메뉴 건너뛰기




Volumn 9, Issue 4, 2014, Pages

Evolutionarily conserved pattern of AMPA receptor subunit glycosylation in mammalian frontal cortex

Author keywords

[No Author keywords available]

Indexed keywords

AMPA RECEPTOR; ENDOGLYCOSIDASE H; FUCOSE; GLYCOPEPTIDASE; MEMBRANE PROTEIN; N ACETYLGLUCOSAMINE; PROTEIN GLUA2; PROTEIN GLUA4; UNCLASSIFIED DRUG; LECTIN; POLYSACCHARIDE; PROTEIN BINDING; PROTEIN SUBUNIT;

EID: 84899457020     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0094255     Document Type: Article
Times cited : (13)

References (30)
  • 2
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler R, Hermjakob H, Sharon N (1999) On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim Biophys Acta 1473: 4-8.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 3
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • Zielinska DF, Gnad F, Wisniewski JR, Mann M (2010) Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell 141: 897-907.
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wisniewski, J.R.3    Mann, M.4
  • 5
    • 0036483593 scopus 로고    scopus 로고
    • The structure and function of glutamate receptor ion channels
    • Madden DR (2002) The structure and function of glutamate receptor ion channels. Nat Rev Neurosci 3: 91-101.
    • (2002) Nat Rev Neurosci , vol.3 , pp. 91-101
    • Madden, D.R.1
  • 6
    • 5344241223 scopus 로고    scopus 로고
    • LTP and LTD: An embarrassment of riches
    • Malenka RC, Bear MF (2004) LTP and LTD: an embarrassment of riches. Neuron 44: 5-21.
    • (2004) Neuron , vol.44 , pp. 5-21
    • Malenka, R.C.1    Bear, M.F.2
  • 7
    • 0026505331 scopus 로고
    • Topography of glycosylation reactions in the endoplasmic reticulum
    • Abeijon C, Hirschberg CB (1992) Topography of glycosylation reactions in the endoplasmic reticulum. Trends Biochem Sci 17: 32-36.
    • (1992) Trends Biochem Sci , vol.17 , pp. 32-36
    • Abeijon, C.1    Hirschberg, C.B.2
  • 8
    • 0030729835 scopus 로고    scopus 로고
    • N-Glycosylation is not a prerequisite for glutamate receptor function but is essential for lectin modulation
    • Everts I, Villmann C, Hollmann M (1997) N-Glycosylation is not a prerequisite for glutamate receptor function but is essential for lectin modulation. Mol Pharmacol 52: 861-873.
    • (1997) Mol Pharmacol , vol.52 , pp. 861-873
    • Everts, I.1    Villmann, C.2    Hollmann, M.3
  • 9
    • 0023068345 scopus 로고
    • Topography of glycosylation in the rough endoplasmic reticulum and Golgi apparatus
    • Hirschberg CB, Snider MD (1987) Topography of glycosylation in the rough endoplasmic reticulum and Golgi apparatus. Annu Rev Biochem 56: 63-87.
    • (1987) Annu Rev Biochem , vol.56 , pp. 63-87
    • Hirschberg, C.B.1    Snider, M.D.2
  • 10
    • 0028596211 scopus 로고
    • N-glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1
    • Hollmann M, Maron C, Heinemann S (1994) N-glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1. Neuron 13: 1331-1343.
    • (1994) Neuron , vol.13 , pp. 1331-1343
    • Hollmann, M.1    Maron, C.2    Heinemann, S.3
  • 11
    • 0033785028 scopus 로고    scopus 로고
    • The role of glycosylation in ionotropic glutamate receptor ligand binding, function, and trafficking
    • Standley S, Baudry M (2000) The role of glycosylation in ionotropic glutamate receptor ligand binding, function, and trafficking. Cell Mol Life Sci 57: 1508-1516.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1508-1516
    • Standley, S.1    Baudry, M.2
  • 12
    • 0037343156 scopus 로고    scopus 로고
    • Characterization of the functional role of the N-glycans in the AMPA receptor ligand-binding domain
