메뉴 건너뛰기




Volumn 78, Issue , 2016, Pages 351-365

Long-Term Potentiation: From CaMKII to AMPA Receptor Trafficking

Author keywords

LTP; Memory; Plasticity; Spine; Synapse

Indexed keywords

AMPA RECEPTOR; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II;

EID: 84958659265     PISSN: 00664278     EISSN: 15451585     Source Type: Book Series    
DOI: 10.1146/annurev-physiol-021014-071753     Document Type: Review
Times cited : (329)

References (96)
  • 2
    • 0001380992 scopus 로고
    • Frequency potentiation of excitatory synaptic activity in the dentate area of the hippocampal formation
    • Lømo T. 1966. Frequency potentiation of excitatory synaptic activity in the dentate area of the hippocampal formation. Acta Physiol. Scand. 68:128
    • (1966) Acta Physiol. Scand , vol.68 , pp. 128
    • Lømo, T.1
  • 3
    • 0015799240 scopus 로고
    • Long-lasting potentiation of synaptic transmission in the dentate area of the anaesthetized rabbit following stimulation of the perforant path
    • Bliss TV, Lømo T. 1973. Long-lasting potentiation of synaptic transmission in the dentate area of the anaesthetized rabbit following stimulation of the perforant path. J. Physiol. 232:331-56
    • (1973) J. Physiol , vol.232 , pp. 331-356
    • Bliss, T.V.1    Lømo, T.2
  • 4
    • 0037884978 scopus 로고    scopus 로고
    • How long will long-term potentiation last
    • AbrahamWC. 2003. How long will long-term potentiation last? Philos. Trans. R. Soc. B 358:735-44
    • (2003) Philos Trans. R. Soc. B , vol.358 , pp. 735-744
    • Abraham, W.C.1
  • 5
    • 0025150883 scopus 로고
    • Presynaptic mechanism for long-term potentiation in the hippocampus
    • Bekkers JM, Stevens CF. 1990. Presynaptic mechanism for long-term potentiation in the hippocampus. Nature 346:724-29
    • (1990) Nature , vol.346 , pp. 724-729
    • Bekkers, J.M.1    Stevens, C.F.2
  • 6
    • 0025353308 scopus 로고
    • Presynaptic enhancement shown by whole-cell recordings of long-term potentiation in hippocampal slices
    • Malinow R, Tsien RW. 1990. Presynaptic enhancement shown by whole-cell recordings of long-term potentiation in hippocampal slices. Nature 346:177-80
    • (1990) Nature , vol.346 , pp. 177-180
    • Malinow, R.1    Tsien, R.W.2
  • 7
    • 0029162513 scopus 로고
    • Evidence for silent synapses: Implications for the expression of LTP
    • Isaac JT, Nicoll RA, Malenka RC. 1995. Evidence for silent synapses: implications for the expression of LTP. Neuron 15:427-34
    • (1995) Neuron , vol.15 , pp. 427-434
    • Isaac, J.T.1    Nicoll, R.A.2    Malenka, R.C.3
  • 8
    • 0029018512 scopus 로고
    • Activation of postsynaptically silent synapses during pairinginduced LTP in CA1 region of hippocampal slice
    • Liao D, Hessler NA, Malinow R. 1995. Activation of postsynaptically silent synapses during pairinginduced LTP in CA1 region of hippocampal slice. Nature 375:400-4
    • (1995) Nature , vol.375 , pp. 400-404
    • Liao, D.1    Hessler, N.A.2    Malinow, R.3
  • 9
    • 54249097847 scopus 로고    scopus 로고
    • Silent synapses and the emergence of a postsynapticmechanism for LTP
    • Kerchner GA, Nicoll RA. 2008. Silent synapses and the emergence of a postsynapticmechanism for LTP. Nat. Rev. Neurosci. 9:813-25
    • (2008) Nat. Rev. Neurosci , vol.9 , pp. 813-825
    • Kerchner, G.A.1    Nicoll, R.A.2
  • 10
    • 0020647470 scopus 로고
    • Excitatory amino acids in synaptic transmission in the Schaffer collateral-commissural pathway of the rat hippocampus
    • Collingridge GL, Kehl SJ, McLennan H. 1983. Excitatory amino acids in synaptic transmission in the Schaffer collateral-commissural pathway of the rat hippocampus. J. Physiol. 334:33-46
    • (1983) J. Physiol , vol.334 , pp. 33-46
    • Collingridge, G.L.1    Kehl, S.J.2    McLennan, H.3
  • 11
    • 84857356081 scopus 로고    scopus 로고
    • Mechanisms of CaMKII action in long-term potentiation
    • Lisman J, Yasuda R, Raghavachari S. 2012. Mechanisms of CaMKII action in long-term potentiation. Nat. Rev. Neurosci. 13:169-82
    • (2012) Nat. Rev. Neurosci , vol.13 , pp. 169-182
    • Lisman, J.1    Yasuda, R.2    Raghavachari, S.3
  • 12
    • 77957675554 scopus 로고    scopus 로고
    • AMPA receptors are exocytosed in stimulated spines and adjacent dendrites in a Ras-ERK-dependentmanner during long-term potentiation
    • Patterson MA, Szatmari EM, Yasuda R. 2010. AMPA receptors are exocytosed in stimulated spines and adjacent dendrites in a Ras-ERK-dependentmanner during long-term potentiation. PNAS 107:15951-56
