메뉴 건너뛰기




Volumn 8, Issue 1, 1998, Pages 128-138

Forward and reverse genetic approaches to synaptogenesis

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 0031924497     PISSN: 09594388     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-4388(98)80016-0     Document Type: Article
Times cited : (19)

References (64)
  • 1
    • 0027480289 scopus 로고
    • Synaptic structure and development: The neuromuscular junction
    • Hall ZW, Sanes JR. Synaptic structure and development: the neuromuscular junction. Neuron. 10:1993;99-121.
    • (1993) Neuron , vol.10 , pp. 99-121
    • Hall, Z.W.1    Sanes, J.R.2
  • 2
    • 0028027417 scopus 로고
    • Synaptogenesis in Drosphila: Coupling genetics and electrophysiology
    • Broadie KS. Synaptogenesis in Drosphila: coupling genetics and electrophysiology. J Physiol. 88:1994;123-139.
    • (1994) J Physiol , vol.88 , pp. 123-139
    • Broadie, K.S.1
  • 3
    • 0029926999 scopus 로고    scopus 로고
    • The Drosophila neuromuscular junction: A model system for studying synaptic development and function
    • Keshishian H, Broadie K, Chiba A, Bate M. The Drosophila neuromuscular junction: a model system for studying synaptic development and function. Annu Rev Neurosci. 19:1996;545-575.
    • (1996) Annu Rev Neurosci , vol.19 , pp. 545-575
    • Keshishian, H.1    Broadie, K.2    Chiba, A.3    Bate, M.4
  • 4
    • 0028875329 scopus 로고
    • Dynamics of nerve-muscle interaction in developing and mature neuromuscular junctions
    • Grinnell AD. Dynamics of nerve-muscle interaction in developing and mature neuromuscular junctions. Physiol Rev. 75:1995;789-834.
    • (1995) Physiol Rev , vol.75 , pp. 789-834
    • Grinnell, A.D.1
  • 5
    • 0031045636 scopus 로고    scopus 로고
    • Genetic analysis of postsynaptic differentiation at the vertebrate neuromuscular junction
    • Sanes JR. Genetic analysis of postsynaptic differentiation at the vertebrate neuromuscular junction. Curr Opin Neurobiol. 7:1997;93-100.
    • (1997) Curr Opin Neurobiol , vol.7 , pp. 93-100
    • Sanes, J.R.1
  • 6
    • 15844380040 scopus 로고    scopus 로고
    • Agrin acts via a MuSK receptor complex
    • of special interest. Agrin is proposed to play a key role in postsynaptic AChR clustering, but the mechanism of its action remains poorly understood. This study provides strong evidence that agrin acts via a receptor complex that includes MuSK as wel as a MASC. The agrin - MuSK interaction is not direct, but it is suggested that agrin - mediated activation of MuSK is a key step in the AChR aggregation mechanism.
    • Glass DJ, Bowen DC, Stitt TN, Radziejewski C, Bruno J, Ryan TE, Gies DR, Shah S, Mattsson K, Burden SJ, et al. Agrin acts via a MuSK receptor complex. of special interest Cell. 85:1996;513-523 Agrin is proposed to play a key role in postsynaptic AChR clustering, but the mechanism of its action remains poorly understood. This study provides strong evidence that agrin acts via a receptor complex that includes MuSK as wel as a MASC. The agrin - MuSK interaction is not direct, but it is suggested that agrin - mediated activation of MuSK is a key step in the AChR aggregation mechanism.
    • (1996) Cell , vol.85 , pp. 513-523
    • Glass, D.J.1    Bowen, D.C.2    Stitt, T.N.3    Radziejewski, C.4    Bruno, J.5    Ryan, T.E.6    Gies, D.R.7    Shah, S.8    Mattsson, K.9    Burden, S.J.10
  • 7
    • 0029928633 scopus 로고    scopus 로고
    • Agrin-induced acetylcholine-receptor clustering requires tyrosine phosphorylation
    • Ferns M, Deiner M, Hall Z. Agrin-induced acetylcholine-receptor clustering requires tyrosine phosphorylation. J Cell Biol. 132:1996;937-944.
    • (1996) J Cell Biol , vol.132 , pp. 937-944
    • Ferns, M.1    Deiner, M.2    Hall, Z.3
  • 8
    • 0031059146 scopus 로고    scopus 로고
    • ARIA: A neuromuscular junction neuregulin
    • Fishbach GD, Rosen KM. ARIA: a neuromuscular junction neuregulin. Annu Rev Neurosci. 20:1997;429-458.
    • (1997) Annu Rev Neurosci , vol.20 , pp. 429-458
    • Fishbach, G.D.1    Rosen, K.M.2
  • 9
    • 0028846281 scopus 로고
    • Synapse-associated expression of an acetylcholine receptor-inducing protein, ARIA/heregulin, and its putative receptors, ErbB2 and ErbB3, in developing mammalian muscle
    • Moscoso LM, Chu GC, Gautam M, Noakes PG, Merlie JP, Sanes JP. Synapse-associated expression of an acetylcholine receptor-inducing protein, ARIA/heregulin, and its putative receptors, ErbB2 and ErbB3, in developing mammalian muscle. Dev Biol. 172:1995;158-169.
