메뉴 건너뛰기




Volumn 9, Issue 7, 2014, Pages

α-Actinin-2 mediates spine morphology and assembly of the post-synaptic density in hippocampal neurons

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA ACTININ 2; ALPHA ACTININ 4; CALCIUM ION; GLUTAMATE RECEPTOR; GLUTAMIC ACID; N METHYL DEXTRO ASPARTIC ACID; PHENYLALANINE; ACTININ; ACTN2 PROTEIN, RAT;

EID: 84904052300     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0101770     Document Type: Article
Times cited : (39)

References (61)
  • 1
    • 42349091996 scopus 로고    scopus 로고
    • Actin in action: The interplay between the actin cytoskeleton and synaptic efficacy
    • DOI 10.1038/nrn2373, PII NRN2373
    • Cingolani LA, Goda Y (2008) Actin in action: the interplay between the actin cytoskeleton and synaptic efficacy. Nat Rev Neurosci 9: 344-356. doi:10.1038/nrn2373 (Pubitemid 351556045)
    • (2008) Nature Reviews Neuroscience , vol.9 , Issue.5 , pp. 344-356
    • Cingolani, L.A.1    Goda, Y.2
  • 2
    • 0036082812 scopus 로고    scopus 로고
    • Dendritic spine pathology: Cause or consequence of neurological disorders?
    • DOI 10.1016/S0165-0173(02)00158-3, PII S0165017302001583
    • Fiala JC, Spacek J, Harris KM (2002) Dendritic spine pathology: cause or consequence of neurological disorders? Brain Res Brain Res Rev 39: 29-54. (Pubitemid 34666985)
    • (2002) Brain Research Reviews , vol.39 , Issue.1 , pp. 29-54
    • Fiala, J.C.1    Spacek, J.2    Harris, K.M.3
  • 3
    • 77952334420 scopus 로고    scopus 로고
    • Actin in dendritic spines: Connecting dynamics to function
    • doi:10.1083/jcb.201003008
    • Hotulainen P, Hoogenraad CC (2010) Actin in dendritic spines: connecting dynamics to function. J Cell Biol 189: 619-629. doi:10.1083/jcb.201003008
    • (2010) J Cell Biol , vol.189 , pp. 619-629
    • Hotulainen, P.1    Hoogenraad, C.C.2
  • 4
    • 0033797735 scopus 로고    scopus 로고
    • Dendritic anomalies in disorders associated with mental retardation
    • Kaufmann WE, Moser HW (2000) Dendritic anomalies in disorders associated with mental retardation. Cereb Cortex 10: 981-991.
    • (2000) Cereb Cortex , vol.10 , pp. 981-991
    • Kaufmann, W.E.1    Moser, H.W.2
  • 7
    • 2442481067 scopus 로고    scopus 로고
    • α-actinin revisited: A fresh look at an old player
    • DOI 10.1002/cm.20007
    • Otey CA, Carpen O (2004) Alpha-actinin revisited: a fresh look at an old player. Cell Motil Cytoskeleton 58: 104-111. doi:10.1002/cm.20007 (Pubitemid 38697587)
    • (2004) Cell Motility and the Cytoskeleton , vol.58 , Issue.2 , pp. 104-111
    • Otey, C.A.1    Carpen, O.2
  • 8
    • 5344278258 scopus 로고    scopus 로고
    • The dynamic turnover and functional roles of α-actinin in dendritic spines
    • DOI 10.1016/j.neuropharm.2004.07.022, PII S002839080400214X, The Cytoskeleton and Synaptic Function
    • Nakagawa T, Engler JA, Sheng M (2004) The dynamic turnover and functional roles of alpha-actinin in dendritic spines. Neuropharmacology 47: 734-745. doi:10.1016/j.neuropharm.2004.07.022. (Pubitemid 39348955)
