메뉴 건너뛰기




Volumn 51, Issue 2-4 SPEC. ISS., 2007, Pages 92-104

Role of actin cytoskeleton in dendritic spine morphogenesis

Author keywords

Actin; Actin binding protein; Actin myosin interaction; Drebrin; Spine formation; Spine morphology; Synaptic activity

Indexed keywords

ACTIN; ADDUCIN; DREBRIN; F ACTIN; FASCIN; G ACTIN; GELSOLIN; GLUTAMATE RECEPTOR; GUANOSINE TRIPHOSPHATASE; MYOSIN; MYOSIN II; PROFILIN; SPINOPHILIN;

EID: 34547488455     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuint.2007.04.029     Document Type: Review
Times cited : (248)

References (160)
  • 1
    • 0025222971 scopus 로고
    • Effect of calponin on actin-activated myosin ATPase activity
    • Abe M., Takahashi K., and Hiwada K. Effect of calponin on actin-activated myosin ATPase activity. J. Biochem. (Tokyo) 108 (1990) 835-838
    • (1990) J. Biochem. (Tokyo) , vol.108 , pp. 835-838
    • Abe, M.1    Takahashi, K.2    Hiwada, K.3
  • 2
    • 0242384720 scopus 로고    scopus 로고
    • Activity-induced targeting of profilin and stabilization of dendritic spine morphology
    • Ackermann M., and Matus A. Activity-induced targeting of profilin and stabilization of dendritic spine morphology. Nat. Neurosci. 6 (2003) 1194-1200
    • (2003) Nat. Neurosci. , vol.6 , pp. 1194-1200
    • Ackermann, M.1    Matus, A.2
  • 5
    • 0030922920 scopus 로고    scopus 로고
    • Spinophilin, a novel protein phosphatase 1 binding protein localized to dendritic spines
    • Allen P.B., Ouimet C.C., and Greengard P. Spinophilin, a novel protein phosphatase 1 binding protein localized to dendritic spines. Proc. Natl. Acad. Sci. U.S.A. 94 (1997) 9956-9961
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 9956-9961
    • Allen, P.B.1    Ouimet, C.C.2    Greengard, P.3
  • 6
    • 0032054473 scopus 로고    scopus 로고
    • Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: differential attachment of NMDA versus AMPA receptors
    • Allison D.W., Gelfand V.I., Spector I., and Craig A.M. Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: differential attachment of NMDA versus AMPA receptors. J. Neurosci. 18 (1998) 2423-2436
    • (1998) J. Neurosci. , vol.18 , pp. 2423-2436
    • Allison, D.W.1    Gelfand, V.I.2    Spector, I.3    Craig, A.M.4
  • 7
    • 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 D.W., Chervin A.S., Gelfand V.I., and Craig A.M. Postsynaptic scaffolds of excitatory and inhibitory synapses in hippocampal neurons: maintenance of core components independent of actin filaments and microtubules. J. Neurosci. 20 (2000) 4545-4554
    • (2000) J. Neurosci. , vol.20 , pp. 4545-4554
    • Allison, D.W.1    Chervin, A.S.2    Gelfand, V.I.3    Craig, A.M.4
  • 8
    • 14644401845 scopus 로고    scopus 로고
    • Drebrin A is a postsynaptic protein that localizes in vivo to the submembranous surface of dendritic sites forming excitatory synapses
    • Aoki C., Sekino Y., Hanamura K., Fujisawa S., Mahadomrongkul V., Ren Y., and Shirao T. Drebrin A is a postsynaptic protein that localizes in vivo to the submembranous surface of dendritic sites forming excitatory synapses. J. Comp. Neurol. 483 (2005) 383-402
    • (2005) J. Comp. Neurol. , vol.483 , pp. 383-402
    • Aoki, C.1    Sekino, Y.2    Hanamura, K.3    Fujisawa, S.4    Mahadomrongkul, V.5    Ren, Y.6    Shirao, T.7
  • 9
    • 0019170917 scopus 로고
    • Partial purification and characterization of an actin depolymerizing factor from brain
    • Bamburg J.R., Harris H.E., and Weeds A.G. Partial purification and characterization of an actin depolymerizing factor from brain. FEBS Lett. 121 (1980) 178-182
    • (1980) FEBS Lett. , vol.121 , pp. 178-182
    • Bamburg, J.R.1    Harris, H.E.2    Weeds, A.G.3
  • 11
    • 0842269066 scopus 로고    scopus 로고
    • Myosin-dependent transport in neurons
    • Bridgman P.C. Myosin-dependent transport in neurons. J. Neurobiol. 58 (2004) 164-174
    • (2004) J. Neurobiol. , vol.58 , pp. 164-174
    • Bridgman, P.C.1
  • 12
    • 0018068395 scopus 로고
    • Separation and interaction of the major components of sea urchin actin gel
    • Bryan J., and Kane R.E. Separation and interaction of the major components of sea urchin actin gel. J. Mol. Biol. 125 (1978) 207-224
    • (1978) J. Mol. Biol. , vol.125 , pp. 207-224
    • Bryan, J.1    Kane, R.E.2
  • 13
    • 1942445036 scopus 로고    scopus 로고
    • Drebrin is a novel connexin-43 binding partner that links gap junctions to the submembrane cytoskeleton
    • Butkevich E., Hulsmann S., Wenzel D., Shirao T., Duden R., and Majoul I. Drebrin is a novel connexin-43 binding partner that links gap junctions to the submembrane cytoskeleton. Curr. Biol. 14 (2004) 650-658
    • (2004) Curr. Biol. , vol.14 , pp. 650-658
    • Butkevich, E.1    Hulsmann, S.2    Wenzel, D.3    Shirao, T.4    Duden, R.5    Majoul, I.6
  • 15
    • 0031580210 scopus 로고    scopus 로고
    • Control of actin dynamics in cell motility
    • Carlier M.F., and Pantaloni D. Control of actin dynamics in cell motility. J. Mol. Biol. 269 (1997) 459-467
    • (1997) J. Mol. Biol. , vol.269 , pp. 459-467
    • Carlier, M.F.1    Pantaloni, D.2
  • 16
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility
    • Carlier M.F., Laurent V., Santolini J., Melki R., Didry D., Xia G.X., Hong Y., Chua N.H., and Pantaloni D. Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J. Cell Biol. 136 (1997) 1307-1322
    • (1997) J. Cell Biol. , vol.136 , pp. 1307-1322