    • (1995) Dev Biol , vol.172 , pp. 158-169
    • Moscoso, L.M.1    Chu, G.C.2    Gautam, M.3    Noakes, P.G.4    Merlie, J.P.5    Sanes, J.P.6
  • 10
    • 0029893117 scopus 로고    scopus 로고
    • Defective neuromuscular synaptogenesis in Agrin-deficient mice
    • of outstanding interest. Over a decade of in vitro evidence suggests that a specific neuronal splice form of agrin is the key inducer of postsynaptic differentiation, including AChR aggregation. This study tests this hypothesis in vivo using agrin knockout mice. AChR aggregation is reduced in the mutant mice but not absent, suggesting that an agrin-independent signal can trigger postsynaptic specialization. In addition, the mutant mice show defects in presynaptic differentiation and synapse-specific transcription. This study has confounded the agrin hypothesis (see [64]) and suggests that further work is necessary to unravel the mechanisms of postsynaptic specialization.
    • Gautam M, Noakes PG, Moscoso LM, Rupp F, Scheller RH, Merlie JP, Sanes JR. Defective neuromuscular synaptogenesis in Agrin-deficient mice. of outstanding interest Cell. 85:1996;525-536 Over a decade of in vitro evidence suggests that a specific neuronal splice form of agrin is the key inducer of postsynaptic differentiation, including AChR aggregation. This study tests this hypothesis in vivo using agrin knockout mice. AChR aggregation is reduced in the mutant mice but not absent, suggesting that an agrin-independent signal can trigger postsynaptic specialization. In addition, the mutant mice show defects in presynaptic differentiation and synapse-specific transcription. This study has confounded the agrin hypothesis (see [64]) and suggests that further work is necessary to unravel the mechanisms of postsynaptic specialization.
    • (1996) Cell , vol.85 , pp. 525-536
    • Gautam, M.1    Noakes, P.G.2    Moscoso, L.M.3    Rupp, F.4    Scheller, R.H.5    Merlie, J.P.6    Sanes, J.R.7
  • 11
    • 15844417385 scopus 로고    scopus 로고
    • The receptor tyrosine kinase MuSK is required for neuromuscular junction formation in vivo
    • of special interest. MuSK is a receptor tyrosine kinase proposed to be part of the agrin receptor complex. This study tests this hypothesis in MuSK knockout mice. Neuromuscular synapses do not form in these mice, suggesting that MuSK is required for all aspects of synapse formation, including postsynaptic specialization, synapse-specific transcription, and presynaptic differentiation.
    • DeChiara TM, Bowen DC, Valenzuela DM, Simmons MV, Poueymirou WT, Thomas S, Kinetz E, Compoton DL, Rojas E, Park JS, et al. The receptor tyrosine kinase MuSK is required for neuromuscular junction formation in vivo. of special interest Cell. 85:1996;501-512 MuSK is a receptor tyrosine kinase proposed to be part of the agrin receptor complex. This study tests this hypothesis in MuSK knockout mice. Neuromuscular synapses do not form in these mice, suggesting that MuSK is required for all aspects of synapse formation, including postsynaptic specialization, synapse-specific transcription, and presynaptic differentiation.
    • (1996) Cell , vol.85 , pp. 501-512
    • Dechiara, T.M.1    Bowen, D.C.2    Valenzuela, D.M.3    Simmons, M.V.4    Poueymirou, W.T.5    Thomas, S.6    Kinetz, E.7    Compoton, D.L.8    Rojas, E.9    Park, J.S.10
  • 12
    • 0031043462 scopus 로고    scopus 로고
    • Agrin inhibits neurite outgrowth but promotes attachment of embryonic motor and sensory neurons
    • Chang D, Woo JS, Campanelli J, Scheller RH, Ignatius MJ. Agrin inhibits neurite outgrowth but promotes attachment of embryonic motor and sensory neurons. Dev Biol. 181:1997;21-35.
    • (1997) Dev Biol , vol.181 , pp. 21-35
    • Chang, D.1    Woo, J.S.2    Campanelli, J.3    Scheller, R.H.4    Ignatius, M.J.5
  • 13
    • 0030919509 scopus 로고    scopus 로고
    • Neuregulins and their receptors: A versatile signaling module in organogenesis and oncogenesis
    • Burden S, Yarden Y. Neuregulins and their receptors: a versatile signaling module in organogenesis and oncogenesis. Neuron. 18:1997;847-855.
    • (1997) Neuron , vol.18 , pp. 847-855
    • Burden, S.1    Yarden, Y.2
  • 15
    • 0031036977 scopus 로고    scopus 로고
    • Subtle neuromuscular defects in utrophin-deficient mice
    • Grady M, Merlie JP, Sanes JR. Subtle neuromuscular defects in utrophin-deficient mice. J Cell Biol. 136:1997;871-872.