    • (2004) Neuropharmacology , vol.47 , Issue.5 , pp. 734-745
    • Nakagawa, T.1    Engler, J.A.2    Sheng, M.3
  • 9
    • 0033588277 scopus 로고    scopus 로고
    • Structure of the α-actinin rod: Molecular basis for cross-linking of actin filaments
    • DOI 10.1016/S0092-8674(00)81981-9
    • Djinović-Carugo K, Young P, Gautel M, Saraste M (1999) Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments. Cell 98: 537-546. (Pubitemid 29402490)
    • (1999) Cell , vol.98 , Issue.4 , pp. 537-546
    • Djinovic-Carugo, K.1    Young, P.2    Gautel, M.3    Saraste, M.4
  • 10
    • 17444415361 scopus 로고    scopus 로고
    • Spectrin, alpha-actinin, and dystrophin
    • doi:10.1016/S0065-3233(05)70007-3
    • Broderick MJF, Winder SJ (2005) Spectrin, alpha-actinin, and dystrophin. Adv Protein Chem 70: 203-246. doi:10.1016/S0065-3233(05)70007-3
    • (2005) Adv Protein Chem , vol.70 , pp. 203-246
    • Broderick, M.J.F.1    Winder, S.J.2
  • 11
    • 0037225490 scopus 로고    scopus 로고
    • The α-actinin gene family: A revised classification
    • DOI 10.1007/s00239-002-2374-5
    • Dixson JD, Forstner MJ, Garcia DM (2003) The alpha-actinin gene family: a revised classification. J Mol Evol 56: 1-10. doi:10.1007/s00239-002-2374-5 (Pubitemid 36078610)
    • (2003) Journal of Molecular Evolution , vol.56 , Issue.1 , pp. 1-10
    • Dixson, J.D.1    Forstner, M.R.J.2    Garcia, D.M.3
  • 12
    • 51349091855 scopus 로고    scopus 로고
    • α-Actinin structure and regulation
    • doi:10.1007/s00018-008-8080-8
    • Sjöblom B, Salmazo A, Djinović-Carugo K (2008) α-Actinin structure and regulation. Cell Mol Life Sci 65: 2688-2701. doi:10.1007/s00018-008-8080-8
    • (2008) Cell Mol Life Sci , vol.65 , pp. 2688-2701
    • Sjöblom, B.1    Salmazo, A.2    Djinović-Carugo, K.3
  • 13
    • 2442683994 scopus 로고    scopus 로고
    • Semiquantitative proteomic analysis of rat forebrain postsynaptic density fractions by mass spectrometry
    • DOI 10.1074/jbc.M400103200
    • Peng J, Kim MJ, Cheng D, Duong DM, Gygi SP, et al. (2004) Semiquantitative proteomic analysis of rat forebrain postsynaptic density fractions by mass spectrometry. J Biol Chem 279: 21003-21011. doi:10.1074/jbc.M400103200 (Pubitemid 38656501)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.20 , pp. 21003-21011
    • Peng, J.1    Kim, M.J.2    Cheng, D.3    Duong, D.M.4    Gygi, S.P.5    Sheng, M.6
  • 15
    • 59149099842 scopus 로고    scopus 로고
    • The cytoskeletal protein alpha-actinin regulates acid-sensing ion channel 1a through a C-terminal interaction
    • doi:10.1074/jbc.M805110200
    • Schnizler MK, Schnizler K, Zha X-M, Hall DD, Wemmie JA, et al. (2009) The cytoskeletal protein alpha-actinin regulates acid-sensing ion channel 1a through a C-terminal interaction. J Biol Chem 284: 2697-2705. doi:10.1074/jbc.M805110200
    • (2009) J Biol Chem , vol.284 , pp. 2697-2705
    • Schnizler, M.K.1    Schnizler, K.2    Zha, X.-M.3    Hall, D.D.4    Wemmie, J.A.5
  • 16
