메뉴 건너뛰기




Volumn 139, Issue 6, 2016, Pages 959-972

Interplay of enzymatic and structural functions of CaMKII in long-term potentiation

Author keywords

CaMKII; cytoskeleton; synaptic plasticity

Indexed keywords

ACTIN; ALPHA AMINO 3 HYDROXY 5 METHYL 4 ISOXAZOLEPROPIONIC ACID; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CALMODULIN; CASEIN KINASE II; GLUTAMATE RECEPTOR; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PROTEASOME; PROTEIN ARC; PROTEIN ARG3.1; UNCLASSIFIED DRUG;

EID: 84977118618     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/jnc.13672     Document Type: Review
Times cited : (37)

References (143)
  • 2
    • 84920715741 scopus 로고    scopus 로고
    • Rapid dispersion of SynGAP from synaptic spines triggers AMPA receptor insertion and spine enlargement during LTP
    • Araki Y., Zeng M., Zhang M. and Huganir R. L. (2015) Rapid dispersion of SynGAP from synaptic spines triggers AMPA receptor insertion and spine enlargement during LTP. Neuron 85, 173–189.
    • (2015) Neuron , vol.85 , pp. 173-189
    • Araki, Y.1    Zeng, M.2    Zhang, M.3    Huganir, R.L.4
  • 3
    • 26944487610 scopus 로고    scopus 로고
    • NMDA receptor subunit composition controls synaptic plasticity by regulating binding to CaMKII
    • Barria A. and Malinow R. (2005) NMDA receptor subunit composition controls synaptic plasticity by regulating binding to CaMKII. Neuron 48, 289–301.
    • (2005) Neuron , vol.48 , pp. 289-301
    • Barria, A.1    Malinow, R.2
  • 4
    • 0030744875 scopus 로고    scopus 로고
    • Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation
    • Barria A., Muller D., Derkach V., Griffith L. C. and Soderling T. R. (1997) Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation. Science 276, 2042–2045.
    • (1997) Science , vol.276 , pp. 2042-2045
    • Barria, A.1    Muller, D.2    Derkach, V.3    Griffith, L.C.4    Soderling, T.R.5
  • 5
    • 0035859082 scopus 로고    scopus 로고
    • Interaction with the NMDA receptor locks CaMKII in an active conformation
    • Bayer K. U., De Koninck P., Leonard A. S., Hell J. W. and Schulman H. (2001) Interaction with the NMDA receptor locks CaMKII in an active conformation. Nature 411, 801–805.
    • (2001) Nature , vol.411 , pp. 801-805
    • Bayer, K.U.1    De Koninck, P.2    Leonard, A.S.3    Hell, J.W.4    Schulman, H.5
  • 6
    • 32544447355 scopus 로고    scopus 로고
    • Transition from reversible to persistent binding of CaMKII to postsynaptic sites and NR2B
    • Bayer K. U., LeBel E., McDonald G. L., O'Leary H., Schulman H. and De Koninck P. (2006) Transition from reversible to persistent binding of CaMKII to postsynaptic sites and NR2B. J. Neurosci. 26, 1164–1174.
    • (2006) J. Neurosci. , vol.26 , pp. 1164-1174
    • Bayer, K.U.1    LeBel, E.2    McDonald, G.L.3    O'Leary, H.4    Schulman, H.5    De Koninck, P.6
  • 7
    • 0021032297 scopus 로고
    • Purification and characterization of a calmodulin-dependent protein kinase that is highly concentrated in brain
    • Bennett M. K., Erondu N. E. and Kennedy M. B. (1983) Purification and characterization of a calmodulin-dependent protein kinase that is highly concentrated in brain. J. Biol. Chem. 258, 12735–12744.
    • (1983) J. Biol. Chem. , vol.258 , pp. 12735-12744
    • Bennett, M.K.1    Erondu, N.E.2    Kennedy, M.B.3
  • 8
    • 33745593049 scopus 로고    scopus 로고
    • Activity-dependent dynamics and sequestration of proteasomes in dendritic spines
    • Bingol B. and Schuman E. M. (2006) Activity-dependent dynamics and sequestration of proteasomes in dendritic spines. Nature 441, 1144–1148.
    • (2006) Nature , vol.441 , pp. 1144-1148
    • Bingol, B.1    Schuman, E.M.2
  • 9
    • 76749131595 scopus 로고    scopus 로고
    • Autophosphorylated CaMKIIalpha acts as a scaffold to recruit proteasomes to dendritic spines
    • Bingol B., Wang C. F., Arnott D., Cheng D., Peng J. and Sheng M. (2010) Autophosphorylated CaMKIIalpha acts as a scaffold to recruit proteasomes to dendritic spines. Cell 140, 567–578.
    • (2010) Cell , vol.140 , pp. 567-578
    • Bingol, B.1    Wang, C.F.2    Arnott, D.3    Cheng, D.4    Peng, J.5    Sheng, M.6
  • 10
    • 0030463470 scopus 로고    scopus 로고
    • 2+- and stimulus duration-dependent switch for hippocampal gene expression
    • 2+- and stimulus duration-dependent switch for hippocampal gene expression. Cell 87, 1203–1214.
    • (1996) Cell , vol.87 , pp. 1203-1214
    • Bito, H.1    Deisseroth, K.2    Tsien, R.W.3
  • 11
    • 0033991008 scopus 로고    scopus 로고
    • Casein kinase 2 as a potentially important enzyme in the nervous system
    • Blanquet P. R. (2000) Casein kinase 2 as a potentially important enzyme in the nervous system. Prog. Neurobiol. 60, 211–246.
    • (2000) Prog. Neurobiol. , vol.60 , pp. 211-246
    • Blanquet, P.R.1
  • 12
    • 79960404131 scopus 로고    scopus 로고
    • betaCaMKII plays a nonenzymatic role in hippocampal synaptic plasticity and learning by targeting alphaCaMKII to synapses
    • Borgesius N. Z., van Woerden G. M., Buitendijk G. H., Keijzer N., Jaarsma D., Hoogenraad C. C. and Elgersma Y. (2011) betaCaMKII plays a nonenzymatic role in hippocampal synaptic plasticity and learning by targeting alphaCaMKII to synapses. J. Neurosci. 31, 10141–10148.
    • (2011) J. Neurosci. , vol.31 , pp. 10141-10148
    • Borgesius, N.Z.1    van Woerden, G.M.2    Buitendijk, G.H.3    Keijzer, N.4    Jaarsma, D.5    Hoogenraad, C.C.6    Elgersma, Y.7
  • 13
    • 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. and Hayashi Y. (2014) Structural and molecular remodeling of dendritic spine substructures during long-term potentiation. Neuron 82, 444–459.
    • (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
  • 14
    • 0028071507 scopus 로고
    • Deficient long-term memory in mice with a targeted mutation of the cAMP-responsive element-binding protein
    • Bourtchuladze R., Frenguelli B., Blendy J., Cioffi D., Schutz G. and Silva A. J. (1994) Deficient long-term memory in mice with a targeted mutation of the cAMP-responsive element-binding protein. Cell 79, 59–68.