    • (1997) J Cell Biol , vol.136 , pp. 871-872
    • Grady, M.1    Merlie, J.P.2    Sanes, J.R.3
  • 17
    • 0029050847 scopus 로고
    • Failure of postsynaptic specialisation to develop at neuromuscular junctions of rapsyn-deficient mice
    • Gautam M, Noakes PG, Mudd J, Nichol M, Chu GC, Sanes JR, Merlie JP. Failure of postsynaptic specialisation to develop at neuromuscular junctions of rapsyn-deficient mice. Nature. 377:1995;232-236.
    • (1995) Nature , vol.377 , pp. 232-236
    • Gautam, M.1    Noakes, P.G.2    Mudd, J.3    Nichol, M.4    Chu, G.C.5    Sanes, J.R.6    Merlie, J.P.7
  • 18
    • 0030940161 scopus 로고    scopus 로고
    • Rapsyn is required for MuSK signaling and recruits synaptic components to a MuSK-containing scaffold
    • of special interest. rapsyn knockout mice fail to cluster any known postsynaptic elements at their NMJs, with the sole exception of MuSK. This finding suggests that MuSK forms a primary structural scaffold to which other postsynaptic components are attached through the action of rapsyn. In addition to this MuSK-rapsyn structural role, the authors show that rapsyn is required for AChR phosphorylation, an early step in MuSK signaling.
    • Apel ED, Glass DJ, Moscoso LM, Yancopoulos GD, Sanes JR. Rapsyn is required for MuSK signaling and recruits synaptic components to a MuSK-containing scaffold. of special interest Neuron. 18:1997;623-635 rapsyn knockout mice fail to cluster any known postsynaptic elements at their NMJs, with the sole exception of MuSK. This finding suggests that MuSK forms a primary structural scaffold to which other postsynaptic components are attached through the action of rapsyn. In addition to this MuSK-rapsyn structural role, the authors show that rapsyn is required for AChR phosphorylation, an early step in MuSK signaling.
    • (1997) Neuron , vol.18 , pp. 623-635
    • Apel, E.D.1    Glass, D.J.2    Moscoso, L.M.3    Yancopoulos, G.D.4    Sanes, J.R.5
  • 19
    • 0025941465 scopus 로고
    • The Discs-Large tumor suppressor gene encodes a guanylate kinase homolog localized to septate junctions
    • Woods DF, Bryant PJ. The Discs-Large tumor suppressor gene encodes a guanylate kinase homolog localized to septate junctions. Cell. 66:1991;451-464.
    • (1991) Cell , vol.66 , pp. 451-464
    • Woods, D.F.1    Bryant, P.J.2
  • 20
    • 0027768992 scopus 로고
    • ZO-1, DLGA and PSD-95/SAP-90: Homologous proteins in tight, septate and synaptic cell junctions
    • Woods DF, Bryant PJ. ZO-1, DLGA and PSD-95/SAP-90: homologous proteins in tight, septate and synaptic cell junctions. Mech Dev. 44:1993;85-89.
    • (1993) Mech Dev , vol.44 , pp. 85-89
    • Woods, D.F.1    Bryant, P.J.2
  • 21
    • 0028091586 scopus 로고
    • The Drosophila tumor suppressor gene dlg is required for normal synaptic bouton structure
    • Lahey T, Gorczyca M, Jia X, Budnik V. the Drosophila tumor suppressor gene dlg is required for normal synaptic bouton structure. Neuron. 13:1994;823-835.
    • (1994) Neuron , vol.13 , pp. 823-835
    • Lahey, T.1    Gorczyca, M.2    Jia, X.3    Budnik, V.4
  • 22
    • 0030273505 scopus 로고    scopus 로고
    • Regulation of synapse structure and function by the Drosophila tumor suppressor gene Discs-Large
    • of special interest. DLG is shown to regulate postsynaptic structural specialization and presynaptic function. The authors use the GAL4 enhancer trap method to show that the level of postsynaptic protein regulates the degree of postsynaptic specialization. Also, surprisingly, presynaptic expression of the protein rescues the postsynaptic defect in dlg mutants, showing that postsynaptic cell.
    • Budnik V, Guan B, Kho Y-H, Hartmann B, Hough C, Woods D, Gorczyca M. Regulation of synapse structure and function by the Drosophila tumor suppressor gene Discs-Large. of special interest Neuron. 17:1996;627-640 DLG is shown to regulate postsynaptic structural specialization and presynaptic function. The authors use the GAL4 enhancer trap method to show that the level of postsynaptic protein regulates the degree of postsynaptic specialization. Also, surprisingly, presynaptic expression of the protein rescues the postsynaptic defect in dlg mutants, showing that postsynaptic cell.