    • (2010) PNAS , vol.107 , pp. 15951-15956
    • Patterson, M.A.1    Szatmari, E.M.2    Yasuda, R.3
  • 13
    • 84885163085 scopus 로고    scopus 로고
    • Long-term potentiation: Peeling the onion
    • Nicoll RA, Roche KW. 2013. Long-term potentiation: peeling the onion. Neuropharmacology 74:18-22
    • (2013) Neuropharmacology , vol.74 , pp. 18-22
    • Nicoll, R.A.1    Roche, K.W.2
  • 15
    • 84887009409 scopus 로고    scopus 로고
    • AMPARs and synaptic plasticity: The last 25 years
    • Huganir RL, Nicoll RA. 2013. AMPARs and synaptic plasticity: the last 25 years. Neuron 80:704-17
    • (2013) Neuron , vol.80 , pp. 704-717
    • Huganir, R.L.1    Nicoll, R.A.2
  • 16
    • 84890828308 scopus 로고    scopus 로고
    • Plasticity of dendritic spines: Subcompartmentalization of signaling
    • Colgan LA, Yasuda R. 2014. Plasticity of dendritic spines: subcompartmentalization of signaling. Annu. Rev. Physiol. 76:365-85
    • (2014) Annu. Rev. Physiol , vol.76 , pp. 365-385
    • Colgan, L.A.1    Yasuda, R.2
  • 17
    • 84872477442 scopus 로고    scopus 로고
    • Expression of NMDA receptor-dependent LTP in the hippocampus: Bridging the divide
    • Bliss TV, Collingridge GL. 2013. Expression of NMDA receptor-dependent LTP in the hippocampus: bridging the divide. Mol. Brain 6:5
    • (2013) Mol. Brain , vol.6 , pp. 5
    • Bliss, T.V.1    Collingridge, G.L.2
  • 18
    • 0034142054 scopus 로고    scopus 로고
    • Postsynaptic protein phosphorylation and LTP
    • SoderlingTR, Derkach VA. 2000. Postsynaptic protein phosphorylation and LTP. TrendsNeurosci. 23:75-80
    • (2000) TrendsNeurosci , vol.23 , pp. 75-80
    • Soderling, T.R.1    Derkach, V.A.2
  • 19
    • 0026637195 scopus 로고
    • Deficient hippocampal long-term potentiation in alpha-calcium-calmodulin kinase II mutant mice
    • Silva AJ, Stevens CF, Tonegawa S, Wang Y. 1992. Deficient hippocampal long-term potentiation in alpha-calcium-calmodulin kinase II mutant mice. Science 257:201-6
    • (1992) Science , vol.257 , pp. 201-206
    • Silva, A.J.1    Stevens, C.F.2    Tonegawa, S.3    Wang, Y.4
  • 20
    • 0028880861 scopus 로고
    • Calcium/ calmodulin-dependent kinase II and long-term potentiation enhance synaptic transmission by the same mechanism
    • Lledo PM, Hjelmstad GO, Mukherji S, Soderling TR, Malenka RC, Nicoll RA. 1995. Calcium/ calmodulin-dependent kinase II and long-term potentiation enhance synaptic transmission by the same mechanism. PNAS 92:11175-79
    • (1995) PNAS , vol.92 , pp. 11175-11179
    • Lledo, P.M.1    Hjelmstad, G.O.2    Mukherji, S.3    Soderling, T.R.4    Malenka, R.C.5    Nicoll, R.A.6
  • 21
    • 0028579743 scopus 로고
    • Potentiated transmission and prevention of further LTP by increased CaMKII activity in postsynaptic hippocampal slice neurons
    • Pettit DL, Perlman S, Malinow R. 1994. Potentiated transmission and prevention of further LTP by increased CaMKII activity in postsynaptic hippocampal slice neurons. Science 266:1881-85
    • (1994) Science , vol.266 , pp. 1881-1885
    • Pettit, D.L.1    Perlman, S.2    Malinow, R.3
  • 22
    • 0032488659 scopus 로고    scopus 로고
    • Autophosphorylation at Thr286 of the alpha calcium-calmodulin kinase II in LTP and learning
    • Giese KP, Fedorov NB, Filipkowski RK, Silva AJ. 1998. Autophosphorylation at Thr286 of the alpha calcium-calmodulin kinase II in LTP and learning. Science 279:870-73
    • (1998) Science , vol.279 , pp. 870-873
    • Giese, K.P.1    Fedorov, N.B.2    Filipkowski, R.K.3    Silva, A.J.4
  • 23
    • 0027480086 scopus 로고
    • Phosphorylation and regulation of glutamate receptors by calcium calmodulin-dependent protein kinase-II
    • McGlade-McCulloh E, Yamamoto H, Tan SE, Brickey DA, Soderling TR. 1993. Phosphorylation and regulation of glutamate receptors by calcium calmodulin-dependent protein kinase-II. Nature 362:640-42
    • (1993) Nature , vol.362 , pp. 640-642
    • McGlade-McCulloh, E.1    Yamamoto, H.2    Tan, S.E.3    Brickey, D.A.4    Soderling, T.R.5
  • 24
    • 0030744875 scopus 로고    scopus 로고
    • Regulatory phosphorylation of AMPAtype glutamate receptors by CaM-KII during long-term potentiation
    • Barria A, MullerD,Derkach V, Griffith LC, Soderling TR. 1997. Regulatory phosphorylation of AMPAtype glutamate receptors by CaM-KII during long-term potentiation. Science 276:2042-45
    • (1997) Science , vol.276 , pp. 2042-2045
    • Barria, A.1    Muller, D.2    Derkach, V.3    Griffith, L.C.4    Soderling, T.R.5
  • 25
    • 0031283172 scopus 로고    scopus 로고
