메뉴 건너뛰기




Volumn 45, Issue 6, 2013, Pages

Synapsin-1 and tau reciprocal O-GlcNAcylation and phosphorylation sites in mouse brain synaptosomes

Author keywords

BEMAD; O GlcNAcylation; Phosphorylation; Synapsin 1; Synaptosome; Tau

Indexed keywords

DITHIOTHREITOL; N ACETYLGLUCOSAMINE; O LINKED N ACETYLGLUCOSAMINE; SERINE; SYNAPSIN I; TAU PROTEIN; TITANIUM DIOXIDE; UNCLASSIFIED DRUG; PEPTIDE; SYNAPSIN;

EID: 84881162103     PISSN: 12263613     EISSN: 20926413     Source Type: Journal    
DOI: 10.1038/emm.2013.56     Document Type: Article
Times cited : (18)

References (18)
  • 2
    • 34247583996 scopus 로고    scopus 로고
    • Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins
    • Hart GW, Housley MP, Slawson C. Cycling of O-linked β-N- acetylglucosamine on nucleocytoplasmic proteins. Nature 2007; 446: 1017-1022.
    • (2007) Nature , vol.446 , pp. 1017-1022
    • Hart, G.W.1    Housley, M.P.2    Slawson, C.3
  • 3
    • 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. Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease. Ann Rev Biochem 2011; 80: 825.
    • (2011) Ann Rev Biochem , vol.80 , pp. 825
    • Hart, G.W.1    Slawson, C.2    Ramirez-Correa, G.3    Lagerlof, O.4
  • 4
    • 78651082539 scopus 로고    scopus 로고
    • O-GlcNAc modification: Why so intimately associated with phosphorylation?
    • Mishra S, Ande S, Salter N. O-GlcNAc modification: why so intimately associated with phosphorylation? Cell Commun Signal 2011; 9: 1.
    • (2011) Cell Commun Signal , vol.9 , pp. 1
    • Mishra, S.1    Ande, S.2    Salter, N.3
  • 5
    • 33646900710 scopus 로고    scopus 로고
    • O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry
    • Vosseller K, Trinidad JC, Chalkley RJ, Specht CG, Thalhammer A, Lynn AJ et 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.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 923-934
    • Vosseller, K.1    Trinidad, J.C.2    Chalkley, R.J.3    Specht, C.G.4    Thalhammer, A.5    Lynn, A.J.6
  • 6
    • 84864812302 scopus 로고    scopus 로고
    • Global identification and characterization of both O-GlcNAcylation and phosphorylation at the murine synapse
    • Trinidad JC, Barkan DT, Gulledge BF, Thalhammer A, Sali A, Schoepfer R et al. Global identification and characterization of both O-GlcNAcylation and phosphorylation at the murine synapse. Mol Cell Proteomics 2012; 11: 215-229.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 215-229
    • Trinidad, J.C.1    Barkan, D.T.2    Gulledge, B.F.3    Thalhammer, A.4    Sali, A.5    Schoepfer, R.6
  • 7
    • 34548438595 scopus 로고    scopus 로고
    • Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation
    • 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.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1365-1379
    • Wang, Z.1    Pandey, A.2    Hart, G.W.3
  • 8
    • 0001607910 scopus 로고    scopus 로고
    • Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications
    • 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.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 791-804
    • Wells, L.1    Vosseller, K.2    Cole, R.N.3    Cronshaw, J.M.4    Matunis, M.J.5    Hart, G.W.6
  • 9
    • 0036024971 scopus 로고    scopus 로고
    • Isolation of biogenetically competent mitochondria from mammalian tissues and cultured cells
    • Fernández-Vizarra E, López-Pérez MJ, Enriquez JA. Isolation of biogenetically competent mitochondria from mammalian tissues and cultured cells. Methods 2002; 26: 292-297.
    • (2002) Methods , vol.26 , pp. 292-297
    • Fernández-Vizarra, E.1    López-Pérez, M.J.2    Enriquez, J.A.3
  • 10
    • 79953652899 scopus 로고    scopus 로고