    • (1996) Neuron , vol.17 , pp. 627-640
    • Budnik, V.1    Guan, B.2    Kho Y-H3    Hartmann, B.4    Hough, C.5    Woods, D.6    Gorczyca, M.7
  • 23
    • 0030469153 scopus 로고    scopus 로고
    • Synapse maturation and structural plasticity at Drosophila neuromuscular junctions
    • Budnik V. Synapse maturation and structural plasticity at Drosophila neuromuscular junctions. Curr Opin Neurobiol. 6:1996;858-867.
    • (1996) Curr Opin Neurobiol , vol.6 , pp. 858-867
    • Budnik, V.1
  • 24
    • 0030156251 scopus 로고    scopus 로고
    • The Drosophila tumor suppressor gene, dlg, is involved in structural plasticity at a glutamatergic synapse
    • Guan B, Hartmann B, Kho Y-H, Gorczyca M, Budnik V. The Drosophila tumor suppressor gene, dlg, is involved in structural plasticity at a glutamatergic synapse. Curr Biol. 6:1996;695-706.
    • (1996) Curr Biol , vol.6 , pp. 695-706
    • Guan, B.1    Hartmann, B.2    Kho Y-H3    Gorczyca, M.4    Budnik, V.5
  • 25
    • 0030604722 scopus 로고    scopus 로고
    • Crystal structures of a complexed and peptide-free membrane protein-binding domain: Molecular basis of peptide recognition by PDZ
    • Doyle DA, Lee A, Lewis J, Jim E, Sheng M. Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell. 85:1996;1067-1076.
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.A.1    Lee, A.2    Lewis, J.3    Jim, E.4    Sheng, M.5
  • 26
    • 0029978023 scopus 로고    scopus 로고
    • Clustering membrane proteins: It's all coming together with the PSD-95/SAP-90 protein family
    • Gomperts SN. Clustering membrane proteins: it's all coming together with the PSD-95/SAP-90 protein family. Cell. 84:1996;659-662.
    • (1996) Cell , vol.84 , pp. 659-662
    • Gomperts, S.N.1
  • 27
    • 0030858386 scopus 로고    scopus 로고
    • Characterization of guanylate kinase-associated protein, a postsynaptic density protein at excitatory synapses that interacts directly with postsynaptic density-95/synapse-associated protein 90
    • Naisbitt S, Kim E, Weinberg RJ, Rao A, Yang F-C, Craig AM, Shen M. Characterization of guanylate kinase-associated protein, a postsynaptic density protein at excitatory synapses that interacts directly with postsynaptic density-95/synapse-associated protein 90. J Neurosci. 17:1997;5687-5696.
    • (1997) J Neurosci , vol.17 , pp. 5687-5696
    • Naisbitt, S.1    Kim, E.2    Weinberg, R.J.3    Rao, A.4    Yang F-C5    Craig, A.M.6    Shen, M.7
  • 28
    • 0029098659 scopus 로고
    • Domain intersection between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Komau H-C, Schenker LT, Kennedy MB, Seeburg PH. Domain intersection between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science. 269:1995;1737-1740.
    • (1995) Science , vol.269 , pp. 1737-1740
    • Komau H-C1    Schenker, L.T.2    Kennedy, M.B.3    Seeburg, P.H.4
  • 30
    • 0029788216 scopus 로고    scopus 로고
    • Interaction of the N-methyl-D-aspartate receptor complex with a novel synapse-associated protein, SAP102
    • Lau LF, Mammen A, Ehlers KD, Kindler S, Chung WJ, Garner CC, Huganir RL. Interaction of the N-methyl-D-aspartate receptor complex with a novel synapse-associated protein, SAP102. J Biol Chem. 271:1996;21622-21628.
    • (1996) J Biol Chem , vol.271 , pp. 21622-21628
    • Lau, L.F.1    Mammen, A.2    Ehlers, K.D.3    Kindler, S.4    Chung, W.J.5    Garner, C.C.6    Huganir, R.L.7
  • 31
    • 0030921919 scopus 로고    scopus 로고
    • Disulfide-linked head-to-head multimerization in the mechanism of ion channel clustering by PSD-95
    • Hsueh Y-P, Kim E, Sheng M. Disulfide-linked head-to-head multimerization in the mechanism of ion channel clustering by PSD-95. Neuron. 18:1997;803-814.
    • (1997) Neuron , vol.18 , pp. 803-814
    • Hsueh Y-P1    Kim, E.2    Sheng, M.3
  • 32
    • 0030900558 scopus 로고    scopus 로고
    • GRIP: A synaptic PDZ-domain-containing protein that interacts with AMPA receptors
    • Dong H, O'Brien RJ, Fung ET, Lanahan AA, Worley PF, Huganir RL. GRIP: a synaptic PDZ-domain-containing protein that interacts with AMPA receptors. Nature. 386:1997;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
  • 33
    • 0030200438 scopus 로고    scopus 로고
    • Heteromultimerization and NMDA receptor clustering activity of chapsyn-110, a members of the PSD-95 family of synaptic proteins
    • Kim E, Cho K-O, Rothschild AR, Sheng M. Heteromultimerization and NMDA receptor clustering activity of chapsyn-110, a members of the PSD-95 family of synaptic proteins. Neuron. 17:1996;103-113.
