메뉴 건너뛰기




Volumn 21, Issue 1, 1998, Pages 99-110

The AMPA receptor GluR2 C terminus can mediate a reversible, ATP- dependent interaction with NSF and α- and β-SNAPs

Author keywords

[No Author keywords available]

Indexed keywords

AMPA RECEPTOR; SYNAPTOSOMAL ASSOCIATED PROTEIN 25;

EID: 0032125884     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(00)80518-8     Document Type: Article
Times cited : (316)

References (43)
  • 1
    • 0024366008 scopus 로고
    • Synaptobrevin: An integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain
    • Baumert, M., Maycox, P.R., Navone, F., De Camilli, P., and Jahn, R. (1989). Synaptobrevin: an integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain. EMBO J 8, 379-384.
    • (1989) EMBO J , vol.8 , pp. 379-384
    • Baumert, M.1    Maycox, P.R.2    Navone, F.3    De Camilli, P.4    Jahn, R.5
  • 2
    • 0029934332 scopus 로고    scopus 로고
    • Relationship between N-methyl-D-aspartate receptor NR1 splice variants and NR2 subunits
    • Blahos, J.N., and Wenthold, R.J. (1996). Relationship between N-methyl-D-aspartate receptor NR1 splice variants and NR2 subunits. J. Biol. Chem. 271, 15669-15674.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15669-15674
    • Blahos, J.N.1    Wenthold, R.J.2
  • 3
    • 0027476024 scopus 로고
    • A synaptic model of memory: Long-term potentiation in the hippocampus
    • Bliss, T.V., and Collingridge, G.L. (1993). A synaptic model of memory: long-term potentiation in the hippocampus. Nature 361, 31-39.
    • (1993) Nature , vol.361 , pp. 31-39
    • Bliss, T.V.1    Collingridge, G.L.2
  • 5
    • 0027226219 scopus 로고
    • Optimized survival of hippocampal neurons in B27-supplemented Neurobasal, a new serum-free medium combination
    • Brewer, G.J., Torricelli, J.R., Evege, E.K., and Price, P.J. (1993). Optimized survival of hippocampal neurons in B27-supplemented Neurobasal, a new serum-free medium combination. J. Neurosci. Res. 35, 567-576.
    • (1993) J. Neurosci. Res. , vol.35 , pp. 567-576
    • Brewer, G.J.1    Torricelli, J.R.2    Evege, E.K.3    Price, P.J.4
  • 6
    • 0026543243 scopus 로고
    • Divalent ion permeability of AMPA receptor channels is dominated by the edited form of a single subunit
    • Burnashev, N., Monyer, H., Seeburg, P.H., and Sakmann, B. (1992). Divalent ion permeability of AMPA receptor channels is dominated by the edited form of a single subunit. Neuron 8, 189-198.
    • (1992) Neuron , vol.8 , pp. 189-198
    • Burnashev, N.1    Monyer, H.2    Seeburg, P.H.3    Sakmann, B.4
  • 7
    • 0025100314 scopus 로고
    • Optimization of differential immunogold-silver and peroxidase labeling with maintenance of ultrastructure in brain sections before plastic embedding
    • Chan, J., Aoki, C., and Pickel, V.M. (1990). Optimization of differential immunogold-silver and peroxidase labeling with maintenance of ultrastructure in brain sections before plastic embedding. Neurosci. Methods 33, 113-127.
    • (1990) Neurosci. Methods , vol.33 , pp. 113-127
    • Chan, J.1    Aoki, C.2    Pickel, V.M.3
  • 8
    • 0029328549 scopus 로고
    • A 200-amino acid ATPase module in search of a basic function
    • Confalonieri, F., and Duguet, M. (1995). A 200-amino acid ATPase module in search of a basic function. Bioessays 17, 639-650.
    • (1995) Bioessays , vol.17 , pp. 639-650
    • Confalonieri, F.1    Duguet, M.2
  • 9
    • 0030900558 scopus 로고    scopus 로고
    • GRIP: A synaptic PDZ domain-containing protein that interacts with AMPA receptors
    • Dong, H., O'Brien, R.J., Fung, E.T., Lanahan, A.A., Worley, P.F., and Huganir, R.L. (1997). GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors. Nature 386, 279-284.
    • (1997) Nature , vol.386 , pp. 279-284
    • Dong, H.1    O'Brien, R.J.2    Fung, E.T.3    Lanahan, A.A.4    Worley, P.F.5    Huganir, R.L.6
  • 10
    • 0029984047 scopus 로고    scopus 로고
    • Regional and ultrastructural distribution of the alpha 8 integrin subunit in developing and adult rat brain suggests a role in synaptic function
    • Einheber, S., Schnapp, L.M., Salzer, J.L., Cappiello, Z.B., and Milner, T.A. (1996). Regional and ultrastructural distribution of the alpha 8 integrin subunit in developing and adult rat brain suggests a role in synaptic function. J. Comp. Neurol. 370, 105-134.