    • Identification of the Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in the alpha-amino-3-hydroxyl-5-methyl-4-isoxazole-propionate-type glutamate receptor
    • Barria A, Derkach V, Soderling T. 1997. Identification of the Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in the alpha-amino-3-hydroxyl-5-methyl-4-isoxazole-propionate-type glutamate receptor. J. Biol. Chem. 272:32727-30
    • (1997) J. Biol. Chem , vol.272 , pp. 32727-32730
    • Barria, A.1    Derkach, V.2    Soderling, T.3
  • 26
    • 0031435496 scopus 로고    scopus 로고
    • Phosphorylation of the alpha-amino-3-hydroxy-5-methylisoxazole4-propionic acid receptor GluR1 subunit by calcium/calmodulin-dependent kinase I.I
    • Mammen AL, Kameyama K, Roche KW, Huganir RL. 1997. Phosphorylation of the alpha-amino-3-hydroxy-5-methylisoxazole4-propionic acid receptor GluR1 subunit by calcium/calmodulin-dependent kinase II. J. Biol. Chem. 272:32528-33
    • (1997) J. Biol. Chem , vol.272 , pp. 32528-32533
    • Mammen, A.L.1    Kameyama, K.2    Roche, K.W.3    Huganir, R.L.4
  • 27
    • 0037423916 scopus 로고    scopus 로고
    • Phosphorylation of the AMPA receptor GluR1 subunit is required for synaptic plasticity and retention of spatial memory
    • Lee HK, Takamiya K, Han JS, Man H, Kim CH, et al. 2003. Phosphorylation of the AMPA receptor GluR1 subunit is required for synaptic plasticity and retention of spatial memory. Cell 112:631-43
    • (2003) Cell , vol.112 , pp. 631-643
    • Lee, H.K.1    Takamiya, K.2    Han, J.S.3    Man, H.4    Kim, C.H.5
  • 28
    • 0037312605 scopus 로고    scopus 로고
    • PKA phosphorylation of AMPA receptor subunits controls synaptic trafficking underlying plasticity
    • Esteban JA, Shi SH, Wilson C, Nuriya M, Huganir RL, Malinow R. 2003. PKA phosphorylation of AMPA receptor subunits controls synaptic trafficking underlying plasticity. Nat. Neurosci. 6:136-43
    • (2003) Nat. Neurosci , vol.6 , pp. 136-143
    • Esteban, J.A.1    Shi, S.H.2    Wilson, C.3    Nuriya, M.4    Huganir, R.L.5    Malinow, R.6
  • 29
    • 33745927153 scopus 로고    scopus 로고
    • Synaptic incorporation of AMPA receptors during LTP is controlled by a PKC phosphorylation site on GluR1
    • Boehm J, Kang MG, Johnson RC, Esteban J, Huganir RL, Malinow R. 2006. Synaptic incorporation of AMPA receptors during LTP is controlled by a PKC phosphorylation site on GluR1. Neuron 51:213-25
    • (2006) Neuron , vol.51 , pp. 213-225
    • Boehm, J.1    Kang, M.G.2    Johnson, R.C.3    Esteban, J.4    Huganir, R.L.5    Malinow, R.6
  • 30
    • 0037339445 scopus 로고    scopus 로고
    • Silence analysis of AMPA receptor mutated at the CaM-kinase II phosphorylation site
    • Derkach VA. 2003. Silence analysis of AMPA receptor mutated at the CaM-kinase II phosphorylation site. Biophys. J. 84:1701-8
    • (2003) Biophys. J , vol.84 , pp. 1701-1708
    • Derkach, V.A.1
  • 31
    • 79960795718 scopus 로고    scopus 로고
    • Mechanism of Ca2+/calmodulin-dependent kinase II regulation of AMPA receptor gating
    • Kristensen AS, Jenkins MA, Banke TG, Schousboe A, Makino Y, et al. 2011. Mechanism of Ca2+/calmodulin-dependent kinase II regulation of AMPA receptor gating. Nat. Neurosci. 14:727-35
    • (2011) Nat. Neurosci , vol.14 , pp. 727-735
    • Kristensen, A.S.1    Jenkins, M.A.2    Banke, T.G.3    Schousboe, A.4    Makino, Y.5
  • 32
    • 0034708587 scopus 로고    scopus 로고
    • Driving AMPA receptors into synapses by LTP and CaMKII: Requirement forGluR1 and PDZ domain interaction
    • Hayashi Y, Shi SH, Esteban JA, Piccini A, Poncer JC, Malinow R. 2000. Driving AMPA receptors into synapses by LTP and CaMKII: requirement forGluR1 and PDZ domain interaction. Science 287:2262-67
    • (2000) Science , vol.287 , pp. 2262-2267
    • Hayashi, Y.1    Shi, S.H.2    Esteban, J.A.3    Piccini, A.4    Poncer, J.C.5    Malinow, R.6
  • 33
    • 0035805143 scopus 로고    scopus 로고
    • Subunit-specific rules governing AMPA receptor trafficking to synapses in hippocampal pyramidal neurons
    • Shi S, Hayashi Y, Esteban JA, Malinow R. 2001. Subunit-specific rules governing AMPA receptor trafficking to synapses in hippocampal pyramidal neurons. Cell 105:331-43
    • (2001) Cell , vol.105 , pp. 331-343
    • Shi, S.1    Hayashi, Y.2    Esteban, J.A.3    Malinow, R.4
  • 34
    • 0033546059 scopus 로고    scopus 로고
    • Importance of AMPA receptors for hippocampal synaptic plasticity but not for spatial learning
    • Zamanillo D, Sprengel R, Hvalby O, Jensen V, Burnashev N, et al. 1999. Importance of AMPA receptors for hippocampal synaptic plasticity but not for spatial learning. Science 284:1805-11