    • (1996) Neuron , vol.17 , pp. 103-113
    • Kim, E.1    Cho K-O2    Rothschild, A.R.3    Sheng, M.4
  • 35
    • 0030777701 scopus 로고    scopus 로고
    • Synaptic clustering of the cell adhesion molecule fasciclin II by Discs-Large and its role in the regulation of presynaptic structure
    • + channels and Fas II, and probably acts to co-cluster these molecules at the synapse. Moreover, loss of either DLG or Fas II results in an upregulation in presynaptic active zones, suggesting that both proteins work in a common pathway. The authors suggest that DLG plays a central role in the synapse: organizing pre- and postsynaptic structural specialization and the localization of CAMs and ion channels.
    • + channels and Fas II, and probably acts to co-cluster these molecules at the synapse. Moreover, loss of either DLG or Fas II results in an upregulation in presynaptic active zones, suggesting that both proteins work in a common pathway. The authors suggest that DLG plays a central role in the synapse: organizing pre- and postsynaptic structural specialization and the localization of CAMs and ion channels.
    • (1997) Neuron , vol.19 , pp. 787-799
    • Thomas, U.1    Kim, E.2    Kuhlendahl, S.3    Koh, Y.H.4    Gundelfinger, E.D.5    Sheng, M.6    Garner, C.C.7    Budnik, V.8
  • 36
    • 0029819449 scopus 로고    scopus 로고
    • The Dlg protein is required for junction structure, cell polarity and proliferation control in Drosophila epithelia
    • Woods DF, Hough C, Peel D, Callaini G, Bryant P. The Dlg protein is required for junction structure, cell polarity and proliferation control in Drosophila epithelia. J Cell Biol. 134:1996;1469-1482.
    • (1996) J Cell Biol , vol.134 , pp. 1469-1482
    • Woods, D.F.1    Hough, C.2    Peel, D.3    Callaini, G.4    Bryant, P.5
  • 37
    • 0028096801 scopus 로고
    • Cloning and characterization of hdlg: The human homologue of the Drosophila discs-large suppressor binds to protein 4.1
    • Lue RA, Marfatia SM, Branton D, Christhi AH. Cloning and characterization of hdlg: the human homologue of the Drosophila discs-large suppressor binds to protein 4.1. Proc Natl Acad Sci USA. 91:1994;9818-9822.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9818-9822
    • Lue, R.A.1    Marfatia, S.M.2    Branton, D.3    Christhi, A.H.4
  • 38
    • 0027959402 scopus 로고
    • Genetic analysis of fasciclin II in Drosophila: Defasciculation, refasciculation and altered fasciculation
    • Lin DM, Fetter RD, Kopczynski C, Grenningloh G, Goodman CS. Genetic analysis of fasciclin II in Drosophila: defasciculation, refasciculation and altered fasciculation. Neuron. 13:1994;1055-1069.
    • (1994) Neuron , vol.13 , pp. 1055-1069
    • Lin, D.M.1    Fetter, R.D.2    Kopczynski, C.3    Grenningloh, G.4    Goodman, C.S.5
  • 40
    • 0026095585 scopus 로고
    • Molecular cloning of an invertebrate glutamate receptor subunit expressed in Drosophila muscle
    • Schuster CM, Ultsch A, Schloss P, Cox JA, Schmidt B, Betz H. Molecular cloning of an invertebrate glutamate receptor subunit expressed in Drosophila muscle. Science. 254:1991;112-114.
    • (1991) Science , vol.254 , pp. 112-114
    • Schuster, C.M.1    Ultsch, A.2    Schloss, P.3    Cox, J.A.4    Schmidt, B.5    Betz, H.6
  • 41
    • 0029968898 scopus 로고    scopus 로고
    • Clustering of Gephyrin at GABAergic but not glutamategic synapses in cultured rate hippocampal neurons
    • Craig AM, Banker G, Chang W, McGrath ME, Serpinskaya AS. Clustering of Gephyrin at GABAergic but not glutamategic synapses in cultured rate hippocampal neurons. J Neurosci. 16:1996;3166-3177.
    • (1996) J Neurosci , vol.16 , pp. 3166-3177
    • Craig, A.M.1    Banker, G.2    Chang, W.3    McGrath, M.E.4    Serpinskaya, A.S.5
  • 42
    • 0029961905 scopus 로고    scopus 로고
    • Gephyrin accumulates at specific plasmalemma loci during neuronal maturation in vitro
    • Colin I, Rostaing P, Triller A. Gephyrin accumulates at specific plasmalemma loci during neuronal maturation in vitro. J Comp Neurol. 374:1996;467-479.