    • (1996) J. Comp. Neurol. , vol.370 , pp. 105-134
    • Einheber, S.1    Schnapp, L.M.2    Salzer, J.L.3    Cappiello, Z.B.4    Milner, T.A.5
  • 12
    • 0029075363 scopus 로고
    • The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin
    • Hanson, P.I., Otto, H., Barton, N., and Jahn, R. (1995). The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin. J. Biol. Chem. 270, 16955-16961.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16955-16961
    • Hanson, P.I.1    Otto, H.2    Barton, N.3    Jahn, R.4
  • 13
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson, P.I., Roth, R., Morisaki, H., Jahn, R., and Heuser, J.E. (1997). Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 90, 523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 14
    • 0030796026 scopus 로고    scopus 로고
    • SNAREs and NSF in targeted membrane fusion
    • Hay, J.C., and Scheller, R.H. (1997). SNAREs and NSF in targeted membrane fusion. Curr. Opin. Cell Biol. 9, 505-512.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 505-512
    • Hay, J.C.1    Scheller, R.H.2
  • 15
    • 0029004741 scopus 로고
    • Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro
    • Hayashi, T., Yamasaki, S., Nauenburg, S., Binz, T., and Niemann, H. (1995). Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro. EMBO J. 14, 2317-2325.
    • (1995) EMBO J. , vol.14 , pp. 2317-2325
    • Hayashi, T.1    Yamasaki, S.2    Nauenburg, S.3    Binz, T.4    Niemann, H.5
  • 17
    • 0028596211 scopus 로고
    • N-glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1
    • Hollmann, M., Maron, C., and 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
  • 18
    • 0028849250 scopus 로고
    • Molecular mechanisms controlling calcium entry through AMPA-type glutamate receptor channels
    • Jonas, P., and Burnashev, N. (1995). Molecular mechanisms controlling calcium entry through AMPA-type glutamate receptor channels. Neuron 15, 987-990.
    • (1995) Neuron , vol.15 , pp. 987-990
    • Jonas, P.1    Burnashev, N.2
  • 20
    • 0030744829 scopus 로고    scopus 로고
    • Interaction of ion channels and receptors with PDZ domain proteins
    • Kornau, H.C., Seeburg, P.H., and Kennedy, M.B. (1997). Interaction of ion channels and receptors with PDZ domain proteins. Curr. Opin. Neurobiol. 7, 368-373.
    • (1997) Curr. Opin. Neurobiol. , vol.7 , pp. 368-373
    • Kornau, H.C.1    Seeburg, P.H.2    Kennedy, M.B.3
  • 21
  • 22
    • 0029980441 scopus 로고    scopus 로고
    • Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles
    • Mayer, A., Wickner, W., and Haas, A. (1996). Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles. Cell 85, 83-94.
    • (1996) Cell , vol.85 , pp. 83-94
    • Mayer, A.1    Wickner, W.2    Haas, A.3
  • 25
    • 0032489499 scopus 로고    scopus 로고
    • Syntaxin 5 is a common component of the NSF-and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro
    • Rabouille, C., Kondo, H., Newman, R., Hui, N., Freemont, P., and Warren, G. (1998). Syntaxin 5 is a common component of the NSF-and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro. Cell 92, 603-610.
    • (1998) Cell , vol.92 , pp. 603-610
    • Rabouille, C.1    Kondo, H.2    Newman, R.3    Hui, N.4    Freemont, P.5    Warren, G.6
  • 27
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J.E. (1994). Mechanisms of intracellular protein transport. Nature 372, 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 28
  • 29
    • 0027234701 scopus 로고
    • The molecular biology of mammalian glutamate receptor channels
    • Seeburg, P. (1993). The molecular biology of mammalian glutamate receptor channels. Trends Neurosci. 16, 359-365.
    • (1993) Trends Neurosci. , vol.16 , pp. 359-365
    • Seeburg, P.1
  • 30
    • 0030031924 scopus 로고    scopus 로고
    • The role of RNA editing in controlling glutamate receptor channel properties
    • Seeburg, P.H. (1996). The role of RNA editing in controlling glutamate receptor channel properties. J. Neurochem. 66, 1-5.
    • (1996) J. Neurochem. , vol.66 , pp. 1-5
    • Seeburg, P.H.1
  • 31