    • Carlier, M.F.1    Laurent, V.2    Santolini, J.3    Melki, R.4    Didry, D.5    Xia, G.X.6    Hong, Y.7    Chua, N.H.8    Pantaloni, D.9
  • 17
    • 84886632310 scopus 로고
    • Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells
    • Carlsson L., Nystrom L.E., Sundkvist I., Markey F., and Lindberg U. Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells. J. Mol. Biol. 115 (1977) 465-483
    • (1977) J. Mol. Biol. , vol.115 , pp. 465-483
    • Carlsson, L.1    Nystrom, L.E.2    Sundkvist, I.3    Markey, F.4    Lindberg, U.5
  • 18
    • 0033983608 scopus 로고    scopus 로고
    • Non-muscle myosin IIB-like immunoreactivity is present at the drebrin-binding cytoskeleton in neurons
    • Cheng X.T., Hayashi K., and Shirao T. Non-muscle myosin IIB-like immunoreactivity is present at the drebrin-binding cytoskeleton in neurons. Neurosci. Res. 36 (2000) 167-173
    • (2000) Neurosci. Res. , vol.36 , pp. 167-173
    • Cheng, X.T.1    Hayashi, K.2    Shirao, T.3
  • 19
    • 0026492629 scopus 로고
    • The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein
    • Cho K.O., Hunt C.A., and Kennedy M.B. The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein. Neuron 9 (1992) 929-942
    • (1992) Neuron , vol.9 , pp. 929-942
    • Cho, K.O.1    Hunt, C.A.2    Kennedy, M.B.3
  • 20
    • 0015898799 scopus 로고
    • Actin-linked regulation of the human platelet contractile system
    • Cohen I., Kaminski E., and De Vries A. Actin-linked regulation of the human platelet contractile system. FEBS Lett. 34 (1973) 315-317
    • (1973) FEBS Lett. , vol.34 , pp. 315-317
    • Cohen, I.1    Kaminski, E.2    De Vries, A.3
  • 21
    • 0022119267 scopus 로고
    • Immunocytochemical localization of actin in dendritic spines of the cerebral cortex using colloidal gold as a probe
    • Cohen R.S., Chung S.K., and Pfaff D.W. Immunocytochemical localization of actin in dendritic spines of the cerebral cortex using colloidal gold as a probe. Cell. Mol. Neurobiol. 5 (1985) 271-284
    • (1985) Cell. Mol. Neurobiol. , vol.5 , pp. 271-284
    • Cohen, R.S.1    Chung, S.K.2    Pfaff, D.W.3
  • 22
    • 33746752209 scopus 로고    scopus 로고
    • Differential expression of synaptic proteins in the frontal and temporal cortex of elderly subjects with mild cognitive impairment
    • Counts S.E., Nadeem M., Lad S.P., Wuu J., and Mufson E.J. Differential expression of synaptic proteins in the frontal and temporal cortex of elderly subjects with mild cognitive impairment. J. Neuropathol. Exp. Neurol. 65 (2006) 592-601
    • (2006) J. Neuropathol. Exp. Neurol. , vol.65 , pp. 592-601
    • Counts, S.E.1    Nadeem, M.2    Lad, S.P.3    Wuu, J.4    Mufson, E.J.5
  • 23
    • 0029998871 scopus 로고    scopus 로고
    • The dynamics of dendritic structure in developing hippocampal slices
    • Dailey M.E., and Smith S.J. The dynamics of dendritic structure in developing hippocampal slices. J. Neurosci. 16 (1996) 2983-2994
    • (1996) J. Neurosci. , vol.16 , pp. 2983-2994
    • Dailey, M.E.1    Smith, S.J.2
  • 24
  • 25
    • 0014396206 scopus 로고
    • Calcium ion and muscle contraction
    • Ebashi S., and Endo M. Calcium ion and muscle contraction. Prog. Biophys. Mol. Biol. 18 (1968) 123-183
    • (1968) Prog. Biophys. Mol. Biol. , vol.18 , pp. 123-183
    • Ebashi, S.1    Endo, M.2
  • 26
    • 0033627645 scopus 로고    scopus 로고
    • Models for spatial polymerization dynamics of rod-like polymers
    • Edelstein-Keshet L., and Ermentrout G.B. Models for spatial polymerization dynamics of rod-like polymers. J. Math. Biol. 40 (2000) 64-96
    • (2000) J. Math. Biol. , vol.40 , pp. 64-96
    • Edelstein-Keshet, L.1    Ermentrout, G.B.2
  • 27
    • 0028799146 scopus 로고
    • Fascins, a family of actin bundling proteins
    • Edwards R.A., and Bryan J. Fascins, a family of actin bundling proteins. Cell Motil. Cytoskeleton 32 (1995) 1-9
    • (1995) Cell Motil. Cytoskeleton , vol.32 , pp. 1-9
    • Edwards, R.A.1    Bryan, J.2
  • 28
    • 18844403842 scopus 로고    scopus 로고
    • Molecular mechanisms of dendritic spine development and remodeling
    • Ethell I.M., and Pasquale E.B. Molecular mechanisms of dendritic spine development and remodeling. Prog. Neurobiol. 75 (2005) 161-205
    • (2005) Prog. Neurobiol. , vol.75 , pp. 161-205
    • Ethell, I.M.1    Pasquale, E.B.2
  • 30
    • 0242456122 scopus 로고    scopus 로고
    • Increased levels of acidic calponin during dendritic spine plasticity after pilocarpine-induced seizures
    • Ferhat L., Esclapez M., Represa A., Fattoum A., Shirao T., and Ben-Ari Y. Increased levels of acidic calponin during dendritic spine plasticity after pilocarpine-induced seizures. Hippocampus 13 (2003) 845-858
    • (2003) Hippocampus , vol.13 , pp. 845-858
    • Ferhat, L.1    Esclapez, M.2    Represa, A.3    Fattoum, A.4    Shirao, T.5    Ben-Ari, Y.6
  • 31
    • 0032211079 scopus 로고    scopus 로고
    • Synaptogenesis via dendritic filopodia in developing hippocampal area CA1
    • Fiala J.C., Feinberg M., Popov V., and Harris K.M. Synaptogenesis via dendritic filopodia in developing hippocampal area CA1. J. Neurosci. 18 (1998) 8900-8911
    • (1998) J. Neurosci. , vol.18 , pp. 8900-8911
    • Fiala, J.C.1    Feinberg, M.2    Popov, V.3    Harris, K.M.4
  • 32
    • 0032078861 scopus 로고    scopus 로고
    • Rapid actin-based plasticity in dendritic spines
    • Fischer M., Kaech S., Knutti D., and Matus A. Rapid actin-based plasticity in dendritic spines. Neuron 20 (1998) 847-854