    • (1994) Cell , vol.79 , pp. 59-68
    • Bourtchuladze, R.1    Frenguelli, B.2    Blendy, J.3    Cioffi, D.4    Schutz, G.5    Silva, A.J.6
  • 15
    • 0028917370 scopus 로고
    • The multifunctional calcium/calmodulin-dependent protein kinase: from form to function
    • Braun A. P. and Schulman H. (1995) The multifunctional calcium/calmodulin-dependent protein kinase: from form to function. Annu. Rev. Physiol. 57, 417–445.
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 417-445
    • Braun, A.P.1    Schulman, H.2
  • 16
    • 0028973159 scopus 로고
    • 2+/calmodulin-dependent protein kinase isoforms in rat brain
    • 2+/calmodulin-dependent protein kinase isoforms in rat brain. J. Neurosci. 15, 6797–6808.
    • (1995) J. Neurosci. , vol.15 , pp. 6797-6808
    • Brocke, L.1    Srinivasan, M.2    Schulman, H.3
  • 17
    • 0033529559 scopus 로고    scopus 로고
    • Functional implications of the subunit composition of neuronal CaM kinase II
    • Brocke L., Chiang L. W., Wagner P. D. and Schulman H. (1999) Functional implications of the subunit composition of neuronal CaM kinase II. J. Biol. Chem. 274, 22713–22722.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22713-22722
    • Brocke, L.1    Chiang, L.W.2    Wagner, P.D.3    Schulman, H.4
  • 18
    • 77953798275 scopus 로고    scopus 로고
    • CaMKII “autonomy” is required for initiating but not for maintaining neuronal long-term information storage
    • Buard I., Coultrap S. J., Freund R. K., Lee Y. S., Dell'Acqua M. L., Silva A. J. and Bayer K. U. (2010) CaMKII “autonomy” is required for initiating but not for maintaining neuronal long-term information storage. J. Neurosci., 30, 8214–8220.
    • (2010) J. Neurosci. , vol.30 , pp. 8214-8220
    • Buard, I.1    Coultrap, S.J.2    Freund, R.K.3    Lee, Y.S.4    Dell'Acqua, M.L.5    Silva, A.J.6    Bayer, K.U.7
  • 19
    • 0034737648 scopus 로고    scopus 로고
    • Translocation of the Rac1 guanine nucleotide exchange factor Tiam1 induced by platelet-derived growth factor and lysophosphatidic acid
    • Buchanan F. G., Elliot C. M., Gibbs M. and Exton J. H. (2000) Translocation of the Rac1 guanine nucleotide exchange factor Tiam1 induced by platelet-derived growth factor and lysophosphatidic acid. J. Biol. Chem. 275, 9742–9748.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9742-9748
    • Buchanan, F.G.1    Elliot, C.M.2    Gibbs, M.3    Exton, J.H.4
  • 20
    • 58149379613 scopus 로고    scopus 로고
    • SynGAP regulates steady-state and activity-dependent phosphorylation of cofilin
    • Carlisle H. J., Manzerra P., Marcora E. and Kennedy M. B. (2008) SynGAP regulates steady-state and activity-dependent phosphorylation of cofilin. J. Neurosci. 28, 13673–13683.
    • (2008) J. Neurosci. , vol.28 , pp. 13673-13683
    • Carlisle, H.J.1    Manzerra, P.2    Marcora, E.3    Kennedy, M.B.4
  • 21
    • 80052284705 scopus 로고    scopus 로고
    • 2+/calmodulin- dependent kinase II holoenzyme
    • 2+/calmodulin- dependent kinase II holoenzyme. Cell 146, 732–745.
    • (2011) Cell , vol.146 , pp. 732-745
    • Chao, L.H.1    Stratton, M.M.2    Lee, I.H.3
  • 23
    • 79952680702 scopus 로고    scopus 로고
    • Calcium/calmodulin dependent protein kinase II bound to NMDA receptor 2B subunit exhibits increased ATP affinity and attenuated dephosphorylation
    • Cheriyan J., Kumar P., Mayadevi M., Surolia A. and Omkumar R. V. (2011) Calcium/calmodulin dependent protein kinase II bound to NMDA receptor 2B subunit exhibits increased ATP affinity and attenuated dephosphorylation. PLoS ONE 6, e16495.
    • (2011) PLoS ONE , vol.6
    • Cheriyan, J.1    Kumar, P.2    Mayadevi, M.3    Surolia, A.4    Omkumar, R.V.5
  • 26
    • 84866763385 scopus 로고    scopus 로고
    • CaMKII regulation in information processing and storage
    • Coultrap S. J. and Bayer K. U. (2012) CaMKII regulation in information processing and storage. Trends Neurosci. 35, 607–618.
    • (2012) Trends Neurosci. , vol.35 , pp. 607-618
    • Coultrap, S.J.1    Bayer, K.U.2
  • 29
    • 0032588030 scopus 로고    scopus 로고
    • 2+/calmodulin-kinase II enhances channel conductance of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate type glutamate receptors
    • 2+/calmodulin-kinase II enhances channel conductance of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate type glutamate receptors. Proc. Natl Acad. Sci. USA 96, 3269–3274.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3269-3274
    • Derkach, V.1    Barria, A.2    Soderling, T.R.3
  • 30
    • 70350389831 scopus 로고    scopus 로고
    • Regulation of the proteasome by neuronal activity and calcium/calmodulin-dependent protein kinase II
    • Djakovic S. N., Schwarz L. A., Barylko B., DeMartino G. N. and Patrick G. N. (2009) Regulation of the proteasome by neuronal activity and calcium/calmodulin-dependent protein kinase II. J. Biol. Chem. 284, 26655–26665.
    • (2009) J. Biol. Chem. , vol.284 , pp. 26655-26665
    • Djakovic, S.N.1    Schwarz, L.A.2    Barylko, B.3    DeMartino, G.N.4    Patrick, G.N.5
  • 33
    • 0029991047 scopus 로고    scopus 로고
    • Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit
    • Ehlers M. D., Zhang S., Bernhadt J. P. and Huganir R. L. (1996) Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit. Cell 84, 745–755.
    • (1996) Cell , vol.84 , pp. 745-755
    • Ehlers, M.D.1    Zhang, S.2    Bernhadt, J.P.3    Huganir, R.L.4
  • 35
    • 0022375477 scopus 로고
    • 2+/calmodulin-dependent protein kinase in rat brain
    • 2+/calmodulin-dependent protein kinase in rat brain. J. Neurosci. 5, 3270–3277.
    • (1985) J. Neurosci. , vol.5 , pp. 3270-3277
    • Erondu, N.E.1    Kennedy, M.B.2
  • 36
    • 80054115149 scopus 로고    scopus 로고
    • Quantitative estimates of the cytoplasmic, PSD, and NMDAR-bound pools of CaMKII in dendritic spines
    • Feng B., Raghavachari S. and Lisman J. (2011) Quantitative estimates of the cytoplasmic, PSD, and NMDAR-bound pools of CaMKII in dendritic spines. Brain Res. 1419, 46–52.