    • 0029025405 scopus 로고
    • Cellular and subcellular localization of syntaxin-like immunoreactivity in the rat striatum and cortex
    • Sesack, S.R., and Snyder, C.L. (1995). Cellular and subcellular localization of syntaxin-like immunoreactivity in the rat striatum and cortex. Neuroscience 67, 993-1007.
    • (1995) Neuroscience , vol.67 , pp. 993-1007
    • Sesack, S.R.1    Snyder, C.L.2
  • 32
    • 0030273003 scopus 로고    scopus 로고
    • PDZs and receptor/channel clustering: Rounding up the latest suspects
    • Sheng, M. (1996). PDZs and receptor/channel clustering: rounding up the latest suspects. Neuron 17, 575-578.
    • (1996) Neuron , vol.17 , pp. 575-578
    • Sheng, M.1
  • 33
    • 0020078977 scopus 로고
    • A simple, rapid, and sensitive method for measuring protein concentration in subcellular membrane fractions prepared by sucrose density ultracentrifugation
    • Simpson, I.A., and Sonne, O. (1982). A simple, rapid, and sensitive method for measuring protein concentration in subcellular membrane fractions prepared by sucrose density ultracentrifugation. Anal. Biochem. 119, 424-427.
    • (1982) Anal. Biochem. , vol.119 , pp. 424-427
    • Simpson, I.A.1    Sonne, O.2
  • 35
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Söllner, T., Bennett, M.K., Whiteheart, S.W., Scheller, R.H., and Rothman, J.E. (1993b). A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 75, 409-418.
    • (1993) Cell , vol.75 , pp. 409-418
    • Söllner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 36
    • 0025995296 scopus 로고
    • RNA editing in brain controls a determinant of ion flow in glutamategated channels
    • Sommer, B., Kohler, M., Sprengel, R., and Seeburg, P.M. (1991). RNA editing in brain controls a determinant of ion flow in glutamategated channels. Cell 67, 11-19.
    • (1991) Cell , vol.67 , pp. 11-19
    • Sommer, B.1    Kohler, M.2    Sprengel, R.3    Seeburg, P.M.4
  • 38
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Südhof, T.C. (1995). The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature 375, 645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 39
    • 0030560773 scopus 로고    scopus 로고
    • Synaptic distribution of the AMPA-GluR2 subunit and its colocalization with calcium-binding proteins in rat cerebral cortex: An immunohistochemical study using a GluR2-specific monoclonal antibody
    • Vissavajjhala, P., Janssen, W.G., Hu, Y., Gazzaley, A.H., Moran, T., Hof, P.R., and Morrison, J.H. (1996). Synaptic distribution of the AMPA-GluR2 subunit and its colocalization with calcium-binding proteins in rat cerebral cortex: an immunohistochemical study using a GluR2-specific monoclonal antibody. Exp. Neurol. 142, 296-312.
    • (1996) Exp. Neurol. , vol.142 , pp. 296-312
    • Vissavajjhala, P.1    Janssen, W.G.2    Hu, Y.3    Gazzaley, A.H.4    Moran, T.5    Hof, P.R.6    Morrison, J.H.7
  • 40
    • 0026651939 scopus 로고
    • The postsynaptic density: Constituent and associated proteins characterized by electrophoresis, immunoblotting, and peptide sequencing
    • Walsh, M.J., and Kuruc, N. (1992). The postsynaptic density: constituent and associated proteins characterized by electrophoresis, immunoblotting, and peptide sequencing. J. Neurochem. 59, 667-678.
    • (1992) J. Neurochem. , vol.59 , pp. 667-678
    • Walsh, M.J.1    Kuruc, N.2
  • 42
    • 0026531244 scopus 로고
    • Immunochemical characterization of the non-NMDA glutamate receptor using subunit-specific antibodies. Evidence for a hetero-oligomeric structure in rat brain
    • Wenthold, R.J., Yokotani, N., Doi, K., and Wada, K. (1992). Immunochemical characterization of the non-NMDA glutamate receptor using subunit-specific antibodies. Evidence for a hetero-oligomeric structure in rat brain. J. Biol. Chem. 267, 501-507.
    • (1992) J. Biol. Chem. , vol.267 , pp. 501-507
    • Wenthold, R.J.1    Yokotani, N.2    Doi, K.3    Wada, K.4
  • 43
    • 0031442806 scopus 로고    scopus 로고
    • Enlightening the postsynaptic density
    • Ziff, E.B. (1997). Enlightening the postsynaptic density. Neuron 19, 1163-1174.
    • (1997) Neuron , vol.19 , pp. 1163-1174
    • Ziff, E.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.