    • 0031013896 scopus 로고    scopus 로고
    • Competitive binding of α-actinin and calmodulin to the NMDA receptor
    • DOI 10.1038/385439a0
    • Wyszynski M, Lin J, Rao A, Nigh E, Beggs AH, et al. (1997) Competitive binding of alpha-actinin and calmodulin to the NMDA receptor. Nature 385: 439-442. doi:10.1038/385439a0 (Pubitemid 27065929)
    • (1997) Nature , vol.385 , Issue.6615 , pp. 439-442
    • Wyszynski, M.1    Lin, J.2    Rao, A.3    Nigh, E.4    Beggs, A.H.5    Craig, A.M.6    Sheng, M.7
  • 17
    • 0032519871 scopus 로고    scopus 로고
    • Differential regional expression and ultrastructural localization of α- actinin-2, a putative NMDA receptor-anchoring protein, in rat brain
    • Wyszynski M, Kharazia V, Shanghvi R, Rao A, Beggs AH, et al. (1998) Differential regional expression and ultrastructural localization of alpha-actinin-2, a putative NMDA receptor-anchoring protein, in rat brain. J Neurosci 18: 1383-1392. (Pubitemid 28082423)
    • (1998) Journal of Neuroscience , vol.18 , Issue.4 , pp. 1383-1392
    • Wyszynski, M.1    Kharazia, V.2    Shanghvi, R.3    Rao, A.4    Beggs, A.H.5    Craig, A.M.6    Weinberg, R.7    Sheng, M.8
  • 18
    • 0034705447 scopus 로고    scopus 로고
    • α-Actinin-2 in rat striatum: Localization and interaction with NMDA glutamate receptor subunits
    • DOI 10.1016/S0169-328X(00)00102-9, PII S0169328X00001029
    • Dunah AW, Wyszynski M, Martin DM, Sheng M, Standaert DG (2000) alpha-actinin-2 in rat striatum: localization and interaction with NMDA glutamate receptor subunits. Brain Res Mol Brain Res 79: 77-87. (Pubitemid 30495531)
    • (2000) Molecular Brain Research , vol.79 , Issue.1-2 , pp. 77-87
    • Dunah, A.W.1    Wyszynski, M.2    Martin, D.M.3    Sheng, M.4    Standaert, D.G.5
  • 19
    • 0034659732 scopus 로고    scopus 로고
    • Postsynaptic scaffolds of excitatory and inhibitory synapses in hippocampal neurons: Maintenance of core components independent of actin filaments and microtubules
    • Allison DW, Chervin AS, Gelfand VI, Craig AM (2000) Postsynaptic scaffolds of excitatory and inhibitory synapses in hippocampal neurons: maintenance of core components independent of actin filaments and microtubules. J Neurosci 20: 4545-4554. (Pubitemid 30396620)
    • (2000) Journal of Neuroscience , vol.20 , Issue.12 , pp. 4545-4554
    • Allison, D.W.1    Chervin, A.S.2    Gelfand, V.I.3    Craig, A.M.4
  • 20
    • 0028979956 scopus 로고
    • Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin
    • Knudsen KA, Soler AP, Johnson KR, Wheelock MJ (1995) Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin. J Cell Biol 130: 67-77.
    • (1995) J Cell Biol , vol.130 , pp. 67-77
    • Knudsen, K.A.1    Soler, A.P.2    Johnson, K.R.3    Wheelock, M.J.4
  • 21
    • 0025291522 scopus 로고
    • An interaction between alpha-actinin and the beta 1 integrin subunit in vitro
    • Otey CA, Pavalko FM, Burridge K (1990) An interaction between alpha-actinin and the beta 1 integrin subunit in vitro. J Cell Biol 111: 721-729.