    • (1998) Neuron , vol.20 , pp. 847-854
    • Fischer, M.1    Kaech, S.2    Knutti, D.3    Matus, A.4
  • 33
    • 0033855708 scopus 로고    scopus 로고
    • Glutamate receptors regulate actin-based plasticity in dendritic spines
    • Fischer M., Kaech S., Wagner U., Brinkhaus H., and Matus A. Glutamate receptors regulate actin-based plasticity in dendritic spines. Nat. Neurosci. 3 (2000) 887-894
    • (2000) Nat. Neurosci. , vol.3 , pp. 887-894
    • Fischer, M.1    Kaech, S.2    Wagner, U.3    Brinkhaus, H.4    Matus, A.5
  • 34
    • 0033666317 scopus 로고    scopus 로고
    • Assembly of new individual excitatory synapses: time course and temporal order of synaptic molecule recruitment
    • Friedman H.V., Bresler T., Garner C.C., and Ziv N.E. Assembly of new individual excitatory synapses: time course and temporal order of synaptic molecule recruitment. Neuron 27 (2000) 57-69
    • (2000) Neuron , vol.27 , pp. 57-69
    • Friedman, H.V.1    Bresler, T.2    Garner, C.C.3    Ziv, N.E.4
  • 35
    • 33745285358 scopus 로고    scopus 로고
    • In vivo, competitive blockade of n-methyl-d-aspartate receptors induces rapid changes in filamentous actin and drebrin a distributions within dendritic spines of adult rat cortex
    • Fujisawa S., Shirao T., and Aoki C. In vivo, competitive blockade of n-methyl-d-aspartate receptors induces rapid changes in filamentous actin and drebrin a distributions within dendritic spines of adult rat cortex. Neuroscience 140 (2006) 1177-1187
    • (2006) Neuroscience , vol.140 , pp. 1177-1187
    • Fujisawa, S.1    Shirao, T.2    Aoki, C.3
  • 36
    • 0038662761 scopus 로고    scopus 로고
    • Hippocampal LTP is accompanied by enhanced F-actin content within the dendritic spine that is essential for late LTP maintenance in vivo
    • Fukazawa Y., Saitoh Y., Ozawa F., Ohta Y., Mizuno K., and Inokuchi K. Hippocampal LTP is accompanied by enhanced F-actin content within the dendritic spine that is essential for late LTP maintenance in vivo. Neuron 38 (2003) 447-460
    • (2003) Neuron , vol.38 , pp. 447-460
    • Fukazawa, Y.1    Saitoh, Y.2    Ozawa, F.3    Ohta, Y.4    Mizuno, K.5    Inokuchi, K.6
  • 37
    • 0037195189 scopus 로고    scopus 로고
    • Multiple spatiotemporal modes of actin reorganization by NMDA receptors and voltage-gated Ca2+ channels
    • Furuyashiki T., Arakawa Y., Takemoto-Kimura S., Bito H., and Narumiya S. Multiple spatiotemporal modes of actin reorganization by NMDA receptors and voltage-gated Ca2+ channels. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 14458-14463
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 14458-14463
    • Furuyashiki, T.1    Arakawa, Y.2    Takemoto-Kimura, S.3    Bito, H.4    Narumiya, S.5
  • 38
    • 0023245565 scopus 로고
    • Modulation of spectrin-actin assembly by erythrocyte adducin
    • Gardner K., and Bennett V. Modulation of spectrin-actin assembly by erythrocyte adducin. Nature 328 (1987) 359-362
    • (1987) Nature , vol.328 , pp. 359-362
    • Gardner, K.1    Bennett, V.2
  • 39
    • 0027104517 scopus 로고
    • The control of actin nucleotide exchange by thymosin beta 4 and profiling. A potential regulatory mechanism for actin polymerization in cells
    • Goldschmidt-Clermont P.J., Furman M.I., Wachsstock D., Safer D., Nachmias V.T., and Pollard T.D. The control of actin nucleotide exchange by thymosin beta 4 and profiling. A potential regulatory mechanism for actin polymerization in cells. Mol. Biol. Cell 3 (1992) 1015-1024
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1015-1024
    • Goldschmidt-Clermont, P.J.1    Furman, M.I.2    Wachsstock, D.3    Safer, D.4    Nachmias, V.T.5    Pollard, T.D.6
  • 40
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A. Rho GTPases and the actin cytoskeleton. Science 279 (1998) 509-514
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 41
    • 0032403433 scopus 로고    scopus 로고
    • Regulation of F-actin stability in dendritic spines by glutamate receptors and calcineurin
    • Halpain S., Hipolito A., and Saffer L. Regulation of F-actin stability in dendritic spines by glutamate receptors and calcineurin. J. Neurosci. 18 (1998) 9835-9844
    • (1998) J. Neurosci. , vol.18 , pp. 9835-9844
    • Halpain, S.1    Hipolito, A.2    Saffer, L.3
  • 42
    • 0030025216 scopus 로고    scopus 로고
    • Disappearance of actin-binding protein, drebrin, from hippocampal synapses in Alzheimer's disease
    • Harigaya Y., Shoji M., Shirao T., and Hirai S. Disappearance of actin-binding protein, drebrin, from hippocampal synapses in Alzheimer's disease. J. Neurosci. Res. 43 (1996) 87-92
    • (1996) J. Neurosci. Res. , vol.43 , pp. 87-92
    • Harigaya, Y.1    Shoji, M.2    Shirao, T.3    Hirai, S.4
  • 43
    • 0028330166 scopus 로고
    • Dendritic spines: cellular specializations imparting both stability and flexibility to synaptic function
    • Harris K.M., and Kater S.B. Dendritic spines: cellular specializations imparting both stability and flexibility to synaptic function. Annu. Rev. Neurosci. 17 (1994) 341-371
    • (1994) Annu. Rev. Neurosci. , vol.17 , pp. 341-371
    • Harris, K.M.1    Kater, S.B.2
  • 44
    • 0033033642 scopus 로고    scopus 로고
    • Loss of proteins regulating synaptic plasticity in normal aging of the human brain and in Alzheimer disease