    • (1999) Science , vol.284 , pp. 1805-1811
    • Zamanillo, D.1    Sprengel, R.2    Hvalby, O.3    Jensen, V.4    Burnashev, N.5
  • 35
    • 0038305219 scopus 로고    scopus 로고
    • Synaptic transmission and plasticity in the absence of AMPA glutamate receptor GluR2 and GluR3
    • Meng Y, Zhang Y, Jia Z. 2003. Synaptic transmission and plasticity in the absence of AMPA glutamate receptor GluR2 and GluR3. Neuron 39:163-76
    • (2003) Neuron , vol.39 , pp. 163-176
    • Meng, Y.1    Zhang, Y.2    Jia, Z.3
  • 36
    • 79955089674 scopus 로고    scopus 로고
    • The expanding social network of ionotropic glutamate receptors: TARPs and other transmembrane auxiliary subunits
    • Jackson AC, Nicoll RA. 2011. The expanding social network of ionotropic glutamate receptors: TARPs and other transmembrane auxiliary subunits. Neuron 70:178-99
    • (2011) Neuron , vol.70 , pp. 178-199
    • Jackson, A.C.1    Nicoll, R.A.2
  • 37
    • 84861001245 scopus 로고    scopus 로고
    • The regulation of glutamate receptor trafficking and function by TARPs and other transmembrane auxiliary subunits
    • Straub C, Tomita S. 2012. The regulation of glutamate receptor trafficking and function by TARPs and other transmembrane auxiliary subunits. Curr. Opin. Neurobiol. 22:488-95
    • (2012) Curr. Opin. Neurobiol , vol.22 , pp. 488-495
    • Straub, C.1    Tomita, S.2
  • 38
    • 12344289653 scopus 로고    scopus 로고
    • Bidirectional synaptic plasticity regulated by phosphorylation of stargazin-like TARPs
    • Tomita S, Stein V, Stocker TJ, Nicoll RA, Bredt DS. 2005. Bidirectional synaptic plasticity regulated by phosphorylation of stargazin-like TARPs. Neuron 45:269-77
    • (2005) Neuron , vol.45 , pp. 269-277
    • Tomita, S.1    Stein, V.2    Stocker, T.J.3    Nicoll, R.A.4    Bredt, D.S.5
  • 39
    • 77953658109 scopus 로고    scopus 로고
    • TARP phosphorylation regulates synaptic AMPA receptors through lipid bilayers
    • Sumioka A, Yan D, Tomita S. 2010. TARP phosphorylation regulates synaptic AMPA receptors through lipid bilayers. Neuron 66:755-67
    • (2010) Neuron , vol.66 , pp. 755-767
    • Sumioka, A.1    Yan, D.2    Tomita, S.3
  • 40
    • 84872936192 scopus 로고    scopus 로고
    • LTP requires a reserve pool of glutamate receptors independent of subunit type
    • Granger AJ, Shi Y, Lu W, Cerpas M, Nicoll RA. 2013. LTP requires a reserve pool of glutamate receptors independent of subunit type. Nature 493:495-500
    • (2013) Nature , vol.493 , pp. 495-500
    • Granger, A.J.1    Shi, Y.2    Lu, W.3    Cerpas, M.4    Nicoll, R.A.5
  • 41
    • 0042856419 scopus 로고    scopus 로고
    • Stargazin differentially controls the trafficking of alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionate and kainate receptors
    • Chen L, El-Husseini A,Tomita S, Bredt DS,Nicoll RA. 2003. Stargazin differentially controls the trafficking of alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionate and kainate receptors. Mol. Pharmacol. 64:703-6
    • (2003) Mol. Pharmacol , vol.64 , pp. 703-706
    • Chen, L.1    El-Husseini, A.2    Tomita, S.3    Bredt, D.S.4    Nicoll, R.A.5
  • 42
    • 84863488995 scopus 로고    scopus 로고
    • Regulation of AMPA receptor surface diffusion by PSD-95 slots
    • Opazo P, Sainlos M, Choquet D. 2012. Regulation of AMPA receptor surface diffusion by PSD-95 slots. Curr. Opin. Neurobiol. 22:453-60
    • (2012) Curr. Opin. Neurobiol , vol.22 , pp. 453-460
    • Opazo, P.1    Sainlos, M.2    Choquet, D.3
  • 43
    • 3042554012 scopus 로고    scopus 로고
    • Structural basis of long-term potentiation in single dendritic spines
    • MatsuzakiM, Honkura N, Ellis-Davies GC, Kasai H. 2004. Structural basis of long-term potentiation in single dendritic spines. Nature 429:761-66
    • (2004) Nature , vol.429 , pp. 761-766
    • Matsuzaki, M.1    Honkura, N.2    Ellis-Davies, G.C.3    Kasai, H.4
  • 44
    • 37549053317 scopus 로고    scopus 로고
    • Locally dynamic synaptic learning rules in pyramidal neuron dendrites
    • Harvey CD, Svoboda K. 2007. Locally dynamic synaptic learning rules in pyramidal neuron dendrites. Nature 450:1195-200
    • (2007) Nature , vol.450 , pp. 1195-1200
    • Harvey, C.D.1    Svoboda, K.2
  • 45
    • 62649108345 scopus 로고    scopus 로고
    • Activation of CaMKII in single dendritic spines during long-term potentiation
    • Lee SJ, Escobedo-Lozoya Y, Szatmari EM, Yasuda R. 2009. Activation of CaMKII in single dendritic spines during long-term potentiation. Nature 458:299-304
