification database. Nucleic Acids Res 39 (Database issue):D253-D260.
    • (2011) Nucleic Acids Res , vol.39 , pp. D253-D260
    • Gnad, F.1    Gunawardena, J.2    Mann, M.3
  • 20
    • 84857047339 scopus 로고    scopus 로고
    • PhosphoSitePlus: A comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
    • Database issue
    • Hornbeck PV, et al. (2012) PhosphoSitePlus: A comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res 40 (Database issue):D261-D270.
    • (2012) Nucleic Acids Res , vol.40 , pp. D261-D270
    • Hornbeck, P.V.1
  • 22
    • 0015241461 scopus 로고
    • Purification and properties of yeast glycogen phosphorylase a and b
    • Fosset M, Muir LW, Nielsen LD, Fischer EH (1971) Purification and properties of yeast glycogen phosphorylase a and b. Biochemistry 10(22):4105-4113.
    • (1971) Biochemistry , vol.10 , Issue.22 , pp. 4105-4113
    • Fosset, M.1    Muir, L.W.2    Nielsen, L.D.3    Fischer, E.H.4
  • 23
    • 0028866974 scopus 로고
    • Mechanism of regulation in yeast glycogen phosphorylase
    • Lin K, Hwang PK, Fletterick RJ (1995) Mechanism of regulation in yeast glycogen phosphorylase. J Biol Chem 270(45):26833-26839.
    • (1995) J Biol Chem , vol.270 , Issue.45 , pp. 26833-26839
    • Lin, K.1    Hwang, P.K.2    Fletterick, R.J.3
  • 24
    • 84864812302 scopus 로고    scopus 로고
    • Global identification and characterization of both O-GlcNAcylation and phosphorylation at the murine synapse
    • Trinidad JC, et al. (2012) Global identification and characterization of both O-GlcNAcylation and phosphorylation at the murine synapse. Mol Cell Proteomics 11(8):215-229.
    • (2012) Mol Cell Proteomics , vol.11 , Issue.8 , pp. 215-229
    • Trinidad, J.C.1
  • 25
    • 84860811239 scopus 로고    scopus 로고
    • Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-specific O-GlcNAc transferase targets
    • Alfaro JF, et al. (2012) Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-specific O-GlcNAc transferase targets. Proc Natl Acad Sci USA 109(19):7280-7285.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.19 , pp. 7280-7285
    • Alfaro, J.F.1
  • 26
    • 84884890368 scopus 로고    scopus 로고
    • Discovery and confirmation of O-GlcNAcylated proteins in rat liver mitochondria by combination of mass spectrometry and immunological methods
    • Cao W, et al. (2013) Discovery and confirmation of O-GlcNAcylated proteins in rat liver mitochondria by combination of mass spectrometry and immunological methods. PLoS One 8(10):e76399.
    • (2013) PLoS One , vol.8 , Issue.10 , pp. e76399
    • Cao, W.1
  • 27
    • 79953652899 scopus 로고    scopus 로고
    • DbOGAP-An integrated bioinformatics resource for protein O-GlcNAcylation
    • Wang J, Torii M, Liu H, Hart GW, Hu ZZ (2011) dbOGAP-An integrated bioinformatics resource for protein O-GlcNAcylation. BMC Bioinformatics 12:91.
    • (2011) BMC Bioinformatics , vol.12 , pp. 91
    • Wang, J.1    Torii, M.2    Liu, H.3    Hart, G.W.4    Hu, Z.Z.5
  • 28
    • 84943812931 scopus 로고    scopus 로고
    • Undetectable histone O-GlcNAcylation in mammalian cells
    • Gagnon J, et al. (2015) Undetectable histone O-GlcNAcylation in mammalian cells. Epigenetics 10(8):677-691.
    • (2015) Epigenetics , vol.10 , Issue.8 , pp. 677-691
    • Gagnon, J.1
  • 29
    • 78650447665 scopus 로고    scopus 로고
    • Beta-N-acetylglucosamine (O-GlcNAc) is part of the histone code
    • Sakabe K, Wang Z, Hart GW (2010) Beta-N-acetylglucosamine (O-GlcNAc) is part of the histone code. Proc Natl Acad Sci USA 107(46):19915-19920.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.46 , pp. 19915-19920
    • Sakabe, K.1    Wang, Z.2    Hart, G.W.3
  • 30
    • 84355161950 scopus 로고    scopus 로고
    • GlcNAcylation of histone H2B facilitates its monoubiquitination
    • Fujiki R, et al. (2011) GlcNAcylation of histone H2B facilitates its monoubiquitination. Nature 480(7378):557-560.