    • (1990) J Cell Biol , vol.111 , pp. 721-729
    • Otey, C.A.1    Pavalko, F.M.2    Burridge, K.3
  • 22
    • 84877359523 scopus 로고    scopus 로고
    • Competition between α-actinin and Ca(2+)-Calmodulin Controls Surface Retention of the L-type Ca(2+) Channel CaV1.2
    • doi:10.1016/j.neuron.2013.02.032
    • HallDD, Dai S, Tseng P-Y, Malik Z, NguyenM, et al. (2013) Competition between α-actinin and Ca(2+)-Calmodulin Controls Surface Retention of the L-type Ca(2+) Channel CaV1.2. Neuron 78: 483-497. doi:10.1016/j.neuron.2013.02. 032
    • (2013) Neuron , vol.78 , pp. 483-497
    • Hall, D.D.1    Dai, S.2    Tseng, P.-Y.3    Malik, Z.4    Nguyen, M.5
  • 23
    • 27444434998 scopus 로고    scopus 로고
    • Multivalent interactions of calcium/calmodulin-dependent protein kinase II with the postsynaptic density proteins NR2B, densin-180, and α-actinin-2
    • DOI 10.1074/jbc.M502191200
    • Robison AJ, Bass MA, Jiao Y, MacMillan LB, Carmody LC, et al. (2005) Multivalent interactions of calcium/calmodulin-dependent protein kinase II with the postsynaptic density proteins NR2B, densin-180, and alpha-actinin-2. J Biol Chem 280: 35329-35336. doi:10.1074/jbc.M502191200 (Pubitemid 41532721)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.42 , pp. 35329-35336
    • Robison, A.J.1    Bass, M.A.2    Jiao, Y.3    MacMillan, L.B.4    Carmody, L.C.5    Bartlett, R.K.6    Colbran, R.J.7
  • 24
    • 84860842301 scopus 로고    scopus 로고
    • Substrate-selective and calcium-independent activation of CaMKII by α-actinin
    • doi:10.1074/jbc.M112.351817
    • Jalan-Sakrikar N, Bartlett RK, Baucum AJ, Colbran RJ (2012) Substrate-selective and calcium-independent activation of CaMKII by α-actinin. J Biol Chem 287: 15275-15283. doi:10.1074/jbc.M112.351817
    • (2012) J Biol Chem , vol.287 , pp. 15275-15283
    • Jalan-Sakrikar, N.1    Bartlett, R.K.2    Baucum, A.J.3    Colbran, R.J.4
  • 25
    • 34249050764 scopus 로고    scopus 로고
    • Phosphatidylinositol-4,5-bisphosphate regulates NMDA receptor activity through α-actinin
    • DOI 10.1523/JNEUROSCI.4378-06.2007
    • Michailidis IE, Helton TD, Petrou VI, Mirshahi T, Ehlers MD, et al. (2007) Phosphatidylinositol-4,5-bisphosphate regulates NMDA receptor activity through alpha-actinin. Journal of Neuroscience 27: 5523-5532. doi:10.1523/JNEUROSCI.4378-06.2007 (Pubitemid 46790162)
    • (2007) Journal of Neuroscience , vol.27 , Issue.20 , pp. 5523-5532
    • Michailidis, I.E.1    Helton, T.D.2    Petrou, V.I.3    Mirshahi, T.4    Ehlers, M.D.5    Logothetis, D.E.6
  • 26
    • 0037134020 scopus 로고    scopus 로고
    • A system for stable expression of short interfering RNAs in mammalian cells
    • DOI 10.1126/science.1068999
    • Brummelkamp TR, Bernards R, Agami R (2002) A system for stable expression of short interfering RNAs in mammalian cells. Science 296: 550-553. doi:10.1126/science.1068999 (Pubitemid 34408678)
    • (2002) Science , vol.296 , Issue.5567 , pp. 550-553
    • Brummelkamp, T.R.1    Bernards, R.2    Agami, R.3
  • 27
    • 65549085129 scopus 로고    scopus 로고
    • Combinatorial morphogenesis of dendritic spines and filopodia by SPAR and alpha-actinin2
    • doi:10.1016/j.bbrc.2009.04.069
    • Hoe H-S, Lee J-Y, Pak DTS (2009) Combinatorial morphogenesis of dendritic spines and filopodia by SPAR and alpha-actinin2. Biochem Biophys Res Commun 384: 55-60. doi:10.1016/j.bbrc.2009.04.069
    • (2009) Biochem Biophys Res Commun , vol.384 , pp. 55-60