    • DbOGAP - An integrated bioinformatics resource for protein O-GlcNAcylation
    • Wang J, Torii M, Liu H, Hart GW, Hu Z-Z. dbOGAP-an integrated bioinformatics resource for protein O-GlcNAcylation. BMC Bioinform 2011; 12: 91.
    • (2011) BMC Bioinform , vol.12 , pp. 91
    • Wang, J.1    Torii, M.2    Liu, H.3    Hart, G.W.4    Hu, Z.-Z.5
  • 11
    • 0033579464 scopus 로고    scopus 로고
    • Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
    • Blom N, Gammeltoft S, Brunak S. Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol 1999; 294: 1351.
    • (1999) J Mol Biol , vol.294 , pp. 1351
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 12
    • 0036370537 scopus 로고    scopus 로고
    • Prediction of glycosylation across the human proteome and the correlation to protein function
    • Gupta R, Brunak S. Prediction of glycosylation across the human proteome and the correlation to protein function. Pac Symp Biocomput 2002; 7: 310-322.
    • (2002) Pac Symp Biocomput , vol.7 , pp. 310-322
    • Gupta, R.1    Brunak, S.2
  • 14
    • 0035887768 scopus 로고    scopus 로고
    • Opposing changes in phosphorylation of specific sites in synapsin i during Ca2+-dependent glutamate release in isolated nerve terminals
    • Jovanovic JN, Sihra TS, Nairn AC, Hemmings HC, Greengard P, Czernik AJ. Opposing changes in phosphorylation of specific sites in synapsin I during Ca2+-dependent glutamate release in isolated nerve terminals. J Neurosci 2001; 21: 7944-7953.
    • (2001) J Neurosci , vol.21 , pp. 7944-7953
    • Jovanovic, J.N.1    Sihra, T.S.2    Nairn, A.C.3    Hemmings, H.C.4    Greengard, P.5    Czernik, A.J.6
  • 15
    • 3242739968 scopus 로고    scopus 로고
    • O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease
    • Liu F, Iqbal K, Grundke-Iqbal I, Hart GW, Gong C-X. O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer's disease. Proc Natl Acad Sci USA 2004; 101: 10804-10809.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10804-10809
    • Liu, F.1    Iqbal, K.2    Grundke-Iqbal, I.3    Hart, G.W.4    Gong, C.-X.5
  • 16
    • 38049121347 scopus 로고    scopus 로고
    • Regulation between O-GlcNAcylation and phosphorylation of neurofilament-M and their dysregulation in Alzheimer disease
    • Deng Y, Li B, Liu F, Iqbal K, Grundke-Iqbal I, Brandt R et al. Regulation between O-GlcNAcylation and phosphorylation of neurofilament-M and their dysregulation in Alzheimer disease. FASEB J 2008; 22: 138-145.
    • (2008) FASEB J , vol.22 , pp. 138-145
    • Deng, Y.1    Li, B.2    Liu, F.3    Iqbal, K.4    Grundke-Iqbal, I.5    Brandt, R.6
  • 17
    • 58649120835 scopus 로고    scopus 로고
    • In vivo modulation of O-GlcNAc levels regulates hippocampal synaptic plasticity through interplay with phosphorylation
    • Tallent MK, Varghis N, Skorobogatko Y, Hernandez-Cuebas L, Whelan K, Vocadlo DJ et al. In vivo modulation of O-GlcNAc levels regulates hippocampal synaptic plasticity through interplay with phosphorylation. J Biol Chem 2009; 284: 174-181.
    • (2009) J Biol Chem , vol.284 , pp. 174-181
    • Tallent, M.K.1    Varghis, N.2    Skorobogatko, Y.3    Hernandez-Cuebas, L.4    Whelan, K.5    Vocadlo, D.J.6
  • 18
    • 33646008860 scopus 로고    scopus 로고
    • Concurrent alterations of O-GlcNAcylation and phosphorylation of tau in mouse brains during fasting
    • Li X, Lu F, Wang JZ, Gong CX. Concurrent alterations of O-GlcNAcylation and phosphorylation of tau in mouse brains during fasting. Eur J Neurosci 2006; 23: 2078-2086.
    • (2006) Eur J Neurosci , vol.23 , pp. 2078-2086
    • Li, X.1    Lu, F.2    Wang, J.Z.3    Gong, C.X.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.