    • (2011) Brain Res. , vol.1419 , pp. 46-52
    • Feng, B.1    Raghavachari, S.2    Lisman, J.3
  • 37
    • 0042347897 scopus 로고    scopus 로고
    • Selective regulation of neurite extension and synapse formation by the beta but not the alpha isoform of CaMKII
    • Fink C. C., Bayer K. U., Myers J. W., Ferrell J. E. Jr, Schulman H. and Meyer T. (2003) Selective regulation of neurite extension and synapse formation by the beta but not the alpha isoform of CaMKII. Neuron 39, 283–297.
    • (2003) Neuron , vol.39 , pp. 283-297
    • Fink, C.C.1    Bayer, K.U.2    Myers, J.W.3    Ferrell, J.E.4    Schulman, H.5    Meyer, T.6
  • 39
    • 33749620749 scopus 로고    scopus 로고
    • A balance of protein synthesis and proteasome-dependent degradation determines the maintenance of LTP
    • Fonseca R., Vabulas R. M., Hartl F. U., Bonhoeffer T. and Nagerl U. V. (2006) A balance of protein synthesis and proteasome-dependent degradation determines the maintenance of LTP. Neuron 52, 239–245.
    • (2006) Neuron , vol.52 , pp. 239-245
    • Fonseca, R.1    Vabulas, R.M.2    Hartl, F.U.3    Bonhoeffer, T.4    Nagerl, U.V.5
  • 41
    • 0031024891 scopus 로고    scopus 로고
    • Synaptic tagging and long-term potentiation
    • Frey U. and Morris R. G. (1997) Synaptic tagging and long-term potentiation. Nature 385, 533–536.
    • (1997) Nature , vol.385 , pp. 533-536
    • Frey, U.1    Morris, R.G.2
  • 44
    • 58149225472 scopus 로고    scopus 로고
    • Microtubules in dendritic spine development
    • Gu J., Firestein B. L. and Zheng J. Q. (2008) Microtubules in dendritic spine development. J. Neurosci. 28, 12120–12124.
    • (2008) J. Neurosci. , vol.28 , pp. 12120-12124
    • Gu, J.1    Firestein, B.L.2    Zheng, J.Q.3
  • 45
    • 37749000849 scopus 로고    scopus 로고
    • Disruption of KIF17-Mint1 interaction by CaMKII-dependent phosphorylation: a molecular model of kinesin-cargo release
    • Guillaud L., Wong R. and Hirokawa N. (2008) Disruption of KIF17-Mint1 interaction by CaMKII-dependent phosphorylation: a molecular model of kinesin-cargo release. Nat. Cell Biol. 10, 19–29.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 19-29
    • Guillaud, L.1    Wong, R.2    Hirokawa, N.3
  • 46
    • 84862777427 scopus 로고    scopus 로고
    • CaMKII binding to GluN2B is critical during memory consolidation
    • Halt A. R., Dallapiazza R. F., Zhou Y. et al. (2012) CaMKII binding to GluN2B is critical during memory consolidation. EMBO J. 31, 1203–1216.
    • (2012) EMBO J. , vol.31 , pp. 1203-1216
    • Halt, A.R.1    Dallapiazza, R.F.2    Zhou, Y.3
  • 48
    • 84892710830 scopus 로고    scopus 로고
    • CaMKII: claiming center stage in postsynaptic function and organization
    • Hell J. W. (2014) CaMKII: claiming center stage in postsynaptic function and organization. Neuron 81, 249–265.
    • (2014) Neuron , vol.81 , pp. 249-265
    • Hell, J.W.1
  • 49
    • 84959386886 scopus 로고    scopus 로고
    • Kalirin and Trio proteins serve critical roles in excitatory synaptic transmission and LTP
    • Herring B. E. and Nicoll R. A. (2016) Kalirin and Trio proteins serve critical roles in excitatory synaptic transmission and LTP. Proc. Natl Acad. Sci. USA 113, 2264–2269.
    • (2016) Proc. Natl Acad. Sci. USA , vol.113 , pp. 2264-2269
    • Herring, B.E.1    Nicoll, R.A.2
  • 50
    • 84920830221 scopus 로고    scopus 로고
    • Stoichiometry and phosphoisotypes of hippocampal AMPA-type glutamate receptor phosphorylation
    • Hosokawa T., Mitsushima D., Kaneko R. and Hayashi Y. (2015) Stoichiometry and phosphoisotypes of hippocampal AMPA-type glutamate receptor phosphorylation. Neuron 85, 60–67.
    • (2015) Neuron , vol.85 , pp. 60-67
    • Hosokawa, T.1    Mitsushima, D.2    Kaneko, R.3    Hayashi, Y.4
  • 51
    • 58149272090 scopus 로고    scopus 로고
    • Activity-dependent dynamic microtubule invasion of dendritic spines
    • Hu X., Viesselmann C., Nam S., Merriam E. and Dent E. W. (2008) Activity-dependent dynamic microtubule invasion of dendritic spines. J. Neurosci. 28, 13094–13105.
    • (2008) J. Neurosci. , vol.28 , pp. 13094-13105
    • Hu, X.1    Viesselmann, C.2    Nam, S.3    Merriam, E.4    Dent, E.W.5
  • 52
    • 84954515218 scopus 로고    scopus 로고
    • CaMKII regulates proteasome phosphorylation and activity and promotes memory destabilization following retrieval
    • Jarome T. J., Ferrara N. C., Kwapis J. L. and Helmstetter F. J. (2016) CaMKII regulates proteasome phosphorylation and activity and promotes memory destabilization following retrieval. Neurobiol. Learn. Mem. 128, 103–109.
    • (2016) Neurobiol. Learn. Mem. , vol.128 , pp. 103-109
    • Jarome, T.J.1    Ferrara, N.C.2    Kwapis, J.L.3    Helmstetter, F.J.4
  • 53
    • 58149214025 scopus 로고    scopus 로고
    • Dynamic microtubules regulate dendritic spine morphology and synaptic plasticity
    • Jaworski J., Kapitein L. C., Gouveia S. M. et al. (2009) Dynamic microtubules regulate dendritic spine morphology and synaptic plasticity. Neuron 61, 85–100.
    • (2009) Neuron , vol.61 , pp. 85-100
    • Jaworski, J.1    Kapitein, L.C.2    Gouveia, S.M.3
  • 54
    • 79960146846 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase IIalpha/beta binding domain in densin that selectively modulates glutamate receptor subunit phosphorylation
    • 2+/calmodulin-dependent protein kinase IIalpha/beta binding domain in densin that selectively modulates glutamate receptor subunit phosphorylation. J. Biol. Chem. 286, 24806–24818.
    • (2011) J. Biol. Chem. , vol.286 , pp. 24806-24818
    • Jiao, Y.1    Jalan-Sakrikar, N.2    Robison, A.J.3    Baucum, A.J.4    Bass, M.A.5    Colbran, R.J.6
  • 56
    • 79958021499 scopus 로고    scopus 로고
    • NMDA receptor activation suppresses microtubule growth and spine entry
    • Kapitein L. C., Yau K. W., Gouveia S. M. et al. (2011) NMDA receptor activation suppresses microtubule growth and spine entry. J. Neurosci. 31, 8194–8209.