    • Hoe, H.-S.1    Lee, J.-Y.2    Pak, D.T.S.3
  • 29
    • 33644560354 scopus 로고    scopus 로고
    • Glutamate receptor exocytosis and spine enlargement during chemically induced long-term potentiation
    • doi:10.1523/JNEUROSCI.3918-05.2006
    • Kopec CD, Li B,Wei W, Boehm J,Malinow R (2006) Glutamate receptor exocytosis and spine enlargement during chemically induced long-term potentiation. Journal of Neuroscience 26: 2000-2009. doi:10.1523/JNEUROSCI.3918- 05.2006
    • (2006) Journal of Neuroscience , vol.26 , pp. 2000-2009
    • Kopec, C.D.1    Li, B.2    Wei, W.3    Boehm, J.4    Malinow, R.5
  • 30
    • 4644287672 scopus 로고    scopus 로고
    • Recycling endosomes supply AMPA receptors for LTP
    • DOI 10.1126/science.1102026
    • ParkM, Penick EC, Edwards JG, Kauer JA, EhlersMD (2004) Recycling endosomes supply AMPA receptors for LTP. Science 305: 1972-1975. doi:10.1126/science.1102026 (Pubitemid 39287999)
    • (2004) Science , vol.305 , Issue.5692 , pp. 1972-1975
    • Park, M.1    Penick, E.C.2    Edwards, J.G.3    Kauer, J.A.4    Ehlers, M.D.5
  • 31
    • 0035132869 scopus 로고    scopus 로고
    • Activation of synaptic NMDA receptors induces membrane insertion of new AMPA receptors and LTP in cultured hippocampal neurons
    • DOI 10.1016/S0896-6273(01)00194-5
    • Lu W, Man H, Ju W, Trimble WS, MacDonald JF, et al. (2001) Activation of synaptic NMDA receptors induces membrane insertion of new AMPA receptors and LTP in cultured hippocampal neurons. Neuron 29: 243-254. (Pubitemid 32108736)
    • (2001) Neuron , vol.29 , Issue.1 , pp. 243-254
    • Lu, W.-Y.1    Man, H.-Y.2    Ju, W.3    Trimble, W.S.4    MacDonald, J.F.5    Wang, Y.T.6
  • 32
    • 5344265106 scopus 로고    scopus 로고
    • Influx of extracellular calcium regulates actin-dependent morphological plasticity in dendritic spines
    • DOI 10.1016/j.neuropharm.2004.07.038, PII S0028390804002254, The Cytoskeleton and Synaptic Function
    • Brünig I, Kaech S, Brinkhaus H, Oertner TG, Matus A (2004) Influx of extracellular calcium regulates actin-dependent morphological plasticity in dendritic spines. Neuropharmacology 47: 669-676. doi:10.1016/j.neuropharm.2004. 07.038 (Pubitemid 39348948)
    • (2004) Neuropharmacology , vol.47 , Issue.5 , pp. 669-676
    • Brunig, I.1    Kaech, S.2    Brinkhaus, H.3    Oertner, T.G.4    Matus, A.5
  • 33
    • 7044267351 scopus 로고    scopus 로고
    • Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity
    • DOI 10.1038/nn1311
    • Okamoto K-I, Nagai T, Miyawaki A, Hayashi Y (2004) Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity. Nat Neurosci 7: 1104-1112. doi:10.1038/nn1311 (Pubitemid 41184451)
    • (2004) Nature Neuroscience , vol.7 , Issue.10 , pp. 1104-1112
    • Okamoto, K.-I.1    Nagai, T.2    Miyawaki, A.3    Hayashi, Y.4
  • 34
    • 33847119026 scopus 로고    scopus 로고
    • Cell adhesion molecules: Signalling functions at the synapse
    • DOI 10.1038/nrn2075, PII NRN2075
    • Dalva MB, McClelland AC, Kayser MS (2007) Cell adhesion molecules: signalling functions at the synapse. Nat Rev Neurosci 8: 206-220. doi:10.1038/nrn2075 (Pubitemid 46294663)
    • (2007) Nature Reviews Neuroscience , vol.8 , Issue.3 , pp. 206-220
    • Dalva, M.B.1    McClelland, A.C.2    Kayser, M.S.3
  • 36
    • 0034721678 scopus 로고    scopus 로고
    • Signal-processing machines at the postsynaptic density
    • Kennedy MB (2000) Signal-processing machines at the postsynaptic density. Science 290: 750-754.