    • (2009) Nature , vol.458 , pp. 299-304
    • Lee, S.J.1    Escobedo-Lozoya, Y.2    Szatmari, E.M.3    Yasuda, R.4
  • 46
    • 7044267351 scopus 로고    scopus 로고
    • Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity
    • Okamoto K, Nagai T, Miyawaki A, Hayashi Y. 2004. Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity. Nat. Neurosci. 7:1104-12
    • (2004) Nat. Neurosci , vol.7 , pp. 1104-1112
    • Okamoto, K.1    Nagai, T.2    Miyawaki, A.3    Hayashi, Y.4
  • 47
    • 33644560354 scopus 로고    scopus 로고
    • Glutamate receptor exocytosis and spine enlargement during chemically induced long-term potentiation
    • Kopec CD, Li B, WeiW, Boehm J, Malinow R. 2006. Glutamate receptor exocytosis and spine enlargement during chemically induced long-term potentiation. J. Neurosci. 26:2000-9
    • (2006) J. Neurosci , vol.26 , pp. 2000-2009
    • Kopec, C.D.1    Li, B.2    Wei, W.3    Boehm, J.4    Malinow, R.5
  • 48
    • 84899633952 scopus 로고    scopus 로고
    • Spine neck plasticity regulates compartmentalization of synapses
    • Tönnesen J, Katona G, Rózsa B, Nägerl UV. 2014. Spine neck plasticity regulates compartmentalization of synapses. Nat. Neurosci. 17:678-85
    • (2014) Nat. Neurosci , vol.17 , pp. 678-685
    • Tönnesen, J.1    Katona, G.2    Rózsa, B.3    Nägerl, U.V.4
  • 49
    • 84898688394 scopus 로고    scopus 로고
    • Structural and molecular remodeling of dendritic spine substructures during long-term potentiation
    • Bosch M, Castro J, Saneyoshi T, Matsuno H, Sur M, Hayashi Y. 2014. Structural and molecular remodeling of dendritic spine substructures during long-term potentiation. Neuron 82:444-59
    • (2014) Neuron , vol.82 , pp. 444-459
    • Bosch, M.1    Castro, J.2    Saneyoshi, T.3    Matsuno, H.4    Sur, M.5    Hayashi, Y.6
  • 50
    • 0038045645 scopus 로고    scopus 로고
    • Postsynaptic density-95 mimics and occludes hippocampal long-term potentiation and enhances long-term depression
    • SteinV,HouseDR, BredtDS, Nicoll RA. 2003. Postsynaptic density-95 mimics and occludes hippocampal long-term potentiation and enhances long-term depression. J. Neurosci. 23:5503-6
    • (2003) J. Neurosci , vol.23 , pp. 5503-5506
    • Stein, V.1    House, D.R.2    Bredt, D.S.3    Nicoll, R.A.4
  • 51
    • 7044271080 scopus 로고    scopus 로고
    • Quaternary structure, protein dynamics, and synaptic function of SAP97 controlled by L27 domain interactions
    • Nakagawa T, FutaiK, Lashuel HA, Lo I,Okamoto K, et al. 2004. Quaternary structure, protein dynamics, and synaptic function of SAP97 controlled by L27 domain interactions. Neuron 44:453-67
    • (2004) Neuron , vol.44 , pp. 453-467
    • Nakagawa, T.1    Futai, K.2    Lashuel, H.A.3    Lo, I.4    Okamoto, K.5
  • 52
    • 34247237148 scopus 로고    scopus 로고
    • PSD-95 is required for activity-driven synapse stabilization
    • Ehrlich I, Klein M, Rumpel S, Malinow R. 2007. PSD-95 is required for activity-driven synapse stabilization. PNAS 104:4176-81
    • (2007) PNAS , vol.104 , pp. 4176-4181
    • Ehrlich, I.1    Klein, M.2    Rumpel, S.3    Malinow, R.4
  • 53
    • 40249097516 scopus 로고    scopus 로고
    • The subspine organization of actin fibers regulates the structure and plasticity of dendritic spines
    • Honkura N, Matsuzaki M, Noguchi J, Ellis-Davies GCR, Kasai H. 2008. The subspine organization of actin fibers regulates the structure and plasticity of dendritic spines. Neuron 57:719-29
    • (2008) Neuron , vol.57 , pp. 719-729
    • Honkura, N.1    Matsuzaki, M.2    Noguchi, J.3    Ellis-Davies, G.C.R.4    Kasai, H.5
  • 54
    • 84863462907 scopus 로고    scopus 로고
    • Structural plasticity of dendritic spines
    • Bosch M, Hayashi Y. 2012. Structural plasticity of dendritic spines. Curr. Opin. Neurobiol. 22:383-88
    • (2012) Curr. Opin. Neurobiol , vol.22 , pp. 383-388
    • Bosch, M.1    Hayashi, Y.2
  • 56
    • 84864343109 scopus 로고    scopus 로고
    • Structural modulation of dendritic spines during synaptic plasticity
    • Fortin DA, Srivastava T, Soderling TR. 2012. Structural modulation of dendritic spines during synaptic plasticity. Neuroscientist 18:326-41
    • (2012) Neuroscientist , vol.18 , pp. 326-341
    • Fortin, D.A.1    Srivastava, T.2    Soderling, T.R.3
  • 57
    • 46849102728 scopus 로고    scopus 로고
    • The spread of Ras activity triggered by activation of a single dendritic spine
    • Harvey CD, Yasuda R, Zhong HN, Svoboda K. 2008. The spread of Ras activity triggered by activation of a single dendritic spine. Science 321:136-40
    • (2008) Science , vol.321 , pp. 136-140