    • (1996) J Comp Neurol , vol.374 , pp. 467-479
    • Colin, I.1    Rostaing, P.2    Triller, A.3
  • 43
    • 0030273675 scopus 로고    scopus 로고
    • Presynaptic development at the Drosophila neuromuscular junction; Assembly and localization of presynaptic active zones
    • of special interest. Assembly of NMJ presynaptic active zones occurs independently of the target cell but synaptic localization of the active zones requires a muscle-derived mef2-dependent retrograde signal. Thus, the basic components of the pre- and postsynaptic machinery assemble independently of intercellular communication but localize properly only in response to mutually exchanged inducing signals.
    • Prokop A, Landgraf M, Rushton E, Broadie K, Bate M. Presynaptic development at the Drosophila neuromuscular junction; assembly and localization of presynaptic active zones. of special interest Neuron. 17:1996;617-626 Assembly of NMJ presynaptic active zones occurs independently of the target cell but synaptic localization of the active zones requires a muscle-derived mef2-dependent retrograde signal. Thus, the basic components of the pre- and postsynaptic machinery assemble independently of intercellular communication but localize properly only in response to mutually exchanged inducing signals.
    • (1996) Neuron , vol.17 , pp. 617-626
    • Prokop, A.1    Landgraf, M.2    Rushton, E.3    Broadie, K.4    Bate, M.5
  • 44
    • 0027497693 scopus 로고
    • Innervation receptor synthesis and localization in Drosophila embryo synaptogenesis
    • Broadie K, Bate M. Innervation receptor synthesis and localization in Drosophila embryo synaptogenesis. Nature. 361:1993;350-353.
    • (1993) Nature , vol.361 , pp. 350-353
    • Broadie, K.1    Bate, M.2
  • 45
    • 0027301138 scopus 로고
    • Ultrastructure of neuromuscular junctions in Drosophila - Comparison of wild-type and mutants with increased excitability
    • Jia X-X, Gorczyca M, Budnik VJ. Ultrastructure of neuromuscular junctions in Drosophila - comparison of wild-type and mutants with increased excitability. J Neurobiol. 24:1993;1025-1044.
    • (1993) J Neurobiol , vol.24 , pp. 1025-1044
    • Jia X-X1    Gorczyca, M.2    Budnik, V.J.3
  • 46
    • 0025513585 scopus 로고
    • Morphological plasticity of motoraxon terminals in Drosophila mutant with altered excitability
    • Budnik V, Zhong Y, Wu C-F. Morphological plasticity of motoraxon terminals in Drosophila mutant with altered excitability. J Neurosci. 10:1990;3754-3768.
    • (1990) J Neurosci , vol.10 , pp. 3754-3768
    • Budnik, V.1    Zhong, Y.2    Wu C-F3
  • 47
    • 0026544119 scopus 로고
    • Synaptic plasticitiy in Drosophila memory and hyperexcitability mutants: Role of cAMP cascade
    • Zhong Y, Budnik V, Wu C-F. Synaptic plasticitiy in Drosophila memory and hyperexcitability mutants: role of cAMP cascade. J Neurosci. 12:1992;644-651.
    • (1992) J Neurosci , vol.12 , pp. 644-651
    • Zhong, Y.1    Budnik, V.2    Wu C-F3
  • 48
    • 0030273550 scopus 로고    scopus 로고
    • Genetic dissection of structural and functional components of synaptic plasticitity. II. Fasciclin II controls presynaptic structural plasticity
    • Schuster CM, Davis GW, Fetter RD, Goodman CS. Genetic dissection of structural and functional components of synaptic plasticitity. II. Fasciclin II controls presynaptic structural plasticity. Neuron. 17:1996;655-667.
    • (1996) Neuron , vol.17 , pp. 655-667
    • Schuster, C.M.1    Davis, G.W.2    Fetter, R.D.3    Goodman, C.S.4
  • 49
    • 0030273772 scopus 로고    scopus 로고
    • Genetic dissection of structural and functional components of synaptic plasticity III. CREB is necessary for presynaptic functional plasticity
    • of outstanding interest. CREB work in parallel with Fas II to regulate presynaptic function downstream of cAMP regulation. Expression of a CREB repressor in dunce mutants (increased cAMP) blocks increased presynaptic function but structural overgrowth still occurs. Expression of a CREB activator increases synaptic strength but only in fas II mutants with extended presynaptic terminals. The authors suggest that neuronal activity levels regulate presynaptic cAMP levels, which, in turn, initiate parallel changes in Fas II (to control structural growth) and CREB (to control function through the regulation of presynaptic active zones).
    • Davis GW, Schuster CM, Goodman CS. Genetic dissection of structural and functional components of synaptic plasticity III. CREB is necessary for presynaptic functional plasticity. of outstanding interest Neuron. 17:1996;669-679 CREB work in parallel with Fas II to regulate presynaptic function downstream of cAMP regulation. Expression of a CREB repressor in dunce mutants (increased cAMP) blocks increased presynaptic function but structural overgrowth still occurs. Expression of a CREB activator increases synaptic strength but only in fas II mutants with extended presynaptic terminals. The authors suggest that neuronal activity levels regulate presynaptic cAMP levels, which, in turn, initiate parallel changes in Fas II (to control structural growth) and CREB (to control function through the regulation of presynaptic active zones).