    • Hatanpaa K., Isaacs K.R., Shirao T., Brady D.R., and Rapoport S.I. Loss of proteins regulating synaptic plasticity in normal aging of the human brain and in Alzheimer disease. J. Neuropathol. Exp. Neurol. 58 (1999) 637-643
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , pp. 637-643
    • Hatanpaa, K.1    Isaacs, K.R.2    Shirao, T.3    Brady, D.R.4    Rapoport, S.I.5
  • 45
    • 0033562792 scopus 로고    scopus 로고
    • Change in the shape of dendritic spines caused by overexpression of drebrin in cultured cortical neurons
    • Hayashi K., and Shirao T. Change in the shape of dendritic spines caused by overexpression of drebrin in cultured cortical neurons. J. Neurosci. 19 (1999) 3918-3925
    • (1999) J. Neurosci. , vol.19 , pp. 3918-3925
    • Hayashi, K.1    Shirao, T.2
  • 47
    • 0029825623 scopus 로고    scopus 로고
    • Modulatory role of drebrin on the cytoskeleton within dendritic spines in the rat cerebral cortex
    • Hayashi K., Ishikawa R., Ye L.H., He X.L., Takata K., Kohama K., and Shirao T. Modulatory role of drebrin on the cytoskeleton within dendritic spines in the rat cerebral cortex. J. Neurosci. 16 (1996) 7161-7170
    • (1996) J. Neurosci. , vol.16 , pp. 7161-7170
    • Hayashi, K.1    Ishikawa, R.2    Ye, L.H.3    He, X.L.4    Takata, K.5    Kohama, K.6    Shirao, T.7
  • 48
    • 0346433978 scopus 로고    scopus 로고
    • Activity-dependent redistribution and essential role of cortactin in dendritic spine morphogenesis
    • Hering H., and Sheng M. Activity-dependent redistribution and essential role of cortactin in dendritic spine morphogenesis. J. Neurosci. 23 (2003) 11759-11769
    • (2003) J. Neurosci. , vol.23 , pp. 11759-11769
    • Hering, H.1    Sheng, M.2
  • 49
    • 0029046119 scopus 로고
    • Effect of a neuron-specific actin-binding protein, drebrin A, on cell-substratum adhesion
    • Ikeda K., Shirao T., Toda M., Asada H., Toya S., and Uyemura K. Effect of a neuron-specific actin-binding protein, drebrin A, on cell-substratum adhesion. Neurosci. Lett. 194 (1995) 197-200
    • (1995) Neurosci. Lett. , vol.194 , pp. 197-200
    • Ikeda, K.1    Shirao, T.2    Toda, M.3    Asada, H.4    Toya, S.5    Uyemura, K.6
  • 50
    • 0030030678 scopus 로고    scopus 로고
    • Stabilization of adhesion plaques by the expression of drebrin A in fibroblasts
    • Ikeda K., Kaub P.A., Asada H., Uyemura K., Toya S., and Shirao T. Stabilization of adhesion plaques by the expression of drebrin A in fibroblasts. Dev. Brain Res. 91 (1996) 227-236
    • (1996) Dev. Brain Res. , vol.91 , pp. 227-236
    • Ikeda, K.1    Kaub, P.A.2    Asada, H.3    Uyemura, K.4    Toya, S.5    Shirao, T.6
  • 51
    • 0033797832 scopus 로고    scopus 로고
    • Dendritic spine structural anomalies in fragile-X mental retardation syndrome
    • Irwin S.A., Galvez R., and Greenough W.T. Dendritic spine structural anomalies in fragile-X mental retardation syndrome. Cereb. Cortex 10 (2000) 1038-1044
    • (2000) Cereb. Cortex , vol.10 , pp. 1038-1044
    • Irwin, S.A.1    Galvez, R.2    Greenough, W.T.3
  • 52
    • 0024565757 scopus 로고
    • Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin. Potentiation of protective ability of tropomyosins by 83 kDa nonmuscle caldesmon
    • Ishikawa R., Yamashiro S., and Matsumura F. Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin. Potentiation of protective ability of tropomyosins by 83 kDa nonmuscle caldesmon. J. Biol. Chem. 264 (1989) 7490-7497
    • (1989) J. Biol. Chem. , vol.264 , pp. 7490-7497
    • Ishikawa, R.1    Yamashiro, S.2    Matsumura, F.3
  • 54
    • 0029087151 scopus 로고
    • Purification of an ATP-dependent actin-binding protein from a lower eukaryote, Physarum polycephalum
    • Ishikawa R., Sasaki Y., Nakamura A., Takagi T., and Kohama K. Purification of an ATP-dependent actin-binding protein from a lower eukaryote, Physarum polycephalum. Biochem. Biophys. Res. Commun. 212 (1995) 347-352
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 347-352
    • Ishikawa, R.1    Sasaki, Y.2    Nakamura, A.3    Takagi, T.4    Kohama, K.5
  • 55
    • 0142148230 scopus 로고    scopus 로고
    • Polarized actin bundles formed by human fascin-1: their sliding and disassembly on myosin II and myosin V in vitro
    • Ishikawa R., Sakamoto T., Ando T., Higashi-Fujime S., and Kohama K. Polarized actin bundles formed by human fascin-1: their sliding and disassembly on myosin II and myosin V in vitro. J. Neurochem. 87 (2003) 676-685
    • (2003) J. Neurochem. , vol.87 , pp. 676-685
    • Ishikawa, R.1    Sakamoto, T.2    Ando, T.3    Higashi-Fujime, S.4    Kohama, K.5
  • 56
    • 0028139040 scopus 로고
    • Drebrin, a development-associated brain protein from rat embryo, causes the dissociation of tropomyosin from actin filaments
    • Ishikawa R., Hayashi K., Shirao T., Xue Y., Takagi T., Sasaki Y., and Kohama K. Drebrin, a development-associated brain protein from rat embryo, causes the dissociation of tropomyosin from actin filaments. J. Biol. Chem. 269 (1994) 29928-29933
    • (1994) J. Biol. Chem. , vol.269 , pp. 29928-29933
    • Ishikawa, R.1    Hayashi, K.2    Shirao, T.3    Xue, Y.4    Takagi, T.5    Sasaki, Y.6    Kohama, K.7
  • 57
    • 0023157142 scopus 로고
    • Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate
    • Janmey P.A., and Stossel T.P. Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate. Nature 325 (1987) 362-364
    • (1987) Nature , vol.325 , pp. 362-364
    • Janmey, P.A.1    Stossel, T.P.2
  • 58
    • 0021801388 scopus 로고