    • Harvey, C.D.1    Yasuda, R.2    Zhong, H.N.3    Svoboda, K.4
  • 58
    • 0033152432 scopus 로고    scopus 로고
    • A role of actin filament in synaptic transmission and long-term potentiation
    • Kim CH, Lisman JE. 1999. A role of actin filament in synaptic transmission and long-term potentiation. J. Neurosci. 19:4314-24
    • (1999) J. Neurosci , vol.19 , pp. 4314-4324
    • Kim, C.H.1    Lisman, J.E.2
  • 59
    • 79953748494 scopus 로고    scopus 로고
    • Local, persistent activation of Rho GTPases during plasticity of single dendritic spines
    • Murakoshi H, Wang H, Yasuda R. 2011. Local, persistent activation of Rho GTPases during plasticity of single dendritic spines. Nature 472:100-4
    • (2011) Nature , vol.472 , pp. 100-104
    • Murakoshi, H.1    Wang, H.2    Yasuda, R.3
  • 60
    • 0034661746 scopus 로고    scopus 로고
    • Small GTPases Rac and Rho in the maintenance of dendritic spines and branches in hippocampal pyramidal neurons
    • Nakayama AY, Harms MB, Luo LQ. 2000. Small GTPases Rac and Rho in the maintenance of dendritic spines and branches in hippocampal pyramidal neurons. J. Neurosci. 20:5329-38
    • (2000) J. Neurosci , vol.20 , pp. 5329-5338
    • Nakayama, A.Y.1    Harms, M.B.2    Luo, L.Q.3
  • 61
    • 34548436564 scopus 로고    scopus 로고
    • The postsynaptic architecture of excitatory synapses: Amore quantitative view
    • Sheng M, Hoogenraad CC. 2007. The postsynaptic architecture of excitatory synapses: amore quantitative view. Annu. Rev. Biochem. 76:823-47
    • (2007) Annu. Rev. Biochem , vol.76 , pp. 823-847
    • Sheng, M.1    Hoogenraad, C.C.2
  • 62
    • 77955495739 scopus 로고    scopus 로고
    • Quantifying the effects of elastic collisions and non-covalent binding on glutamate receptor trafficking in the post-synaptic density
    • Santamaria F, Gonzalez J, Augustine GJ, Raghavachari S. 2010. Quantifying the effects of elastic collisions and non-covalent binding on glutamate receptor trafficking in the post-synaptic density. PLOS Comput. Biol. 6:e1000780
    • (2010) PLOS Comput. Biol , vol.6 , pp. e1000780
    • Santamaria, F.1    Gonzalez, J.2    Augustine, G.J.3    Raghavachari, S.4
  • 63
    • 34247464768 scopus 로고    scopus 로고
    • Diffusional trapping of GluR1AMPAreceptors by input-specific synaptic activity
    • EhlersMD,Heine M, Groc L, LeeMC, ChoquetD. 2007. Diffusional trapping of GluR1AMPAreceptors by input-specific synaptic activity. Neuron 54:447-60
    • (2007) Neuron , vol.54 , pp. 447-460
    • Ehlers, M.D.1    Heine, M.2    Groc, L.3    Lee, M.C.4    Choquet, D.5
  • 64
    • 0032054473 scopus 로고    scopus 로고
    • Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: Differential attachment of NMDA versus AMPA receptors
    • Allison DW, Gelfand VI, Spector I, Craig AM. 1998. Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: differential attachment of NMDA versus AMPA receptors. J. Neurosci. 18:2423-36
    • (1998) J. Neurosci , vol.18 , pp. 2423-2436
    • Allison, D.W.1    Gelfand, V.I.2    Spector, I.3    Craig, A.M.4
  • 65
    • 0035970107 scopus 로고    scopus 로고
    • Contribution of cytoskeleton to the internalization of AMPAreceptors
    • Zhou Q, Xiao M, Nicoll RA. 2001. Contribution of cytoskeleton to the internalization of AMPAreceptors. PNAS 98:1261-66
    • (2001) PNAS , vol.98 , pp. 1261-1266
    • Zhou, Q.1    Xiao, M.2    Nicoll, R.A.3
  • 66
    • 33748185659 scopus 로고    scopus 로고
    • Cytoskeleton regulation of glycine receptor number at synapses and diffusion in the plasma membrane
    • Charrier C, Ehrensperger MV, Dahan M, Levi S, Triller A. 2006. Cytoskeleton regulation of glycine receptor number at synapses and diffusion in the plasma membrane. J. Neurosci. 26:8502-11
    • (2006) J. Neurosci , vol.26 , pp. 8502-8511
    • Charrier, C.1    Ehrensperger, M.V.2    Dahan, M.3    Levi, S.4    Triller, A.5
  • 68
    • 0035132869 scopus 로고    scopus 로고
    • Activation of synaptic NMDA receptors induces membrane insertion of newAMPAreceptors andLTPin cultured hippocampal neurons
    • Lu W, Man H, Ju W, Trimble WS, MacDonald JF, Wang YT. 2001. Activation of synaptic NMDA receptors induces membrane insertion of newAMPAreceptors andLTPin cultured hippocampal neurons. Neuron 29:243-54
    • (2001) Neuron , vol.29 , pp. 243-254
    • Lu, W.1    Man, H.2    Ju, W.3    Trimble, W.S.4    MacDonald, J.F.5    Wang, Y.T.6
  • 69
    • 77951913551 scopus 로고    scopus 로고
    • Syntaxin-4 defines a domain for activitydependent exocytosis in dendritic spines