    • (2000) Science , vol.290 , pp. 750-754
    • Kennedy, M.B.1
  • 38
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Kornau HC, Schenker LT, Kennedy MB, Seeburg PH (1995) Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science 269: 1737-1740.
    • (1995) Science , vol.269 , pp. 1737-1740
    • Kornau, H.C.1    Schenker, L.T.2    Kennedy, M.B.3    Seeburg, P.H.4
  • 40
    • 0032473998 scopus 로고    scopus 로고
    • Synaptic vesicles retain their identity through the endocytic cycle
    • DOI 10.1038/33152
    • Murthy VN, Stevens CF (1998) Synaptic vesicles retain their identity through the endocytic cycle. Nature 392: 497-501. doi:10.1038/33152 (Pubitemid 28168981)
    • (1998) Nature , vol.392 , Issue.6675 , pp. 497-501
    • Murthy, V.N.1    Stevens, C.F.2
  • 41
    • 84872084802 scopus 로고    scopus 로고
    • The tension mounts: Stress fibers as force-generating mechanotransducers
    • doi:10.1083/jcb.201210090
    • Burridge K, Wittchen ES (2013) The tension mounts: Stress fibers as force-generating mechanotransducers. J Cell Biol 200: 9-19. doi:10.1083/jcb. 201210090
    • (2013) J Cell Biol , vol.200 , pp. 9-19
    • Burridge, K.1    Wittchen, E.S.2
  • 42
    • 0036498546 scopus 로고    scopus 로고
    • The lamellipodium: Where motility begins
    • DOI 10.1016/S0962-8924(01)02237-1, PII S0962892401022371
    • Small JV, Stradal T, Vignal E, Rottner K (2002) The lamellipodium: where motility begins. Trends Cell Biol 12: 112-120. (Pubitemid 34164650)
    • (2002) Trends in Cell Biology , vol.12 , Issue.3 , pp. 112-120
    • Small J.Victor1    Stradal, T.2    Vignal, E.3    Rottner, K.4
  • 43
    • 51049104617 scopus 로고    scopus 로고
    • Actin and alpha-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner
    • Choi CK, Vicente-Manzanares M, Zareno J, Whitmore LA, Mogilner A, et al. (2008) Actin and alpha-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner. Nat Cell Biol 10: 1039-1050.
    • (2008) Nat Cell Biol , vol.10 , pp. 1039-1050
    • Choi, C.K.1    Vicente-Manzanares, M.2    Zareno, J.3    Whitmore, L.A.4    Mogilner, A.5
  • 45
    • 34547488455 scopus 로고    scopus 로고
    • Role of actin cytoskeleton in dendritic spine morphogenesis
    • DOI 10.1016/j.neuint.2007.04.029, PII S0197018607001209
    • Sekino Y, Kojima N, Shirao T (2007) Role of actin cytoskeleton in dendritic spine morphogenesis. Neurochem Int 51: 92-104. doi:10.1016/j.neuint. 2007.04.029 (Pubitemid 47176704)
    • (2007) Neurochemistry International , vol.51 , Issue.2-4 SPEC. ISS. , pp. 92-104
    • Sekino, Y.1    Kojima, N.2    Shirao, T.3
  • 46
    • 69249100460 scopus 로고    scopus 로고
    • Experience-dependent structural synaptic plasticity in the mammalian brain
    • doi:10.1038/nrn2699
    • Holtmaat A, Svoboda K (2009) Experience-dependent structural synaptic plasticity in the mammalian brain. Nat Rev Neurosci 10: 647-658. doi:10.1038/nrn2699
    • (2009) Nat Rev Neurosci , vol.10 , pp. 647-658
    • Holtmaat, A.1    Svoboda, K.2
  • 47
    • 33751036726 scopus 로고    scopus 로고
    • Rapid redistribution of synaptic PSD-95 in the neocortex in vivo
    • doi:10.1371/journal.pbio.0040370