    • (2011) J. Neurosci. , vol.31 , pp. 8194-8209
    • Kapitein, L.C.1    Yau, K.W.2    Gouveia, S.M.3
  • 57
    • 0038823489 scopus 로고
    • Biochemical and immunochemical evidence that the “major postsynaptic density protein” is a subunit of a calmodulin-dependent protein kinase
    • Kennedy M. B., Bennett M. K. and Erondu N. E. (1983) Biochemical and immunochemical evidence that the “major postsynaptic density protein” is a subunit of a calmodulin-dependent protein kinase. Proc. Natl Acad. Sci. USA 80, 7357–7361.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 7357-7361
    • Kennedy, M.B.1    Bennett, M.K.2    Erondu, N.E.3
  • 58
    • 84939515157 scopus 로고    scopus 로고
    • A temporary gating of actin remodeling during synaptic plasticity consists of the interplay between the kinase and structural functions of CaMKII
    • Kim K., Lakhanpal G., Lu H. E. et al. (2015) A temporary gating of actin remodeling during synaptic plasticity consists of the interplay between the kinase and structural functions of CaMKII. Neuron 87, 813–826.
    • (2015) Neuron , vol.87 , pp. 813-826
    • Kim, K.1    Lakhanpal, G.2    Lu, H.E.3
  • 59
    • 4143133173 scopus 로고    scopus 로고
    • SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity and NMDA receptor-dependent synaptic AMPA receptor potentiation
    • Krapivinsky G., Medina I., Krapivinsky L., Gapon S. and Clapham D. E. (2004) SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity and NMDA receptor-dependent synaptic AMPA receptor potentiation. Neuron 43, 563–574.
    • (2004) Neuron , vol.43 , pp. 563-574
    • Krapivinsky, G.1    Medina, I.2    Krapivinsky, L.3    Gapon, S.4    Clapham, D.E.5
  • 62
    • 0034702259 scopus 로고    scopus 로고
    • Regulation of distinct AMPA receptor phosphorylation sites during bidirectional synaptic plasticity
    • Lee H. K., Barbarosie M., Kameyama K., Bear M. F. and Huganir R. L. (2000) Regulation of distinct AMPA receptor phosphorylation sites during bidirectional synaptic plasticity. Nature 405, 955–959.
    • (2000) Nature , vol.405 , pp. 955-959
    • Lee, H.K.1    Barbarosie, M.2    Kameyama, K.3    Bear, M.F.4    Huganir, R.L.5
  • 63
    • 0037423916 scopus 로고    scopus 로고
    • Phosphorylation of the AMPA receptor GluR1 subunit is required for synaptic plasticity and retention of spatial memory
    • Lee H. K., Takamiya K., Han J. S. et al. (2003) Phosphorylation of the AMPA receptor GluR1 subunit is required for synaptic plasticity and retention of spatial memory. Cell 112, 631–643.
    • (2003) Cell , vol.112 , pp. 631-643
    • Lee, H.K.1    Takamiya, K.2    Han, J.S.3
  • 64
    • 40049106834 scopus 로고    scopus 로고
    • Synaptic protein degradation underlies destabilization of retrieved fear memory
    • Lee S. H., Choi J. H., Lee N., Lee H. R., Kim J. I., Yu N. K., Choi S. L., Kim H. and Kaang B. K. (2008) Synaptic protein degradation underlies destabilization of retrieved fear memory. Science 319, 1253–1256.
    • (2008) Science , vol.319 , pp. 1253-1256
    • Lee, S.H.1    Choi, J.H.2    Lee, N.3    Lee, H.R.4    Kim, J.I.5    Yu, N.K.6    Choi, S.L.7    Kim, H.8    Kaang, B.K.9
  • 65
    • 62649108345 scopus 로고    scopus 로고
    • Activation of CaMKII in single dendritic spines during long-term potentiation
    • Lee S. J., Escobedo-Lozoya Y., Szatmari E. M. and 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
  • 66
    • 74049162430 scopus 로고    scopus 로고
    • Specific roles of AMPA receptor subunit GluR1 (GluA1) phosphorylation sites in regulating synaptic plasticity in the CA1 region of hippocampus
    • Lee H. K., Takamiya K., He K., Song L. and Huganir R. L. (2010) Specific roles of AMPA receptor subunit GluR1 (GluA1) phosphorylation sites in regulating synaptic plasticity in the CA1 region of hippocampus. J. Neurophysiol. 103, 479–489.
    • (2010) J. Neurophysiol. , vol.103 , pp. 479-489
    • Lee, H.K.1    Takamiya, K.2    He, K.3    Song, L.4    Huganir, R.L.5
  • 67
    • 84869102343 scopus 로고    scopus 로고
    • Translocation of CaMKII to dendritic microtubules supports the plasticity of local synapses
    • Lemieux M., Labrecque S., Tardif C., Labrie-Dion E., Lebel E. and De Koninck P. (2012) Translocation of CaMKII to dendritic microtubules supports the plasticity of local synapses. J. Cell Biol. 198, 1055–1073.
    • (2012) J. Cell Biol. , vol.198 , pp. 1055-1073
    • Lemieux, M.1    Labrecque, S.2    Tardif, C.3    Labrie-Dion, E.4    Lebel, E.5    De Koninck, P.6
  • 68
    • 0033026832 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II is associated with the N-methyl-D-aspartate receptor
    • Leonard A. S., Lim I. A., Hemsworth D. E., Horne M. C. and Hell J. W. (1999) Calcium/calmodulin-dependent protein kinase II is associated with the N-methyl-D-aspartate receptor. Proc. Natl Acad. Sci. USA 96, 3239–3244.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3239-3244
    • Leonard, A.S.1    Lim, I.A.2    Hemsworth, D.E.3    Horne, M.C.4    Hell, J.W.5
  • 69
    • 2242425422 scopus 로고    scopus 로고
    • Regulation of calcium/calmodulin-dependent protein kinase II docking to N-methyl-D-aspartate receptors by calcium/calmodulin and alpha-actinin
    • Leonard A. S., Bayer K. U., Merrill M. A., Lim I. A., Shea M. A., Schulman H. and Hell J. W. (2002) Regulation of calcium/calmodulin-dependent protein kinase II docking to N-methyl-D-aspartate receptors by calcium/calmodulin and alpha-actinin. J. Biol. Chem. 277, 48441–48448.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48441-48448
    • Leonard, A.S.1    Bayer, K.U.2    Merrill, M.A.3    Lim, I.A.4    Shea, M.A.5    Schulman, H.6    Hell, J.W.7
  • 70
    • 57349087691 scopus 로고    scopus 로고
    • CaMKIIβ binding to stable F-actin in vivo regulates F-actin filament stability
    • Lin Y. C. and Redmond L. (2008) CaMKIIβ binding to stable F-actin in vivo regulates F-actin filament stability. Proc. Natl Acad. Sci. USA 105, 15791–15796.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 15791-15796
    • Lin, Y.C.1    Redmond, L.2
  • 72
    • 0010424768 scopus 로고
    • A mechanism for memory storage insensitive to molecular turnover: a bistable autophosphorylating kinase
    • Lisman J. E. (1985) A mechanism for memory storage insensitive to molecular turnover: a bistable autophosphorylating kinase. Proc. Natl Acad. Sci. USA 82, 3055–3057.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 3055-3057
    • Lisman, J.E.1
  • 73
    • 84941600832 scopus 로고    scopus 로고
    • Biochemical principles underlying the stable maintenance of LTP by the CaMKII/NMDAR complex
    • Lisman J. and Raghavachari S. (2015) Biochemical principles underlying the stable maintenance of LTP by the CaMKII/NMDAR complex. Brain Res. 1621, 51–61.