    • Pasternack A, Coleman SK, Fethiere J, Madden DR, LeCaer JP, et al. (2003) Characterization of the functional role of the N-glycans in the AMPA receptor ligand-binding domain. J Neurochem 84: 1184-1192.
    • (2003) J Neurochem , vol.84 , pp. 1184-1192
    • Pasternack, A.1    Coleman, S.K.2    Fethiere, J.3    Madden, D.R.4    LeCaer, J.P.5
  • 14
    • 71049182589 scopus 로고    scopus 로고
    • HNK-1 glyco-epitope regulates the stability of the glutamate receptor subunit GluR2 on the neuronal cell surface
    • Morita I, Kakuda S, Takeuchi Y, Itoh S, Kawasaki N, et al. (2009) HNK-1 glyco-epitope regulates the stability of the glutamate receptor subunit GluR2 on the neuronal cell surface. J Biol Chem 284: 30209-30217.
    • (2009) J Biol Chem , vol.284 , pp. 30209-30217
    • Morita, I.1    Kakuda, S.2    Takeuchi, Y.3    Itoh, S.4    Kawasaki, N.5
  • 15
    • 70449526388 scopus 로고    scopus 로고
    • HNK-1 (human natural killer-1) glyco-epitope is essential for normal spine morphogenesis in developing hippocampal neurons
    • Morita I, Kakuda S, Takeuchi Y, Kawasaki T, Oka S (2009) HNK-1 (human natural killer-1) glyco-epitope is essential for normal spine morphogenesis in developing hippocampal neurons. Neuroscience 164: 1685-1694.
    • (2009) Neuroscience , vol.164 , pp. 1685-1694
    • Morita, I.1    Kakuda, S.2    Takeuchi, Y.3    Kawasaki, T.4    Oka, S.5
  • 16
    • 84861427459 scopus 로고    scopus 로고
    • Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery
    • Zielinska DF, Gnad F, Schropp K, Wisniewski JR, Mann M (2012) Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548.
    • (2012) Mol Cell , vol.46 , pp. 542-548
    • Zielinska, D.F.1    Gnad, F.2    Schropp, K.3    Wisniewski, J.R.4    Mann, M.5
  • 18
    • 34250205191 scopus 로고    scopus 로고
    • The role of the GluR2 subunit in AMPA receptor function and synaptic plasticity
    • Isaac JTR, Ashby MC, McBain CJ (2007) The role of the GluR2 subunit in AMPA receptor function and synaptic plasticity. Neuron 54: 859-871.
    • (2007) Neuron , vol.54 , pp. 859-871
    • Isaac, J.T.R.1    Ashby, M.C.2    McBain, C.J.3
  • 19
    • 75749138515 scopus 로고    scopus 로고
    • Abnormal glycosylation of EAAT1 and EAAT2 in prefrontal cortex of elderly patients with schizophrenia
    • Bauer D, Haroutunian V, Meador-Woodruff JH, McCullumsmith RE (2010) Abnormal glycosylation of EAAT1 and EAAT2 in prefrontal cortex of elderly patients with schizophrenia. Schizophr Res 117: 92-98.
    • (2010) Schizophr Res , vol.117 , pp. 92-98
    • Bauer, D.1    Haroutunian, V.2    Meador-Woodruff, J.H.3    McCullumsmith, R.E.4
  • 20
    • 50249161203 scopus 로고    scopus 로고
    • Abnormal expression of glutamate transporter and transporter interacting molecules in prefrontal cortex in elderly patients with schizophrenia
    • Bauer D, Gupta D, Harotunian V, Meador-Woodruff JH, McCullumsmith RE (2008) Abnormal expression of glutamate transporter and transporter interacting molecules in prefrontal cortex in elderly patients with schizophrenia. Schizophr Res 104: 108-120.
    • (2008) Schizophr Res , vol.104 , pp. 108-120
    • Bauer, D.1    Gupta, D.2    Harotunian, V.3    Meador-Woodruff, J.H.4    McCullumsmith, R.E.5
  • 21
    • 84877126705 scopus 로고    scopus 로고
    • Transmembrane AMPA receptor regulatory protein (TARP) dysregulation in anterior cingulate cortex in schizophrenia
    • Drummond JB, Tucholski J, Haroutunian V, Meador-Woodruff JH (2013) Transmembrane AMPA receptor regulatory protein (TARP) dysregulation in anterior cingulate cortex in schizophrenia. Schizophr Res 147: 32-38.