    • (2011) Nature , vol.480 , Issue.7378 , pp. 557-560
    • Fujiki, R.1
  • 31
    • 0346457229 scopus 로고    scopus 로고
    • Carbohydrates induce mono-ubiquitination of H2B in yeast
    • Dong L, Xu CW (2004) Carbohydrates induce mono-ubiquitination of H2B in yeast. J Biol Chem 279(3):1577-1580.
    • (2004) J Biol Chem , vol.279 , Issue.3 , pp. 1577-1580
    • Dong, L.1    Xu, C.W.2
  • 32
    • 0025101069 scopus 로고
    • The ATP binding site of the yeast plasma membrane proton-translocating ATPase
    • Davis CB, Smith KE, Campbell BN, Jr, Hammes GG (1990) The ATP binding site of the yeast plasma membrane proton-translocating ATPase. J Biol Chem 265(3):1300-1305.
    • (1990) J Biol Chem , vol.265 , Issue.3 , pp. 1300-1305
    • Davis, C.B.1    Smith, K.E.2    Campbell, B.N.3    Hammes, G.G.4
  • 33
    • 37249056940 scopus 로고    scopus 로고
    • Tandem phosphorylation of Ser-911 and Thr-912 at the C terminus of yeast plasma membrane H+-ATPase leads to glucose-dependent activation
    • Lecchi S, et al. (2007) Tandem phosphorylation of Ser-911 and Thr-912 at the C terminus of yeast plasma membrane H+-ATPase leads to glucose-dependent activation. J Biol Chem 282(49):35471-35481.
    • (2007) J Biol Chem , vol.282 , Issue.49 , pp. 35471-35481
    • Lecchi, S.1
  • 34
    • 0021115563 scopus 로고
    • In vivo glucose activation of the yeast plasma membrane ATPase
    • Serrano R (1983) In vivo glucose activation of the yeast plasma membrane ATPase. FEBS Lett 156(1):11-14.
    • (1983) FEBS Lett , vol.156 , Issue.1 , pp. 11-14
    • Serrano, R.1
  • 35
    • 84875974045 scopus 로고    scopus 로고
    • Enhanced mass spectrometric mapping of the human GalNAc-type O-glycoproteome with SimpleCells
    • Vakhrushev SY, et al. (2013) Enhanced mass spectrometric mapping of the human GalNAc-type O-glycoproteome with SimpleCells. Mol Cell Proteomics 12(4):932-944.
    • (2013) Mol Cell Proteomics , vol.12 , Issue.4 , pp. 932-944
    • Vakhrushev, S.Y.1
  • 36
    • 84891796097 scopus 로고    scopus 로고
    • ProteomeXchange provides globally coordinated proteomics data submission and dissemination
    • Vizcaíno JA, et al. (2014) ProteomeXchange provides globally coordinated proteomics data submission and dissemination. Nat Biotechnol 32(3):223-226.
    • (2014) Nat Biotechnol , vol.32 , Issue.3 , pp. 223-226
    • Vizcaíno, J.A.1
  • 37
    • 0347064294 scopus 로고    scopus 로고
    • Elimination of oxidative degradation during the per-O-methylation of carbohydrates
    • Ciucanu I, Costello CE (2003) Elimination of oxidative degradation during the per-O-methylation of carbohydrates. J Am Chem Soc 125(52):16213-16219.
    • (2003) J Am Chem Soc , vol.125 , Issue.52 , pp. 16213-16219
    • Ciucanu, I.1    Costello, C.E.2
  • 39
    • 84858588614 scopus 로고    scopus 로고
    • Saccharomyces genome database: The genomics resource of budding yeast
    • Database issue
    • Cherry JM, et al. (2012) Saccharomyces Genome Database: The genomics resource of budding yeast. Nucleic Acids Res 40 (Database issue):D700-D705.
    • (2012) Nucleic Acids Res , vol.40 , pp. D700-D705
    • Cherry, J.M.1


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