    • Interactions of gelsolin and gelsolin-actin complexes with actin. Effects of calcium on actin nucleation, filament severing, and end blocking
    • Janmey P.A., Chaponnier C., Lind S.E., Zaner K.S., Stossel T.P., and Yin H.L. Interactions of gelsolin and gelsolin-actin complexes with actin. Effects of calcium on actin nucleation, filament severing, and end blocking. Biochemistry 24 (1985) 3714-3723
    • (1985) Biochemistry , vol.24 , pp. 3714-3723
    • Janmey, P.A.1    Chaponnier, C.2    Lind, S.E.3    Zaner, K.S.4    Stossel, T.P.5    Yin, H.L.6
  • 59
    • 0036247552 scopus 로고    scopus 로고
    • A novel, brain-specific mouse drebrin: cDNA cloning, chromosomal mapping, genomic structure, expression, and functional characterization
    • Jin M., Tanaka S., Sekino Y., Ren Y., Yamazaki H., Kawai-Hirai R., Kojima N., and Shirao T. A novel, brain-specific mouse drebrin: cDNA cloning, chromosomal mapping, genomic structure, expression, and functional characterization. Genomics 79 (2002) 686-692
    • (2002) Genomics , vol.79 , pp. 686-692
    • Jin, M.1    Tanaka, S.2    Sekino, Y.3    Ren, Y.4    Yamazaki, H.5    Kawai-Hirai, R.6    Kojima, N.7    Shirao, T.8
  • 61
    • 0031439662 scopus 로고    scopus 로고
    • Isoform specificity in the relationship of actin to dendritic spines
    • Kaech S., Fischer M., Doll T., and Matus A. Isoform specificity in the relationship of actin to dendritic spines. J. Neurosci. 17 (1997) 9565-9572
    • (1997) J. Neurosci. , vol.17 , pp. 9565-9572
    • Kaech, S.1    Fischer, M.2    Doll, T.3    Matus, A.4
  • 62
    • 0035912770 scopus 로고    scopus 로고
    • Cytoskeletal microdifferentiation: a mechanism for organizing morphological plasticity in dendrites
    • Kaech S., Parmar H., Roelandse M., Bornmann C., and Matus A. Cytoskeletal microdifferentiation: a mechanism for organizing morphological plasticity in dendrites. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 7086-7092
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 7086-7092
    • Kaech, S.1    Parmar, H.2    Roelandse, M.3    Bornmann, C.4    Matus, A.5
  • 63
    • 0021894617 scopus 로고
    • The function of myosin and myosin light chain kinase phosphorylation in smooth muscle
    • Kamm K.E., and Stull J.T. The function of myosin and myosin light chain kinase phosphorylation in smooth muscle. Annu. Rev. Pharmacol. Toxicol. 25 (1985) 593-620
    • (1985) Annu. Rev. Pharmacol. Toxicol. , vol.25 , pp. 593-620
    • Kamm, K.E.1    Stull, J.T.2
  • 64
    • 31644445194 scopus 로고    scopus 로고
    • Activation of Rac1 by RhoG regulates cell migration
    • Katoh H., Hiramoto K., and Negishi M. Activation of Rac1 by RhoG regulates cell migration. J. Cell Sci. 119 (2006) 56-65
    • (2006) J. Cell Sci. , vol.119 , pp. 56-65
    • Katoh, H.1    Hiramoto, K.2    Negishi, M.3
  • 65
    • 0026029783 scopus 로고
    • Chicken nonmuscle myosin heavy chains: differential expression of two mRNAs and evidence for two different polypeptides
    • Kawamoto S., and Adelstein R.S. Chicken nonmuscle myosin heavy chains: differential expression of two mRNAs and evidence for two different polypeptides. J. Cell Biol. 112 (1991) 915-924
    • (1991) J. Cell Biol. , vol.112 , pp. 915-924
    • Kawamoto, S.1    Adelstein, R.S.2
  • 66
    • 0031172429 scopus 로고    scopus 로고
    • The postsynaptic density at glutamatergic synapses
    • Kennedy M.B. The postsynaptic density at glutamatergic synapses. Trends Neurosci. 20 (1997) 264-268
    • (1997) Trends Neurosci. , vol.20 , pp. 264-268
    • Kennedy, M.B.1
  • 67
    • 0025021863 scopus 로고
    • Molecular genetic dissection of myosin heavy chain function
    • Kiehart D.P. Molecular genetic dissection of myosin heavy chain function. Cell 60 (1990) 347-350
    • (1990) Cell , vol.60 , pp. 347-350
    • Kiehart, D.P.1
  • 71
    • 0023718581 scopus 로고
    • Nucleotide sequences of two embryonic drebrins, developmentally regulated brain proteins, and developmental change in their mRNAs
    • Kojima N., Kato Y., Shirao T., and Obata K. Nucleotide sequences of two embryonic drebrins, developmentally regulated brain proteins, and developmental change in their mRNAs. Brain Res. 464 (1988) 207-215
    • (1988) Brain Res. , vol.464 , pp. 207-215
    • Kojima, N.1    Kato, Y.2    Shirao, T.3    Obata, K.4
  • 72
    • 0027289194 scopus 로고
    • Molecular cloning of a developmentally regulated brain protein, chicken drebrin A and its expression by alternative splicing of the drebrin gene
    • Kojima N., Shirao T., and Obata K. Molecular cloning of a developmentally regulated brain protein, chicken drebrin A and its expression by alternative splicing of the drebrin gene. Mol. Brain Res. 19 (1993) 101-114
    • (1993) Mol. Brain Res. , vol.19 , pp. 101-114
    • Kojima, N.1    Shirao, T.2    Obata, K.3
  • 73
    • 34247632141 scopus 로고    scopus 로고
    • Synaptic dysfunction and disruption of postsynaptic drebrin-actin complex: a study of neurological disorders accompanied by cognitive deficits
    • Kojima N., and Shirao T. Synaptic dysfunction and disruption of postsynaptic drebrin-actin complex: a study of neurological disorders accompanied by cognitive deficits. Neurosci. Res. 58 (2007) 1-5
    • (2007) Neurosci. Res. , vol.58 , pp. 1-5
    • Kojima, N.1    Shirao, T.2
  • 74
    • 0037468121 scopus 로고    scopus 로고
    • Coordinated development of identified serotonergic neurons and their target ciliary cells in Helisoma trivolvis embryos