    • (2015) Brain Res. , vol.1621 , pp. 51-61
    • Lisman, J.1    Raghavachari, S.2
  • 74
    • 0036513485 scopus 로고    scopus 로고
    • The molecular basis of CaMKII function in synaptic and behavioural memory
    • Lisman J., Schulman H. and Cline H. (2002) The molecular basis of CaMKII function in synaptic and behavioural memory. Nat. Rev. Neurosci. 3, 175–190.
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 175-190
    • Lisman, J.1    Schulman, H.2    Cline, H.3
  • 75
    • 84857356081 scopus 로고    scopus 로고
    • Mechanisms of CaMKII action in long-term potentiation
    • Lisman J., Yasuda R. and Raghavachari S. (2012) Mechanisms of CaMKII action in long-term potentiation. Nat. Rev. Neurosci. 13, 169–182.
    • (2012) Nat. Rev. Neurosci. , vol.13 , pp. 169-182
    • Lisman, J.1    Yasuda, R.2    Raghavachari, S.3
  • 80
    • 3042554012 scopus 로고    scopus 로고
    • Structural basis of long-term potentiation in single dendritic spines
    • Matsuzaki M., Honkura N., Ellis-Davies G. C. and Kasai H. (2004) Structural basis of long-term potentiation in single dendritic spines. Nature 429, 761–766.
    • (2004) Nature , vol.429 , pp. 761-766
    • Matsuzaki, M.1    Honkura, N.2    Ellis-Davies, G.C.3    Kasai, H.4
  • 81
    • 84863312689 scopus 로고    scopus 로고
    • SynGAP isoforms exert opposing effects on synaptic strength
    • McMahon A. C., Barnett M. W., O'Leary T. S. et al. (2012) SynGAP isoforms exert opposing effects on synaptic strength. Nat. Commun. 3, 900.
    • (2012) Nat. Commun. , vol.3 , pp. 900
    • McMahon, A.C.1    Barnett, M.W.2    O'Leary, T.S.3
  • 85
    • 34848919232 scopus 로고    scopus 로고
    • Sustained Arc/Arg3.1 synthesis controls long-term potentiation consolidation through regulation of local actin polymerization in the dentate gyrus in vivo
    • Messaoudi E., Kanhema T., Soule J., Tiron A., Dagyte G., da Silva B. and Bramham C. R. (2007) Sustained Arc/Arg3.1 synthesis controls long-term potentiation consolidation through regulation of local actin polymerization in the dentate gyrus in vivo. J. Neurosci. 27, 10445–10455.
    • (2007) J. Neurosci. , vol.27 , pp. 10445-10455
    • Messaoudi, E.1    Kanhema, T.2    Soule, J.3    Tiron, A.4    Dagyte, G.5    da Silva, B.6    Bramham, C.R.7
  • 86
    • 84881417751 scopus 로고    scopus 로고
    • The delicate bistability of CaMKII
    • Michalski P. J. (2013) The delicate bistability of CaMKII. Biophys. J. 105, 794–806.
    • (2013) Biophys. J. , vol.105 , pp. 794-806
    • Michalski, P.J.1
  • 87
    • 19344362210 scopus 로고    scopus 로고
    • The stability of a stochastic CaMKII switch: dependence on the number of enzyme molecules and protein turnover
    • Miller P., Zhabotinsky A. M., Lisman J. E. and Wang X. J. (2005) The stability of a stochastic CaMKII switch: dependence on the number of enzyme molecules and protein turnover. PLoS Biol. 3, e107.
    • (2005) PLoS Biol. , vol.3
    • Miller, P.1    Zhabotinsky, A.M.2    Lisman, J.E.3    Wang, X.J.4
  • 88
    • 1642462381 scopus 로고    scopus 로고
    • Activity-regulated cytoskeletal-associated protein is localized to recently activated excitatory synapses
    • Moga D. E., Calhoun M. E., Chowdhury A., Worley P., Morrison J. H. and Shapiro M. L. (2004) Activity-regulated cytoskeletal-associated protein is localized to recently activated excitatory synapses. Neuroscience 125, 7–11.
    • (2004) Neuroscience , vol.125 , pp. 7-11
    • Moga, D.E.1    Calhoun, M.E.2    Chowdhury, A.3    Worley, P.4    Morrison, J.H.5    Shapiro, M.L.6
  • 89
    • 79953748494 scopus 로고    scopus 로고
    • Local, persistent activation of Rho GTPases during plasticity of single dendritic spines
    • Murakoshi H., Wang H. and Yasuda R. (2011) Local, persistent activation of Rho GTPases during plasticity of single dendritic spines. Nature 472, 100–104.
    • (2011) Nature , vol.472 , pp. 100-104
    • Murakoshi, H.1    Wang, H.2    Yasuda, R.3
  • 91
    • 0034661746 scopus 로고    scopus 로고
    • Small GTPases Rac and Rho in the maintenance of dendritic spines and branches in hippocampal pyramidal neurons
    • Nakayama A. Y., Harms M. B. and Luo L. (2000) Small GTPases Rac and Rho in the maintenance of dendritic spines and branches in hippocampal pyramidal neurons. J. Neurosci. 20, 5329–5338.
    • (2000) J. Neurosci. , vol.20 , pp. 5329-5338
    • Nakayama, A.Y.1    Harms, M.B.2    Luo, L.3
  • 93
    • 7044267351 scopus 로고    scopus 로고
    • Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity
    • Okamoto K., Nagai T., Miyawaki A. and Hayashi Y. (2004) Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity. Nat. Neurosci. 7, 1104–1112.
    • (2004) Nat. Neurosci. , vol.7 , pp. 1104-1112
    • Okamoto, K.1    Nagai, T.2    Miyawaki, A.3    Hayashi, Y.4
  • 94
    • 34547523623 scopus 로고    scopus 로고
    • The role of CaMKII as an F-actin-bundling protein crucial for maintenance of dendritic spine structure
    • Okamoto K., Narayanan R., Lee S. H., Murata K. and Hayashi Y. (2007) The role of CaMKII as an F-actin-bundling protein crucial for maintenance of dendritic spine structure. Proc. Natl Acad. Sci. USA 104, 6418–6423.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 6418-6423
    • Okamoto, K.1    Narayanan, R.2    Lee, S.H.3    Murata, K.4    Hayashi, Y.5
  • 95
    • 74049108643 scopus 로고    scopus 로고
    • The roles of CaMKII and F-actin in the structural plasticity of dendritic spines: a potential molecular identity of a synaptic tag?
    • Okamoto K., Bosch M. and Hayashi Y. (2009) The roles of CaMKII and F-actin in the structural plasticity of dendritic spines: a potential molecular identity of a synaptic tag? Physiology (Bethesda) 24, 357–366.