    • Gray NW, Weimer RM, Bureau I, Svoboda K (2006) Rapid redistribution of synaptic PSD-95 in the neocortex in vivo. PLoS Biol 4: e370. doi:10.1371/journal.pbio.0040370
    • (2006) PLoS Biol , vol.4
    • Gray, N.W.1    Weimer, R.M.2    Bureau, I.3    Svoboda, K.4
  • 48
    • 0037155199 scopus 로고    scopus 로고
    • PDZ domains: Structural modules for protein complex assembly
    • DOI 10.1074/jbc.R100065200
    • Hung AY, Sheng M (2002) PDZ domains: structural modules for protein complex assembly. J Biol Chem 277: 5699-5702. doi:10.1074/jbc.R100065200 (Pubitemid 34968344)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.8 , pp. 5699-5702
    • Hung, A.Y.1    Sheng, M.2
  • 49
    • 84859730415 scopus 로고    scopus 로고
    • Building and remodeling synapses
    • doi:10.1002/hipo.20872
    • Benson DL, Huntley GW (2012) Building and remodeling synapses. Hippocampus 22: 954-968. doi:10.1002/hipo.20872
    • (2012) Hippocampus , vol.22 , pp. 954-968
    • Benson, D.L.1    Huntley, G.W.2
  • 50
    • 70349883839 scopus 로고    scopus 로고
    • Rapid assembly of functional presynaptic boutons triggered by adhesive contacts
    • doi:10.1523/JNEUROSCI.1381-09.2009
    • Lucido AL, Suarez Sanchez F, Thostrup P, Kwiatkowski AV, Leal-Ortiz S, et al. (2009) Rapid assembly of functional presynaptic boutons triggered by adhesive contacts. J Neurosci 29: 12449-12466. doi:10.1523/JNEUROSCI.1381-09. 2009
    • (2009) J Neurosci , vol.29 , pp. 12449-12466
    • Lucido, A.L.1    Suarez Sanchez, F.2    Thostrup, P.3    Kwiatkowski, A.V.4    Leal-Ortiz, S.5
  • 51
    • 0033562792 scopus 로고    scopus 로고
    • Change in the shape of dendritic spines caused by overexpression of drebrin in cultured cortical neurons
    • Hayashi K, Shirao T (1999) Change in the shape of dendritic spines caused by overexpression of drebrin in cultured cortical neurons. Journal of Neuroscience 19: 3918-3925. (Pubitemid 29222266)
    • (1999) Journal of Neuroscience , vol.19 , Issue.10 , pp. 3918-3925
    • Hayashi, K.1    Shirao, T.2
  • 52
    • 80052063518 scopus 로고    scopus 로고
    • Myosin IIb activity and phosphorylation status determines dendritic spine and post-synaptic density morphology
    • doi:10.1371/journal.pone.0024149
    • Hodges JL, Newell-Litwa K, Asmussen H, Vicente-Manzanares M, Horwitz AR (2011) Myosin IIb activity and phosphorylation status determines dendritic spine and post-synaptic density morphology. PLoS ONE 6: e24149. doi:10.1371/journal. pone.0024149
    • (2011) PLoS ONE , vol.6
    • Hodges, J.L.1    Newell-Litwa, K.2    Asmussen, H.3    Vicente-Manzanares, M.4    Horwitz, A.R.5
  • 54
    • 0019843141 scopus 로고
    • Non-muscle α-actinins are calcium-sensitive actin-binding proteins
    • Burridge K, Feramisco JR (1981) Non-muscle alpha actinins are calcium-sensitive actin-binding proteins. Nature 294: 565-567. (Pubitemid 12164579)
    • (1981) Nature , vol.294 , Issue.5841 , pp. 565-567
    • Burridge, K.1    Feramisco, J.R.2
  • 55
    • 84856716925 scopus 로고    scopus 로고
    • α-Actinin-4/FSGS1 is required for Arp2/3-dependent actin assembly at the adherens junction
    • doi:10.1083/jcb.201103116
    • Tang VW, Brieher WM (2012) α-Actinin-4/FSGS1 is required for Arp2/3-dependent actin assembly at the adherens junction. J Cell Biol 196: 115-130. doi:10.1083/jcb.201103116