    • (1996) Neuron , vol.17 , pp. 669-679
    • Davis, G.W.1    Schuster, C.M.2    Goodman, C.S.3
  • 50
    • 0030273379 scopus 로고    scopus 로고
    • Genetic dissection of structural and functional components of synaptic plasticity I. Fasciclin II controls synaptic stabilization and growth
    • of special interest. NMJ synaptogenesis proceeds normally in fas II null mutant embryos but the presynaptic terminal regresses postembryonically, suggesting that Fas II is required for synaptic stabilization. Use of the GAL4 technique to drive Fas II expression shows that the homophilic protein is required in both the pre- and postsynaptic cells.
    • Schuster CM, Davis GW, Fetter RD, Goodman CS. Genetic dissection of structural and functional components of synaptic plasticity I. Fasciclin II controls synaptic stabilization and growth. of special interest Neuron. 17:1996;641-654 NMJ synaptogenesis proceeds normally in fas II null mutant embryos but the presynaptic terminal regresses postembryonically, suggesting that Fas II is required for synaptic stabilization. Use of the GAL4 technique to drive Fas II expression shows that the homophilic protein is required in both the pre- and postsynaptic cells.
    • (1996) Neuron , vol.17 , pp. 641-654
    • Schuster, C.M.1    Davis, G.W.2    Fetter, R.D.3    Goodman, C.S.4
  • 51
    • 0029948786 scopus 로고    scopus 로고
    • Homeostasis of synaptic transmission in Drosophila with genetically altered nerve terminal morphology
    • of special interest. Hypomorphic fasII mutants show 50% fewer synaptic boutons but maintained synaptic transmission strength. The loss of presynaptic boutons is compensated for by an increased density of presynaptic active zones. These results show that Fas II regulates presynaptic structural differentiation independently of presynaptic function.
    • Stewart BA, Schuster CM, Goodman CS, Atwood HL. Homeostasis of synaptic transmission in Drosophila with genetically altered nerve terminal morphology. of special interest J Neurosci. 16:1996;3877-3886 Hypomorphic fasII mutants show 50% fewer synaptic boutons but maintained synaptic transmission strength. The loss of presynaptic boutons is compensated for by an increased density of presynaptic active zones. These results show that Fas II regulates presynaptic structural differentiation independently of presynaptic function.
    • (1996) J Neurosci , vol.16 , pp. 3877-3886
    • Stewart, B.A.1    Schuster, C.M.2    Goodman, C.S.3    Atwood, H.L.4
  • 52
    • 0028808056 scopus 로고
    • Altered nerve terminal arborization and synaptic transmission in Drosophila mutants of cell adhesion molecule fasciclin I
    • Zhong Y, Shanley J. Altered nerve terminal arborization and synaptic transmission in Drosophila mutants of cell adhesion molecule fasciclin I. J Neurosci. 15:1995;6679-6687.
    • (1995) J Neurosci , vol.15 , pp. 6679-6687
    • Zhong, Y.1    Shanley, J.2
  • 53
    • 0030294611 scopus 로고    scopus 로고
    • Olfactory learning deficits in mutants for leonardo, a Drosophila gene encoding a 14-3-3 protein
    • Skoulakis EMC, Davis RL. Olfactory learning deficits in mutants for leonardo, a Drosophila gene encoding a 14-3-3 protein. Neuron. 17:1996;931-944.
    • (1996) Neuron , vol.17 , pp. 931-944
    • Skoulakis, E.M.C.1    Davis, R.L.2
  • 54
    • 0030822692 scopus 로고    scopus 로고
    • Leonardo, a Drosophila 14-3-3 protein involved in learning, regulates presynaptic function
    • of outstanding interest. Leonardo, a Drosophila 14-3-3 protein, is expressed in the presynaptic terminal starting midway through synaptogenesis and regulates the maturation of synaptic modulation properties. In leonardo mutants, basal synaptic function is not strongly perturbed, but long-term facilitation, potentiation and fatigue-resistance properties are all lost. The authors suggest that Leonardo is required for the functional maturation of presynaptic active zones through the regulation of either the fusion machinery or synaptic vesicle dynamics
    • Broadie K, Rushton E, Skoulakis EMC, Davis RL. Leonardo, a Drosophila 14-3-3 protein involved in learning, regulates presynaptic function. of outstanding interest Neuron. 19:1997;391-402 Leonardo, a Drosophila 14-3-3 protein, is expressed in the presynaptic terminal starting midway through synaptogenesis and regulates the maturation of synaptic modulation properties. In leonardo mutants, basal synaptic function is not strongly perturbed, but long-term facilitation, potentiation and fatigue-resistance properties are all lost. The authors suggest that Leonardo is required for the functional maturation of presynaptic active zones through the regulation of either the fusion machinery or synaptic vesicle dynamics.