    • (2009) Physiology (Bethesda) , vol.24 , pp. 357-366
    • Okamoto, K.1    Bosch, M.2    Hayashi, Y.3
  • 96
    • 84860871082 scopus 로고    scopus 로고
    • Inverse synaptic tagging of inactive synapses via dynamic interaction of Arc/Arg3.1 with CaMKIIbeta
    • Okuno H., Akashi K., Ishii Y. et al. (2012) Inverse synaptic tagging of inactive synapses via dynamic interaction of Arc/Arg3.1 with CaMKIIbeta. Cell 149, 886–898.
    • (2012) Cell , vol.149 , pp. 886-898
    • Okuno, H.1    Akashi, K.2    Ishii, Y.3
  • 97
    • 77955478311 scopus 로고    scopus 로고
    • CaMKII triggers the diffusional trapping of surface AMPARs through phosphorylation of stargazin
    • Opazo P., Labrecque S., Tigaret C. M., Frouin A., Wiseman P. W., De Koninck P. and Choquet D. (2010) CaMKII triggers the diffusional trapping of surface AMPARs through phosphorylation of stargazin. Neuron 67, 239–252.
    • (2010) Neuron , vol.67 , pp. 239-252
    • Opazo, P.1    Labrecque, S.2    Tigaret, C.M.3    Frouin, A.4    Wiseman, P.W.5    De Koninck, P.6    Choquet, D.7
  • 98
    • 7044270772 scopus 로고    scopus 로고
    • Persistent accumulation of calcium/calmodulin-dependent protein kinase II in dendritic spines after induction of NMDA receptor-dependent chemical long-term potentiation
    • Otmakhov N., Tao-Cheng J. H., Carpenter S., Asrican B., Dosemeci A., Reese T. S. and Lisman J. (2004) Persistent accumulation of calcium/calmodulin-dependent protein kinase II in dendritic spines after induction of NMDA receptor-dependent chemical long-term potentiation. J. Neurosci. 24, 9324–9331.
    • (2004) J. Neurosci. , vol.24 , pp. 9324-9331
    • Otmakhov, N.1    Tao-Cheng, J.H.2    Carpenter, S.3    Asrican, B.4    Dosemeci, A.5    Reese, T.S.6    Lisman, J.7
  • 99
    • 84939196271 scopus 로고    scopus 로고
    • Fast decay of CaMKII FRET sensor signal in spines after LTP induction Is not due to its dephosphorylation
    • Otmakhov N., Regmi S. and Lisman J. E. (2015) Fast decay of CaMKII FRET sensor signal in spines after LTP induction Is not due to its dephosphorylation. PLoS ONE 10, e0130457.
    • (2015) PLoS ONE , vol.10
    • Otmakhov, N.1    Regmi, S.2    Lisman, J.E.3
  • 100
    • 16944366067 scopus 로고    scopus 로고
    • Visualization of the distribution of autophosphorylated calcium/calmodulin-dependent protein kinase II after tetanic stimulation in the CA1 area of the hippocampus
    • Ouyang Y., Kantor D., Harris K. M., Schuman E. M. and Kennedy M. B. (1997) Visualization of the distribution of autophosphorylated calcium/calmodulin-dependent protein kinase II after tetanic stimulation in the CA1 area of the hippocampus. J. Neurosci. 17, 5416–5427.
    • (1997) J. Neurosci. , vol.17 , pp. 5416-5427
    • Ouyang, Y.1    Kantor, D.2    Harris, K.M.3    Schuman, E.M.4    Kennedy, M.B.5
  • 101
    • 84878254691 scopus 로고    scopus 로고
    • NMDA receptor subunit diversity: impact on receptor properties, synaptic plasticity and disease
    • Paoletti P., Bellone C. and Zhou Q. (2013) NMDA receptor subunit diversity: impact on receptor properties, synaptic plasticity and disease. Nat. Rev. Neurosci. 14, 383–400.
    • (2013) Nat. Rev. Neurosci. , vol.14 , pp. 383-400
    • Paoletti, P.1    Bellone, C.2    Zhou, Q.3
  • 102
    • 46149087988 scopus 로고    scopus 로고
    • Elongation factor 2 and fragile X mental retardation protein control the dynamic translation of Arc/Arg3.1 essential for mGluR-LTD
    • Park S., Park J. M., Kim S. et al. (2008) Elongation factor 2 and fragile X mental retardation protein control the dynamic translation of Arc/Arg3.1 essential for mGluR-LTD. Neuron 59, 70–83.
    • (2008) Neuron , vol.59 , pp. 70-83
    • Park, S.1    Park, J.M.2    Kim, S.3
  • 103
    • 2442683994 scopus 로고    scopus 로고
    • Semiquantitative proteomic analysis of rat forebrain postsynaptic density fractions by mass spectrometry
    • Peng J., Kim M. J., Cheng D., Duong D. M., Gygi S. P. and Sheng M. (2004) Semiquantitative proteomic analysis of rat forebrain postsynaptic density fractions by mass spectrometry. J. Biol. Chem. 279, 21003–21011.
    • (2004) J. Biol. Chem. , vol.279 , pp. 21003-21011
    • Peng, J.1    Kim, M.J.2    Cheng, D.3    Duong, D.M.4    Gygi, S.P.5    Sheng, M.6
  • 104
    • 0028579743 scopus 로고
    • Potentiated transmission and prevention of further LTP by increased CaMKII activity in postsynaptic hippocampal slice neurons
    • Pettit D. L., Perlman S. and Malinow R. (1994) Potentiated transmission and prevention of further LTP by increased CaMKII activity in postsynaptic hippocampal slice neurons. Science 266, 1881–1885.
    • (1994) Science , vol.266 , pp. 1881-1885
    • Pettit, D.L.1    Perlman, S.2    Malinow, R.3
  • 105
    • 33750496896 scopus 로고    scopus 로고
    • Arc/Arg3.1 is essential for the consolidation of synaptic plasticity and memories
    • Plath N., Ohana O., Dammermann B. et al. (2006) Arc/Arg3.1 is essential for the consolidation of synaptic plasticity and memories. Neuron 52, 437–444.
    • (2006) Neuron , vol.52 , pp. 437-444
    • Plath, N.1    Ohana, O.2    Dammermann, B.3
  • 107
    • 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
    • Robison A. J., Bass M. A., Jiao Y., MacMillan L. B., Carmody L. C., Bartlett R. K. and Colbran R. J. (2005) Multivalent interactions of calcium/calmodulin-dependent protein kinase II with the postsynaptic density proteins NR2B, densin-180, and α-actinin-2. J. Biol. Chem. 280, 35329–35336.
    • (2005) J. Biol. Chem. , vol.280 , 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
  • 108
    • 28344445756 scopus 로고    scopus 로고
    • Structure of the autoinhibited kinase domain of CaMKII and SAXS analysis of the holoenzyme
    • Rosenberg O. S., Deindl S., Sung R. J., Nairn A. C. and Kuriyan J. (2005) Structure of the autoinhibited kinase domain of CaMKII and SAXS analysis of the holoenzyme. Cell 123, 849–860.