    • (2012) J Cell Biol , vol.196 , pp. 115-130
    • Tang, V.W.1    Brieher, W.M.2
  • 56
    • 0035954424 scopus 로고    scopus 로고
    • Differential dynamics of α5 integrin, paxillin, and α-actinin during formation and disassembly of adhesions in migrating cells
    • DOI 10.1083/jcb.153.7.1427
    • Laukaitis CM, Webb DJ, Donais K, Horwitz AF (2001) Differential dynamics of alpha 5 integrin, paxillin, and alpha-actinin during formation and disassembly of adhesions in migrating cells. J Cell Biol 153: 1427-1440. (Pubitemid 34286127)
    • (2001) Journal of Cell Biology , vol.153 , Issue.7 , pp. 1427-1440
    • Laukaitis, C.M.1    Webb, D.J.2    Donais, K.3    Horwitz, A.F.4
  • 57
    • 0037437147 scopus 로고    scopus 로고
    • Synapse formation is regulated by the signaling adaptor GIT1
    • DOI 10.1083/jcb.200211002
    • Zhang H, Webb DJ, Asmussen H, Horwitz AF (2003) Synapse formation is regulated by the signaling adaptor GIT1. J Cell Biol 161: 131-142. doi:10.1083/jcb.200211002 (Pubitemid 36459086)
    • (2003) Journal of Cell Biology , vol.161 , Issue.1 , pp. 131-142
    • Zhang, H.1    Webb, D.J.2    Asmussen, H.3    Horwitz, A.F.4
  • 58
    • 0035882289 scopus 로고    scopus 로고
    • Activation of silent synapses by rapid activity-dependent synaptic recruitment of AMPA receptors
    • Liao D, Scannevin RH, Huganir R (2001) Activation of silent synapses by rapid activity-dependent synaptic recruitment of AMPA receptors. Journal of Neuroscience 21: 6008-6017. (Pubitemid 32737734)
    • (2001) Journal of Neuroscience , vol.21 , Issue.16 , pp. 6008-6017
    • Liao, D.1    Scannevin, R.H.2    Huganir, R.3
  • 59
    • 1542722198 scopus 로고    scopus 로고
    • Temporal dynamics of NMDA receptor-induced changes in spine morphology and AMPA receptor recruitment to spines
    • DOI 10.1016/j.bbrc.2004.02.086, PII S0006291X04003353
    • Lin H, Huganir R, Liao D (2004) Temporal dynamics of NMDA receptor-induced changes in spine morphology and AMPA receptor recruitment to spines. Biochem Biophys Res Commun 316: 501-511. doi:10.1016/j.bbrc.2004.02.086 (Pubitemid 38338619)
    • (2004) Biochemical and Biophysical Research Communications , vol.316 , Issue.2 , pp. 501-511
    • Lin, H.1    Huganir, R.2    Liao, D.3
  • 60
    • 79960837954 scopus 로고    scopus 로고
    • Neuronal activity drives matching of pre- and postsynaptic function during synapse maturation
    • doi:10.1038/nn.2826
    • Kay L, Humphreys L, Eickholt BJ, Burrone J (2011) Neuronal activity drives matching of pre- and postsynaptic function during synapse maturation. Nat Neurosci 14: 688-690. doi:10.1038/nn.2826
    • (2011) Nat Neurosci , vol.14 , pp. 688-690
    • Kay, L.1    Humphreys, L.2    Eickholt, B.J.3    Burrone, J.4
  • 61
    • 0346024190 scopus 로고    scopus 로고
    • Genesis of dendritic spines: Insights from ultrastructural and imaging studies
    • Yuste R, Bonhoeffer T (2004) Genesis of dendritic spines: insights from ultrastructural and imaging studies. Nat Rev Neurosci 5: 24-34. doi:10.1038/nrn1300 (Pubitemid 38076181)
    • (2004) Nature Reviews Neuroscience , vol.5 , Issue.1 , pp. 24-34
    • Yuste, R.1    Bonhoeffer, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.