    • (1997) Neuron , vol.19 , pp. 391-402
    • Broadie, K.1    Rushton, E.2    Skoulakis, E.M.C.3    Davis, R.L.4
  • 55
    • 0028903288 scopus 로고
    • 14-3-3 proteins on the MAP
    • Aitken A. 14-3-3 proteins on the MAP. Trends Biochem Sci. 20:1995;95-97.
    • (1995) Trends Biochem Sci , vol.20 , pp. 95-97
    • Aitken, A.1
  • 58
    • 0028063607 scopus 로고
    • Subcellular localisation of 14-3-3 isoforms in rat brain using specific antibodies
    • Martin H, Rostas J, Patel Y, Aitken A. Subcellular localisation of 14-3-3 isoforms in rat brain using specific antibodies. J Neurochem. 63:1994;2253-2265.
    • (1994) J Neurochem , vol.63 , pp. 2253-2265
    • Martin, H.1    Rostas, J.2    Patel, Y.3    Aitken, A.4
  • 59
    • 0028841609 scopus 로고
    • Stimulation of catecholamine secretion from adrenal chromaffin cells by 14-3-3 proteins is due to reorganization of the cortical actin network
    • Roth D, Burgoyne RD. Stimulation of catecholamine secretion from adrenal chromaffin cells by 14-3-3 proteins is due to reorganization of the cortical actin network. FEBS Lett. 374:1995;77-81.
    • (1995) FEBS Lett , vol.374 , pp. 77-81
    • Roth, D.1    Burgoyne, R.D.2
  • 60
    • 0029558545 scopus 로고
    • Synapsin I deficiency results in structural changes in the presynaptic terminals in the murine nervous system
    • Takei Y, Harada A, Takeda S, Kobayashi K, Terada S, Noda T, Takahashi T, Hirokawa N. Synapsin I deficiency results in structural changes in the presynaptic terminals in the murine nervous system. J Cell Biol. 131:1995;1789-1800.
    • (1995) J Cell Biol , vol.131 , pp. 1789-1800
    • Takei, Y.1    Harada, A.2    Takeda, S.3    Kobayashi, K.4    Terada, S.5    Noda, T.6    Takahashi, T.7    Hirokawa, N.8
  • 61
    • 0030271819 scopus 로고    scopus 로고
    • Expression of synapsin I correlates with maturation of the neuromuscular synapse
    • Lu B, Czernik AJ, Popov S, Wang T, Poo M-m, Greengard P. Expression of synapsin I correlates with maturation of the neuromuscular synapse. Neuroscience. 74:1996;1087-1097.
    • (1996) Neuroscience , vol.74 , pp. 1087-1097
    • Lu, B.1    Czernik, A.J.2    Popov, S.3    Wang, T.4    Poo M-M5    Greengard, P.6
  • 62
    • 0030770840 scopus 로고    scopus 로고
    • Binding of neuroligins to PSD-95
    • + channels and the neurologin CAM on its PDZ 1-3 domains, respectively. As neuroligin binds the presynaptic β-neurexin protein, which interacts through its cytosolic domain with the MAGUK CASK, the authors propose that this interaction is a likely mechanism for the coordinate localization of organizing MAGUKs in the pre- and postsynaptic cells. This work is particularly exciting because it proposes a mechanism whereby an unspecialized intercellular junction can be converted into an operational synapses, first through the recruitment of specific pre- and postsynaptic MAGUKs and, subsequently, through the action of these MAGUKs to co-localize receptors, ion channels and CAMs into functional signal-transducing machinery.
    • + channels and the neurologin CAM on its PDZ 1-3 domains, respectively. As neuroligin binds the presynaptic β-neurexin protein, which interacts through its cytosolic domain with the MAGUK CASK, the authors propose that this interaction is a likely mechanism for the coordinate localization of organizing MAGUKs in the pre- and postsynaptic cells. This work is particularly exciting because it proposes a mechanism whereby an unspecialized intercellular junction can be converted into an operational synapses, first through the recruitment of specific pre- and postsynaptic MAGUKs and, subsequently, through the action of these MAGUKs to co-localize receptors, ion channels and CAMs into functional signal-transducing machinery.
    • (1997) Science , vol.277 , pp. 1511-1515
    • Irie, M.1    Hata, Y.2    Takeuchi, M.3    Toyoda, A.4    Hirao, K.5    Takai, Y.6    Rosahl, T.W.7    Sudhof, T.C.8
  • 63
    • 0030612949 scopus 로고    scopus 로고
    • Synaptic clustering of fasciclin II and Shaker: Essential targeting sequences and role of Dlg
    • Zito K, Fetter RD, Goodman CS, Isacoff EY. Synaptic clustering of fasciclin II and Shaker: essential targeting sequences and role of Dlg. Neuron. 19:1997;1007-1016.
    • (1997) Neuron , vol.19 , pp. 1007-1016
    • Zito, K.1    Fetter, R.D.2    Goodman, C.S.3    Isacoff, E.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.