    • (2005) Cell , vol.123 , pp. 849-860
    • Rosenberg, O.S.1    Deindl, S.2    Sung, R.J.3    Nairn, A.C.4    Kuriyan, J.5
  • 109
    • 33645217296 scopus 로고    scopus 로고
    • SynGAP regulates synaptic strength and mitogen-activated protein kinases in cultured neurons
    • Rumbaugh G., Adams J. P., Kim J. H. and Huganir R. L. (2006) SynGAP regulates synaptic strength and mitogen-activated protein kinases in cultured neurons. Proc. Natl Acad. Sci. USA 103, 4344–4351.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 4344-4351
    • Rumbaugh, G.1    Adams, J.P.2    Kim, J.H.3    Huganir, R.L.4
  • 110
    • 21544454679 scopus 로고    scopus 로고
    • The Rho-specific GEF Lfc interacts with neurabin and spinophilin to regulate dendritic spine morphology
    • Ryan X. P., Alldritt J., Svenningsson P., Allen P. B., Wu G. Y., Nairn A. C. and Greengard P. (2005) The Rho-specific GEF Lfc interacts with neurabin and spinophilin to regulate dendritic spine morphology. Neuron 47, 85–100.
    • (2005) Neuron , vol.47 , pp. 85-100
    • Ryan, X.P.1    Alldritt, J.2    Svenningsson, P.3    Allen, P.B.4    Wu, G.Y.5    Nairn, A.C.6    Greengard, P.7
  • 111
    • 84865330853 scopus 로고    scopus 로고
    • 2+ and Rho GTPase signaling pathways underlying activity-dependent actin remodeling at dendritic spines
    • 2+ and Rho GTPase signaling pathways underlying activity-dependent actin remodeling at dendritic spines. Cytoskeleton (Hoboken) 69, 545–554.
    • (2012) Cytoskeleton (Hoboken) , vol.69 , pp. 545-554
    • Saneyoshi, T.1    Hayashi, Y.2
  • 112
    • 84873604107 scopus 로고    scopus 로고
    • The CaMKII/NMDAR complex as a molecular memory
    • Sanhueza M. and Lisman J. (2013) The CaMKII/NMDAR complex as a molecular memory. Mol. Brain 6, 10.
    • (2013) Mol. Brain , vol.6 , pp. 10
    • Sanhueza, M.1    Lisman, J.2
  • 114
    • 77956998216 scopus 로고    scopus 로고
    • Casein kinase 2 regulates the NR2 subunit composition of synaptic NMDA receptors
    • Sanz-Clemente A., Matta J. A., Isaac J. T. and Roche K. W. (2010) Casein kinase 2 regulates the NR2 subunit composition of synaptic NMDA receptors. Neuron 67, 984–996.
    • (2010) Neuron , vol.67 , pp. 984-996
    • Sanz-Clemente, A.1    Matta, J.A.2    Isaac, J.T.3    Roche, K.W.4
  • 115
    • 84875808267 scopus 로고    scopus 로고
    • Activated CaMKII couples GluN2B and casein kinase 2 to control synaptic NMDA receptors
    • Sanz-Clemente A., Gray J. A., Ogilvie K. A., Nicoll R. A. and Roche K. W. (2013) Activated CaMKII couples GluN2B and casein kinase 2 to control synaptic NMDA receptors. Cell Rep. 3, 607–614.
    • (2013) Cell Rep. , vol.3 , pp. 607-614
    • Sanz-Clemente, A.1    Gray, J.A.2    Ogilvie, K.A.3    Nicoll, R.A.4    Roche, K.W.5
  • 116
    • 0037884921 scopus 로고    scopus 로고
    • Small GTPase Cdc42 is required for multiple aspects of dendritic morphogenesis
    • Scott E. K., Reuter J. E. and Luo L. (2003) Small GTPase Cdc42 is required for multiple aspects of dendritic morphogenesis. J. Neurosci. 23, 3118–3123.
    • (2003) J. Neurosci. , vol.23 , pp. 3118-3123
    • Scott, E.K.1    Reuter, J.E.2    Luo, L.3
  • 117
    • 0034625631 scopus 로고    scopus 로고
    • Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport
    • Setou M., Nakagawa T., Seog D. H. and Hirokawa N. (2000) Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport. Science 288, 1796–1802.
    • (2000) Science , vol.288 , pp. 1796-1802
    • Setou, M.1    Nakagawa, T.2    Seog, D.H.3    Hirokawa, N.4
  • 118
    • 0033515884 scopus 로고    scopus 로고
    • Dynamic control of CaMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation
    • Shen K. and Meyer T. (1999) Dynamic control of CaMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation. Science 284, 162–166.
    • (1999) Science , vol.284 , pp. 162-166
    • Shen, K.1    Meyer, T.2
  • 119
    • 0033860922 scopus 로고    scopus 로고
    • Molecular memory by reversible translocation of calcium/calmodulin-dependent protein kinase II
    • Shen K., Teruel M. N., Connor J. H., Shenolikar S. and Meyer T. (2000) Molecular memory by reversible translocation of calcium/calmodulin-dependent protein kinase II. Nat. Neurosci. 3, 881–886.
    • (2000) Nat. Neurosci. , vol.3 , pp. 881-886
    • Shen, K.1    Teruel, M.N.2    Connor, J.H.3    Shenolikar, S.4    Meyer, T.5
  • 120
    • 34548436564 scopus 로고    scopus 로고
    • The postsynaptic architecture of excitatory synapses: a more quantitative view
    • Sheng M. and Hoogenraad C. C. (2007) The postsynaptic architecture of excitatory synapses: a more quantitative view. Annu. Rev. Biochem. 76, 823–847.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 823-847
    • Sheng, M.1    Hoogenraad, C.C.2
  • 122
    • 0026637195 scopus 로고
    • Deficient hippocampal long-term potentiation in alpha-calcium-calmodulin kinase II mutant mice
    • Silva A. J., Stevens C. F., Tonegawa S. and Wang Y. (1992) Deficient hippocampal long-term potentiation in alpha-calcium-calmodulin kinase II mutant mice. Science 257, 201–206.
    • (1992) Science , vol.257 , pp. 201-206
    • Silva, A.J.1    Stevens, C.F.2    Tonegawa, S.3    Wang, Y.4
  • 123
    • 77956188753 scopus 로고    scopus 로고
    • SRF binding to SRE 6.9 in the Arc promoter is essential for LTD in cultured Purkinje cells
    • Smith-Hicks C., Xiao B., Deng R. et al. (2010) SRF binding to SRE 6.9 in the Arc promoter is essential for LTD in cultured Purkinje cells. Nat. Neurosci. 13, 1082–1089.
    • (2010) Nat. Neurosci. , vol.13 , pp. 1082-1089
    • Smith-Hicks, C.1    Xiao, B.2    Deng, R.3
  • 124
    • 0032191909 scopus 로고    scopus 로고
    • Synaptic activation causes the mRNA for the IEG Arc to localize selectively near activated postsynaptic sites on dendrites
    • Steward O., Wallace C. S., Lyford G. L. and Worley P. F. (1998) Synaptic activation causes the mRNA for the IEG Arc to localize selectively near activated postsynaptic sites on dendrites. Neuron 21, 741–751.