    • Kennedy MJ, Davison IG, Robinson CG, Ehlers MD. 2010. Syntaxin-4 defines a domain for activitydependent exocytosis in dendritic spines. Cell 141:524-35
    • (2010) Cell , vol.141 , pp. 524-535
    • Kennedy, M.J.1    Davison, I.G.2    Robinson, C.G.3    Ehlers, M.D.4
  • 72
    • 84863011177 scopus 로고    scopus 로고
    • Postsynaptic complexin controls AMPA receptor exocytosis during LTP
    • AhmadM, Polepalli JS,Goswami D, Yang X, Kaeser-Woo YJ, et al. 2012. Postsynaptic complexin controls AMPA receptor exocytosis during LTP. Neuron 73:260-67
    • (2012) Neuron , vol.73 , pp. 260-267
    • Ahmad, M.1    Polepalli, J.S.2    Goswami, D.3    Yang, X.4    Kaeser-Woo, Y.J.5
  • 74
    • 84889030400 scopus 로고    scopus 로고
    • Secretagogue stimulation of neurosecretory cells elicits filopodial extensions uncovering new functional release sites
    • Papadopulos A, Martin S, Tomatis VM, Gormal RS,Meunier FA. 2013. Secretagogue stimulation of neurosecretory cells elicits filopodial extensions uncovering new functional release sites. J. Neurosci. 33:19143-53
    • (2013) J. Neurosci , vol.33 , pp. 19143-19153
    • Papadopulos, A.1    Martin, S.2    Tomatis, V.M.3    Gormal, R.S.4    Meunier, F.A.5
  • 75
    • 12544259110 scopus 로고    scopus 로고
    • A direct interaction between Cdc42 and vesicle-associated membrane protein 2 regulates SNARE-dependent insulin exocytosis
    • Nevins AK, Thurmond DC. 2005. A direct interaction between Cdc42 and vesicle-associated membrane protein 2 regulates SNARE-dependent insulin exocytosis. J. Biol. Chem. 280:1944-52
    • (2005) J. Biol. Chem , vol.280 , pp. 1944-1952
    • Nevins, A.K.1    Thurmond, D.C.2
  • 76
    • 0030175394 scopus 로고    scopus 로고
    • Definition of the readily releasable pool of vesicles at hippocampal synapses
    • Rosenmund C, Stevens CF. 1996. Definition of the readily releasable pool of vesicles at hippocampal synapses. Neuron 16:1197-207
    • (1996) Neuron , vol.16 , pp. 1197-1207
    • Rosenmund, C.1    Stevens, C.F.2
  • 77
    • 41149119949 scopus 로고    scopus 로고
    • Motor protein-dependent transport of AMPA receptors into spines during long-term potentiation
    • Correia SS, Bassani S, Brown TC, Lise MF, Backos DS, et al. 2008. Motor protein-dependent transport of AMPA receptors into spines during long-term potentiation. Nat. Neurosci. 11:457-66
    • (2008) Nat. Neurosci , vol.11 , pp. 457-466
    • Correia, S.S.1    Bassani, S.2    Brown, T.C.3    Lise, M.F.4    Backos, D.S.5
  • 78
    • 54549123514 scopus 로고    scopus 로고
    • Myosin Vb mobilizes recycling endosomes and AMPA receptors for postsynaptic plasticity
    • Wang ZP, Edwards JG, Riley N, Provance DW, Karcher R, et al. 2008. Myosin Vb mobilizes recycling endosomes and AMPA receptors for postsynaptic plasticity. Cell 135:535-48
    • (2008) Cell , vol.135 , pp. 535-548
    • Wang, Z.P.1    Edwards, J.G.2    Riley, N.3    Provance, D.W.4    Karcher, R.5
  • 79
    • 0035071224 scopus 로고    scopus 로고
    • Hippocampal synaptic transmission and plasticity are preserved in myosin Va mutant mice
    • Schnell E, Nicoll RA. 2001. Hippocampal synaptic transmission and plasticity are preserved in myosin Va mutant mice. J. Neurophysiol. 85:1498-501
    • (2001) J. Neurophysiol , vol.85 , pp. 1498-1501
    • Schnell, E.1    Nicoll, R.A.2
  • 80
    • 0031023590 scopus 로고    scopus 로고
    • Three-dimensional organization of smooth endoplasmic reticulum in hippocampal CA1 dendrites and dendritic spines of the immature and mature rat
    • Spacek J, Harris KM. 1997. Three-dimensional organization of smooth endoplasmic reticulum in hippocampal CA1 dendrites and dendritic spines of the immature and mature rat. J. Neurosci. 17:190-203
    • (1997) J. Neurosci , vol.17 , pp. 190-203
    • Spacek, J.1    Harris, K.M.2
  • 81
    • 0028841456 scopus 로고
    • High-resolution immunogold localization of AMPA type glutamate receptor subunits at synaptic and non-synaptic sites in rat hippocampus
    • Baude A, Nuzzer Z, Molnar E, McIlhinney RAJ, Somogyi P. 1995. High-resolution immunogold localization of AMPA type glutamate receptor subunits at synaptic and non-synaptic sites in rat hippocampus. Neuroscience 69:1031-55
    • (1995) Neuroscience , vol.69 , pp. 1031-1055
    • Baude, A.1    Nuzzer, Z.2    Molnar, E.3    McIlhinney, R.A.J.4    Somogyi, P.5
  • 83
    • 70350752569 scopus 로고    scopus 로고
    • AMPA receptor incorporation into synapses during LTP: The role of lateral movement and exocytosis
    • Makino H, Malinow R. 2009. AMPA receptor incorporation into synapses during LTP: the role of lateral movement and exocytosis. Neuron 64:381-90