    • Koss R., Diefenbach T.J., Kuang S., Doran S.A., and Goldberg J.I. Coordinated development of identified serotonergic neurons and their target ciliary cells in Helisoma trivolvis embryos. J. Comp. Neurol. 457 (2003) 313-325
    • (2003) J. Comp. Neurol. , vol.457 , pp. 313-325
    • Koss, R.1    Diefenbach, T.J.2    Kuang, S.3    Doran, S.A.4    Goldberg, J.I.5
  • 75
    • 31044433924 scopus 로고    scopus 로고
    • Control of the assembly of ATP- and ADP-actin by formins and profilin
    • Kovar D.R., Harris E.S., Mahaffy R., Higgs H.N., and Pollard T.D. Control of the assembly of ATP- and ADP-actin by formins and profilin. Cell 124 (2006) 423-435
    • (2006) Cell , vol.124 , pp. 423-435
    • Kovar, D.R.1    Harris, E.S.2    Mahaffy, R.3    Higgs, H.N.4    Pollard, T.D.5
  • 76
    • 0033557999 scopus 로고    scopus 로고
    • Interactions of calmodulin and alpha-actinin with the NR1 subunit modulate Ca2+-dependent inactivation of NMDA receptors
    • Krupp J.J., Vissel B., Thomas C.G., Heinemann S.F., and Westbrook G.L. Interactions of calmodulin and alpha-actinin with the NR1 subunit modulate Ca2+-dependent inactivation of NMDA receptors. J. Neurosci. 19 (1999) 1165-1178
    • (1999) J. Neurosci. , vol.19 , pp. 1165-1178
    • Krupp, J.J.1    Vissel, B.2    Thomas, C.G.3    Heinemann, S.F.4    Westbrook, G.L.5
  • 77
    • 0030005249 scopus 로고    scopus 로고
    • A new function for adducing. Calcium/calmodulin-regulated capping of the barbed ends of actin filaments
    • Kuhlman P.A., Hughes C.A., Bennett V., and Fowler V.M. A new function for adducing. Calcium/calmodulin-regulated capping of the barbed ends of actin filaments. J. Biol. Chem. 271 (1996) 7986-7991
    • (1996) J. Biol. Chem. , vol.271 , pp. 7986-7991
    • Kuhlman, P.A.1    Hughes, C.A.2    Bennett, V.3    Fowler, V.M.4
  • 78
    • 33846633336 scopus 로고    scopus 로고
    • Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease
    • Lacor P.N., Buniel M.C., Furlow P.W., Clemente A.S., Velasco P.T., Wood M., Viola K.L., and Klein W.L. Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease. J. Neurosci. 27 (2007) 796-807
    • (2007) J. Neurosci. , vol.27 , pp. 796-807
    • Lacor, P.N.1    Buniel, M.C.2    Furlow, P.W.3    Clemente, A.S.4    Velasco, P.T.5    Wood, M.6    Viola, K.L.7    Klein, W.L.8
  • 79
    • 0020550407 scopus 로고
    • Cytoplasmic organization in cerebellar dendritic spines
    • Landis D.M., and Reese T.S. Cytoplasmic organization in cerebellar dendritic spines. J. Cell Biol. 97 (1983) 1169-1178
    • (1983) J. Cell Biol. , vol.97 , pp. 1169-1178
    • Landis, D.M.1    Reese, T.S.2
  • 80
    • 0031878090 scopus 로고    scopus 로고
    • The ADF homology (ADF-H) domain: a highly exploited actin-binding module
    • Lappalainen P., Kessels M.M., Cope M.J., and Drubin D.G. The ADF homology (ADF-H) domain: a highly exploited actin-binding module. Mol. Biol. Cell 9 (1998) 1951-1959
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1951-1959
    • Lappalainen, P.1    Kessels, M.M.2    Cope, M.J.3    Drubin, D.G.4
  • 81
    • 0017288488 scopus 로고
    • Actin, alpha-actinin, and tropomyosin interaction in the structural organization of actin filaments in nonmuscle cells
    • Lazarides E. Actin, alpha-actinin, and tropomyosin interaction in the structural organization of actin filaments in nonmuscle cells. J. Cell Biol. 68 (1976) 202-219
    • (1976) J. Cell Biol. , vol.68 , pp. 202-219
    • Lazarides, E.1
  • 82
    • 0030026182 scopus 로고    scopus 로고
    • Differential effects of the Rac GTPase on Purkinje cell axons and dendritic trunks and spines
    • Luo L., Hensch T.K., Ackerman L., Barbel S., Jan L.Y., and Jan Y.N. Differential effects of the Rac GTPase on Purkinje cell axons and dendritic trunks and spines. Nature 379 (1996) 837-840
    • (1996) Nature , vol.379 , pp. 837-840
    • Luo, L.1    Hensch, T.K.2    Ackerman, L.3    Barbel, S.4    Jan, L.Y.5    Jan, Y.N.6
  • 83
    • 0032500057 scopus 로고    scopus 로고
    • Actin branches out
    • Machesky L.M., and Way M. Actin branches out. Nature 394 (1998) 125-126
    • (1998) Nature , vol.394 , pp. 125-126
    • Machesky, L.M.1    Way, M.2
  • 84
    • 0026340941 scopus 로고
    • Characterization of actin filament severing by actophorin from Acanthamoeba castellanii
    • Maciver S.K., Zot H.G., and Pollard T.D. Characterization of actin filament severing by actophorin from Acanthamoeba castellanii. J. Cell Biol. 115 (1991) 1611-1620
    • (1991) J. Cell Biol. , vol.115 , pp. 1611-1620
    • Maciver, S.K.1    Zot, H.G.2    Pollard, T.D.3
  • 85
    • 28844442257 scopus 로고    scopus 로고
    • Stability of the distribution of spines containing drebrin A in the sensory cortex layer I of mice expressing mutated APP and PS1 genes
    • Mahadomrongkul V., Huerta P.T., Shirao T., and Aoki C. Stability of the distribution of spines containing drebrin A in the sensory cortex layer I of mice expressing mutated APP and PS1 genes. Brain Res. 1064 (2005) 66-74
    • (2005) Brain Res. , vol.1064 , pp. 66-74
    • Mahadomrongkul, V.1    Huerta, P.T.2    Shirao, T.3    Aoki, C.4
  • 86
    • 0014151715 scopus 로고
    • Localization of 6S component of a alpha-actinin at Z-band
    • Masaki T., Endo M., and Ebashi S. Localization of 6S component of a alpha-actinin at Z-band. J. Biochem. (Tokyo) 62 (1967) 630-632
    • (1967) J. Biochem. (Tokyo) , vol.62 , pp. 630-632
    • Masaki, T.1    Endo, M.2    Ebashi, S.3