    • (1998) Neuron , vol.21 , pp. 741-751
    • Steward, O.1    Wallace, C.S.2    Lyford, G.L.3    Worley, P.F.4
  • 125
    • 0032516819 scopus 로고    scopus 로고
    • Autophosphorylation-dependent targeting of calcium/calmodulin-dependent protein kinase II by the NR2B subunit of the N-methyl- D-aspartate receptor
    • Strack S. and Colbran R. J. (1998) Autophosphorylation-dependent targeting of calcium/calmodulin-dependent protein kinase II by the NR2B subunit of the N-methyl- D-aspartate receptor. J. Biol. Chem. 273, 20689–20692.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20689-20692
    • Strack, S.1    Colbran, R.J.2
  • 126
    • 0034682735 scopus 로고    scopus 로고
    • Association of calcium/calmodulin-dependent kinase II with developmentally regulated splice variants of the postsynaptic density protein densin-180
    • Strack S., Robison A. J., Bass M. A. and Colbran R. J. (2000) Association of calcium/calmodulin-dependent kinase II with developmentally regulated splice variants of the postsynaptic density protein densin-180. J. Biol. Chem. 275, 25061–25064.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25061-25064
    • Strack, S.1    Robison, A.J.2    Bass, M.A.3    Colbran, R.J.4
  • 127
    • 77953658109 scopus 로고    scopus 로고
    • TARP phosphorylation regulates synaptic AMPA receptors through lipid bilayers
    • Sumioka A., Yan D. and Tomita S. (2010) TARP phosphorylation regulates synaptic AMPA receptors through lipid bilayers. Neuron 66, 755–767.
    • (2010) Neuron , vol.66 , pp. 755-767
    • Sumioka, A.1    Yan, D.2    Tomita, S.3
  • 129
    • 0033807686 scopus 로고    scopus 로고
    • Regulation of dendritic spine morphology by the rho family of small GTPases: antagonistic roles of Rac and Rho
    • Tashiro A., Minden A. and Yuste R. (2000) Regulation of dendritic spine morphology by the rho family of small GTPases: antagonistic roles of Rac and Rho. Cereb. Cortex 10, 927–938.
    • (2000) Cereb. Cortex , vol.10 , pp. 927-938
    • Tashiro, A.1    Minden, A.2    Yuste, R.3
  • 130
    • 0037137469 scopus 로고    scopus 로고
    • alpha- and betaCaMKII. Inverse regulation by neuronal activity and opposing effects on synaptic strength
    • Thiagarajan T. C., Piedras-Renteria E. S. and Tsien R. W. (2002) alpha- and betaCaMKII. Inverse regulation by neuronal activity and opposing effects on synaptic strength. Neuron 36, 1103–1114.
    • (2002) Neuron , vol.36 , pp. 1103-1114
    • Thiagarajan, T.C.1    Piedras-Renteria, E.S.2    Tsien, R.W.3
  • 131
    • 84896511826 scopus 로고    scopus 로고
    • In vitro reconstitution of a CaMKII memory switch by an NMDA receptor-derived peptide
    • Urakubo H., Sato M., Ishii S. and Kuroda S. (2014) In vitro reconstitution of a CaMKII memory switch by an NMDA receptor-derived peptide. Biophys. J. 106, 1414–1420.
    • (2014) Biophys. J. , vol.106 , pp. 1414-1420
    • Urakubo, H.1    Sato, M.2    Ishii, S.3    Kuroda, S.4
  • 135
    • 46149123205 scopus 로고    scopus 로고
    • Rapid translation of Arc/Arg3.1 selectively mediates mGluR-dependent LTD through persistent increases in AMPAR endocytosis rate
    • Waung M. W., Pfeiffer B. E., Nosyreva E. D., Ronesi J. A. and Huber K. M. (2008) Rapid translation of Arc/Arg3.1 selectively mediates mGluR-dependent LTD through persistent increases in AMPAR endocytosis rate. Neuron 59, 84–97.
    • (2008) Neuron , vol.59 , pp. 84-97
    • Waung, M.W.1    Pfeiffer, B.E.2    Nosyreva, E.D.3    Ronesi, J.A.4    Huber, K.M.5
  • 136
    • 52049121528 scopus 로고    scopus 로고
    • Calmodulin-kinases: modulators of neuronal development and plasticity
    • Wayman G. A., Lee Y. S., Tokumitsu H., Silva A. J. and Soderling T. R. (2008) Calmodulin-kinases: modulators of neuronal development and plasticity. Neuron 59, 914–931.
    • (2008) Neuron , vol.59 , pp. 914-931
    • Wayman, G.A.1    Lee, Y.S.2    Tokumitsu, H.3    Silva, A.J.4    Soderling, T.R.5
  • 137
    • 0345701252 scopus 로고    scopus 로고
    • Derangements of hippocampal calcium/calmodulin-dependent protein kinase II in a mouse model for Angelman mental retardation syndrome
    • Weeber E. J., Jiang Y. H., Elgersma Y. et al. (2003) Derangements of hippocampal calcium/calmodulin-dependent protein kinase II in a mouse model for Angelman mental retardation syndrome. J. Neurosci. 23, 2634–2644.
    • (2003) J. Neurosci. , vol.23 , pp. 2634-2644
    • Weeber, E.J.1    Jiang, Y.H.2    Elgersma, Y.3
  • 138
    • 0037195134 scopus 로고    scopus 로고
    • Overexpression of motor protein KIF17 enhances spatial and working memory in transgenic mice
    • Wong R. W., Setou M., Teng J., Takei Y. and Hirokawa N. (2002) Overexpression of motor protein KIF17 enhances spatial and working memory in transgenic mice. Proc. Natl Acad. Sci. USA 99, 14500–14505.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 14500-14505
    • Wong, R.W.1    Setou, M.2    Teng, J.3    Takei, Y.4    Hirokawa, N.5
  • 141
    • 0032142987 scopus 로고    scopus 로고
    • Calmodulin mediates calcium-dependent inactivation of N-methyl-D-aspartate receptors
    • Zhang S., Ehlers M. D., Bernhardt J. P., Su C. T. and Huganir R. L. (1998) Calmodulin mediates calcium-dependent inactivation of N-methyl-D-aspartate receptors. Neuron 21, 443–453.
    • (1998) Neuron , vol.21 , pp. 443-453
    • Zhang, S.1    Ehlers, M.D.2    Bernhardt, J.P.3    Su, C.T.4    Huganir, R.L.5
  • 142
    • 37249033631 scopus 로고    scopus 로고
    • Interactions between the NR2B receptor and CaMKII modulate synaptic plasticity and spatial learning
    • Zhou Y., Takahashi E., Li W. et al. (2007) Interactions between the NR2B receptor and CaMKII modulate synaptic plasticity and spatial learning. J. Neurosci. 27, 13843–13853.
    • (2007) J. Neurosci. , vol.27 , pp. 13843-13853
    • Zhou, Y.1    Takahashi, E.2    Li, W.3
  • 143
    • 0037162696 scopus 로고    scopus 로고
    • Ras and Rap control AMPA receptor trafficking during synaptic plasticity
    • Zhu J. J., Qin Y., Zhao M., Van Aelst L. and Malinow R. (2002) Ras and Rap control AMPA receptor trafficking during synaptic plasticity. Cell 110, 443–455.
    • (2002) Cell , vol.110 , pp. 443-455
    • Zhu, J.J.1    Qin, Y.2    Zhao, M.3    Van Aelst, L.4    Malinow, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.