    • (2013) Schizophr Res , vol.147 , pp. 32-38
    • Drummond, J.B.1    Tucholski, J.2    Haroutunian, V.3    Meador-Woodruff, J.H.4
  • 22
    • 39549123816 scopus 로고    scopus 로고
    • Endoglycosidase and glycoamidase release of N-linked oligosaccharides
    • Chapter 17: Unit17 13A
    • Freeze HH (2001) Endoglycosidase and glycoamidase release of N-linked oligosaccharides. Curr Protoc Mol Biol Chapter 17: Unit17 13A.
    • (2001) Curr Protoc Mol Biol
    • Freeze, H.H.1
  • 23
    • 59749086716 scopus 로고    scopus 로고
    • Specificity analysis of lectins and antibodies using remodeled glycoproteins
    • Iskratsch T, Braun A, Paschinger K, Wilson IB (2009) Specificity analysis of lectins and antibodies using remodeled glycoproteins. Anal Biochem 386: 133-146.
    • (2009) Anal Biochem , vol.386 , pp. 133-146
    • Iskratsch, T.1    Braun, A.2    Paschinger, K.3    Wilson, I.B.4
  • 25
    • 0031745290 scopus 로고    scopus 로고
    • Identification of lectin-purified neural glycoproteins, GPs 180, 116, and 110, with NMDA and AMPA receptor subunits: Conservation of glycosylation at the synapse
    • Clark RA, Gurd JW, Bissoon N, Tricaud N, Molnar E, et al. (1998) Identification of lectin-purified neural glycoproteins, GPs 180, 116, and 110, with NMDA and AMPA receptor subunits: conservation of glycosylation at the synapse. J Neurochem 70: 2594-2605.
    • (1998) J Neurochem , vol.70 , pp. 2594-2605
    • Clark, R.A.1    Gurd, J.W.2    Bissoon, N.3    Tricaud, N.4    Molnar, E.5
  • 26
    • 0032763888 scopus 로고    scopus 로고
    • Evolutionary considerations in relating oligosaccharide diversity to biological function
    • Gagneux P, Varki A (1999) Evolutionary considerations in relating oligosaccharide diversity to biological function. Glycobiology 9: 747-755.
    • (1999) Glycobiology , vol.9 , pp. 747-755
    • Gagneux, P.1    Varki, A.2
  • 27
    • 0025923253 scopus 로고
    • Peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase F cannot release glycans with fucose attached alpha 1-3 to the asparagine-linked N-acetylglucosamine residue
    • Tretter V, Altmann F, Marz L (1991) Peptide-N4-(N-acetyl-beta- glucosaminyl) asparagine amidase F cannot release glycans with fucose attached alpha 1-3 to the asparagine-linked N-acetylglucosamine residue. Eur J Biochem 199: 647-652.
    • (1991) Eur J Biochem , vol.199 , pp. 647-652
    • Tretter, V.1    Altmann, F.2    Marz, L.3
  • 28
    • 0242573188 scopus 로고    scopus 로고
    • AMPA receptor tetramerization is mediated by Q/R editing
    • Greger IH, Khatri L, Kong X, Ziff EB (2003) AMPA receptor tetramerization is mediated by Q/R editing. Neuron 40: 763-774.
    • (2003) Neuron , vol.40 , pp. 763-774
    • Greger, I.H.1    Khatri, L.2    Kong, X.3    Ziff, E.B.4
  • 29
    • 0037198702 scopus 로고    scopus 로고
    • RNA editing at arg607 controls AMPA receptor exit from the endoplasmic reticulum
    • Greger IH, Khatri L, Ziff EB (2002) RNA editing at arg607 controls AMPA receptor exit from the endoplasmic reticulum. Neuron 34: 759-772.
    • (2002) Neuron , vol.34 , pp. 759-772
    • Greger, I.H.1    Khatri, L.2    Ziff, E.B.3
  • 30
    • 0031798679 scopus 로고    scopus 로고
    • 3H]AMPA) binding sites represent immature and mature forms of AMPA receptors and are composed of differentially glycosylated subunits
    • 3H]AMPA) binding sites represent immature and mature forms of AMPA receptors and are composed of differentially glycosylated subunits. J Neurochem 70: 2434-2445.
    • (1998) J Neurochem , vol.70 , pp. 2434-2445
    • Standley, S.1    Tocco, G.2    Wagle, N.3    Baudry, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.