    • (2009) Neuron , vol.64 , pp. 381-390
    • Makino, H.1    Malinow, R.2
  • 84
    • 67649800746 scopus 로고    scopus 로고
    • Regulation ofAMPAreceptor extrasynaptic insertion by 4 1N, phosphorylation and palmitoylation
    • LinDT, Makino Y, SharmaK,Hayashi T, Neve R, et al. 2009. Regulation ofAMPAreceptor extrasynaptic insertion by 4.1N, phosphorylation and palmitoylation. Nat. Neurosci. 12:879-87
    • (2009) Nat. Neurosci , vol.12 , pp. 879-887
    • Lin, D.T.1    Makino, Y.2    Sharma, K.3    Hayashi, T.4    Neve, R.5
  • 85
    • 35348815012 scopus 로고    scopus 로고
    • Real-time imaging of discrete exocytic events mediating surface delivery of AMPA receptors
    • Yudowski GA, Puthenveedu MA, Leonoudakis D, Panicker S, Thorn KS, et al. 2007. Real-time imaging of discrete exocytic events mediating surface delivery of AMPA receptors. J. Neurosci. 27:11112-21
    • (2007) J. Neurosci , vol.27 , pp. 11112-11121
    • Yudowski, G.A.1    Puthenveedu, M.A.2    Leonoudakis, D.3    Panicker, S.4    Thorn, K.S.5
  • 86
    • 84920715741 scopus 로고    scopus 로고
    • Rapid dispersion of SynGAP from synaptic spines triggers AMPA receptor insertion and spine enlargement during LTP
    • Araki Y, Zeng ML, Zhang MJ, Huganir RL. 2015. Rapid dispersion of SynGAP from synaptic spines triggers AMPA receptor insertion and spine enlargement during LTP. Neuron 85:173-89
    • (2015) Neuron , vol.85 , pp. 173-189
    • Araki, Y.1    Zeng, M.L.2    Zhang, M.J.3    Huganir, R.L.4
  • 87
  • 88
    • 84883437410 scopus 로고    scopus 로고
    • RasGRF2 Rac-GEF activity couples NMDA receptor calcium flux to enhanced synaptic transmission
    • Schwechter B, Rosenmund C, Tolias KF. 2013. RasGRF2 Rac-GEF activity couples NMDA receptor calcium flux to enhanced synaptic transmission. PNAS 110:14462-67
    • (2013) PNAS , vol.110 , pp. 14462-14467
    • Schwechter, B.1    Rosenmund, C.2    Tolias, K.F.3
  • 89
    • 77955379103 scopus 로고    scopus 로고
    • Long-term potentiation in the CA1 hippocampus induced by NR2A subunit-containing NMDA glutamate receptors is mediated by Ras-GRF2/Erk MAP kinase signaling
    • Jin SX, Feig LA. 2010. Long-term potentiation in the CA1 hippocampus induced by NR2A subunit-containing NMDA glutamate receptors is mediated by Ras-GRF2/Erk MAP kinase signaling. PLOS ONE 5:e11732
    • (2010) PLOS ONE , vol.5 , pp. e11732
    • Jin, S.X.1    Feig, L.A.2
  • 90
    • 36049008808 scopus 로고    scopus 로고
    • Kalirin-7 controls activity-dependent structural and functional plasticity of dendritic spines
    • Xie Z, Srivastava DP, Photowala H, Kai L, Cahill ME, et al. 2007. Kalirin-7 controls activity-dependent structural and functional plasticity of dendritic spines. Neuron 56:640-56
    • (2007) Neuron , vol.56 , pp. 640-656
    • Xie, Z.1    Srivastava, D.P.2    Photowala, H.3    Kai, L.4    Cahill, M.E.5
  • 91
    • 58149390800 scopus 로고    scopus 로고
    • Kalirin-7 is required for synaptic structure and function
    • Ma XM, Kiraly DD, Gaier ED, Wang Y, Kim EJ, et al. 2008. Kalirin-7 is required for synaptic structure and function. J. Neurosci. 28:12368-82
    • (2008) J. Neurosci , vol.28 , pp. 12368-12382
    • Ma, X.M.1    Kiraly, D.D.2    Gaier, E.D.3    Wang, Y.4    Kim, E.J.5
  • 92
    • 80052344234 scopus 로고    scopus 로고
    • Kalirin binds the NR2B subunit of the NMDA receptor, altering its synaptic localization and function
    • Kiraly DD, Lemtiri-Chlieh F, Levine ES, Mains RE, Eipper BA. 2011. Kalirin binds the NR2B subunit of the NMDA receptor, altering its synaptic localization and function. J. Neurosci. 31:12554-65
    • (2011) J. Neurosci , vol.31 , pp. 12554-12565
    • Kiraly, D.D.1    Lemtiri-Chlieh, F.2    Levine, E.S.3    Mains, R.E.4    Eipper, B.A.5
  • 94
    • 84862773457 scopus 로고    scopus 로고
    • Rho GTPase regulation by miRNAs and covalent modifications
    • Liu M, Bi F, Zhou X, Zheng Y. 2012. Rho GTPase regulation by miRNAs and covalent modifications. Trends Cell Biol. 22:365-73
    • (2012) Trends Cell Biol , vol.22 , pp. 365-373
    • Liu, M.1    Bi, F.2    Zhou, X.3    Zheng, Y.4
  • 95
    • 84861091777 scopus 로고    scopus 로고
    • Kalirin, a key player in synapse formation, is implicated in human diseases
    • Mandela P, Ma XM. 2012. Kalirin, a key player in synapse formation, is implicated in human diseases. Neural Plast. 2012:728161
    • (2012) Neural Plast , vol.2012 , pp. 728161
    • Mandela, P.1    Ma, X.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.