  • 87
    • 0032847204 scopus 로고    scopus 로고
    • Postsynaptic actin and neuronal plasticity
    • Matus A. Postsynaptic actin and neuronal plasticity. Curr. Opin. Neurobiol. 9 (1999) 561-565
    • (1999) Curr. Opin. Neurobiol. , vol.9 , pp. 561-565
    • Matus, A.1
  • 89
    • 33644775671 scopus 로고    scopus 로고
    • Myosin II functions in actin-bundle turnover in neuronal growth cones
    • Medeiros N.A., Burnette D.T., and Forscher P. Myosin II functions in actin-bundle turnover in neuronal growth cones. Nat. Cell Biol. 8 (2006) 215-226
    • (2006) Nat. Cell Biol. , vol.8 , pp. 215-226
    • Medeiros, N.A.1    Burnette, D.T.2    Forscher, P.3
  • 91
    • 0023600841 scopus 로고
    • Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding
    • Mische S.M., Mooseker M.S., and Morrow J.S. Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding. J. Cell Biol. 105 (1987) 2837-2845
    • (1987) J. Cell Biol. , vol.105 , pp. 2837-2845
    • Mische, S.M.1    Mooseker, M.S.2    Morrow, J.S.3
  • 92
    • 33646042277 scopus 로고    scopus 로고
    • Overexpression of drebrin A in immature neurons induces the accumulation of F-actin and PSD-95 into dendritic filopodia, and the formation of large abnormal protrusions
    • Mizui T., Takahashi H., Sekino Y., and Shirao T. Overexpression of drebrin A in immature neurons induces the accumulation of F-actin and PSD-95 into dendritic filopodia, and the formation of large abnormal protrusions. Mol. Cell. Neurosci. 30 (2005) 630-638
    • (2005) Mol. Cell. Neurosci. , vol.30 , pp. 630-638
    • Mizui, T.1    Takahashi, H.2    Sekino, Y.3    Shirao, T.4
  • 93
    • 0024557848 scopus 로고
    • In situ localization of myosin and actin in dendritic spines with the immunogold technique
    • Morales M., and Fifkova E. In situ localization of myosin and actin in dendritic spines with the immunogold technique. J. Comp. Neurol. 279 (1989) 666-674
    • (1989) J. Comp. Neurol. , vol.279 , pp. 666-674
    • Morales, M.1    Fifkova, E.2
  • 94
    • 0027769523 scopus 로고
    • Phosphorylation of vertebrate nonmuscle and smooth muscle myosin heavy chains and light chains
    • Moussavi R.S., Kelley C.A., and Adelstein R.S. Phosphorylation of vertebrate nonmuscle and smooth muscle myosin heavy chains and light chains. Mol. Cell. Biochem. 127/128 (1993) 219-227
    • (1993) Mol. Cell. Biochem. , vol.127-128 , pp. 219-227
    • Moussavi, R.S.1    Kelley, C.A.2    Adelstein, R.S.3
  • 95
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments
    • Mullins R.D., Heuser J.A., and Pollard T.D. The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 6181-6186
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 97
    • 0021749110 scopus 로고
    • Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin
    • Nishida E., Maekawa S., and Sakai H. Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin. Biochemistry 23 (1984) 5307-5313
    • (1984) Biochemistry , vol.23 , pp. 5307-5313
    • Nishida, E.1    Maekawa, S.2    Sakai, H.3
  • 98
    • 0035882395 scopus 로고    scopus 로고
    • Spine formation and correlated assembly of presynaptic and postsynaptic molecules
    • Okabe S., Miwa A., and Okado H. Spine formation and correlated assembly of presynaptic and postsynaptic molecules. J. Neurosci. 21 (2001) 6105-6114
    • (2001) J. Neurosci. , vol.21 , pp. 6105-6114
    • Okabe, S.1    Miwa, A.2    Okado, H.3
  • 99
    • 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. Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity. Nat. Neurosci. 7 (2004) 1104-1112
    • (2004) Nat. Neurosci. , vol.7 , pp. 1104-1112
    • Okamoto, K.1    Nagai, T.2    Miyawaki, A.3    Hayashi, Y.4
  • 100
    • 0347986677 scopus 로고    scopus 로고
    • Identification of a novel basic helix-loop-helix-PAS factor, NXF, reveals a Sim2 competitive, positive regulatory role in dendritic-cytoskeleton modulator drebrin gene expression
    • Ooe N., Saito K., Mikami N., Nakatuka I., and Kaneko H. Identification of a novel basic helix-loop-helix-PAS factor, NXF, reveals a Sim2 competitive, positive regulatory role in dendritic-cytoskeleton modulator drebrin gene expression. Mol. Cell. Biol. 24 (2004) 608-616
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 608-616
    • Ooe, N.1    Saito, K.2    Mikami, N.3    Nakatuka, I.4    Kaneko, H.5
  • 101
    • 13844294267 scopus 로고    scopus 로고
    • A role for myosin VI in postsynaptic structure and glutamate receptor endocytosis
    • Osterweil E., Wells D.G., and Mooseker M.S. A role for myosin VI in postsynaptic structure and glutamate receptor endocytosis. J. Cell Biol. 168 (2005) 329-338
    • (2005) J. Cell Biol. , vol.168 , pp. 329-338
    • Osterweil, E.1    Wells, D.G.2    Mooseker, M.S.3
  • 102
    • 0028985603 scopus 로고
    • The alpha and gamma 1 isoforms of protein phosphatase 1 are highly and specifically concentrated in dendritic spines
    • Ouimet C.C., da Cruz e Silva E.F., and Greengard P. The alpha and gamma 1 isoforms of protein phosphatase 1 are highly and specifically concentrated in dendritic spines. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 3396-3400
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 3396-3400
    • Ouimet, C.C.1    da Cruz e Silva, E.F.2    Greengard, P.3
  • 103
    • 0344443828 scopus 로고    scopus 로고
    • Targeted protein degradation and synapse remodeling by an inducible protein kinase
    • Pak D.T., and Sheng M. Targeted protein degradation and synapse remodeling by an inducible protein kinase. Science 302 (2003) 1368-1373
    • (2003) Science , vol.302 , pp. 1368-1373
    • Pak, D.T.1    Sheng, M.2
  • 104
    • 0032707615 scopus 로고    scopus 로고
    • Drebrin is a widespread actin-associating protein enriched at junctional plaques, defining a specific microfilament anchorage system in polar epithelial cells
    • Peitsch W.K., Grund C., Kuhn C., Schnolzer M., Spring H., Schmelz M., and Franke W.W. Drebrin is a widespread actin-associating protein enriched at junctional plaques, defining a specific microfilament anchorage system in polar epithelial cells. Eur. J. Cell Biol. 78 (1999) 767-778
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 767-778
    • Peitsch, W.K.1    Grund, C.2    Kuhn, C.3    Schnolzer, M.4    Spring, H.5    Schmelz, M.6    Franke, W.W.7
  • 105
    • 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. Semiquantitative proteomic analysis of rat forebrain postsynaptic density fractions by mass spectrometry. J. Biol. Chem. 279 (2004) 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
  • 106
    • 0022881322 scopus 로고
    • Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments
    • Pollard T.D. Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. J. Cell Biol. 103 (1986) 2747-2754
    • (1986) J. Cell Biol. , vol.103 , pp. 2747-2754
    • Pollard, T.D.1
  • 107
    • 0042626585 scopus 로고    scopus 로고
    • Activity-regulated dynamic behavior of early dendritic protrusions: evidence for different types of dendritic filopodia
    • Portera-Cailliau C., Pan D.T., and Yuste R. Activity-regulated dynamic behavior of early dendritic protrusions: evidence for different types of dendritic filopodia. J. Neurosci. 23 (2003) 7129-7142
    • (2003) J. Neurosci. , vol.23 , pp. 7129-7142
    • Portera-Cailliau, C.1    Pan, D.T.2    Yuste, R.3
  • 108
    • 0020396107 scopus 로고
    • Microtubule disarray in cortical dendrites and neurobehavioral failure. I. Golgi and electron microscopic studies
    • Purpura D.P., Bodick N., Suzuki K., Rapin I., and Wurzelmann S. Microtubule disarray in cortical dendrites and neurobehavioral failure. I. Golgi and electron microscopic studies. Brain Res. 281 (1982) 287-297
    • (1982) Brain Res. , vol.281 , pp. 287-297
    • Purpura, D.P.1    Bodick, N.2    Suzuki, K.3    Rapin, I.4    Wurzelmann, S.5
  • 110
    • 33645065880 scopus 로고    scopus 로고
    • Change in the shape and density of dendritic spines caused by overexpression of acidic calponin in cultured hippocampal neurons
    • Rami G., Caillard O., Medina I., Pellegrino C., Fattoum A., Ben-Ari Y., and Ferhat L. Change in the shape and density of dendritic spines caused by overexpression of acidic calponin in cultured hippocampal neurons. Hippocampus 16 (2006) 183-197
    • (2006) Hippocampus , vol.16 , pp. 183-197
    • Rami, G.1    Caillard, O.2    Medina, I.3    Pellegrino, C.4    Fattoum, A.5    Ben-Ari, Y.6    Ferhat, L.7
  • 111
    • 0033761838 scopus 로고    scopus 로고
    • Signaling between the actin cytoskeleton and the postsynaptic density of dendritic spines
    • Rao A., and Craig A.M. Signaling between the actin cytoskeleton and the postsynaptic density of dendritic spines. Hippocampus 10 (2000) 527-541
    • (2000) Hippocampus , vol.10 , pp. 527-541
    • Rao, A.1    Craig, A.M.2
  • 112
    • 30644456796 scopus 로고    scopus 로고
    • A critical role for myosin IIb in dendritic spine morphology and synaptic function
    • Ryu J., Liu L., Wong T.P., Wu D.C., Burette A., Weinberg R., Wang Y.T., and Sheng M. A critical role for myosin IIb in dendritic spine morphology and synaptic function. Neuron 49 (2006) 175-182
    • (2006) Neuron , vol.49 , pp. 175-182
    • Ryu, J.1    Liu, L.2    Wong, T.P.3    Wu, D.C.4    Burette, A.5    Weinberg, R.6    Wang, Y.T.7    Sheng, M.8
  • 113
    • 0028489887 scopus 로고
    • Beta thymosins as actin binding peptides
    • Safer D., and Nachmias V.T. Beta thymosins as actin binding peptides. Bioessays 16 (1994) 590
    • (1994) Bioessays , vol.16 , pp. 590
    • Safer, D.1    Nachmias, V.T.2
  • 114
    • 0025355476 scopus 로고
    • Isolation of a 5-kDa actin-sequestering peptide from human blood platelets
    • Safer D., Golla R., and Nachmias V.T. Isolation of a 5-kDa actin-sequestering peptide from human blood platelets. Proc. Natl. Acad. Sci. U.S.A. 87 (1990) 2536-2540
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 2536-2540
    • Safer, D.1    Golla, R.2    Nachmias, V.T.3
  • 115
    • 0030040876 scopus 로고    scopus 로고
    • Inhibition by drebrin of the actin-bundling activity of brain fascin, a protein localized in filopodia of growth cones
    • Sasaki Y., Hayashi K., Shirao T., Ishikawa R., and Kohama K. Inhibition by drebrin of the actin-bundling activity of brain fascin, a protein localized in filopodia of growth cones. J. Neurochem. 66 (1996) 980-988
    • (1996) J. Neurochem. , vol.66 , pp. 980-988
    • Sasaki, Y.1    Hayashi, K.2    Shirao, T.3    Ishikawa, R.4    Kohama, K.5
  • 117
    • 31944444621 scopus 로고    scopus 로고
    • Localized recruitment and activation of RhoA underlies dendritic spine morphology in a glutamate receptor-dependent manner
    • Schubert V., Da Silva J.S., and Dotti C.G. Localized recruitment and activation of RhoA underlies dendritic spine morphology in a glutamate receptor-dependent manner. J. Cell Biol. 172 (2006) 453-467
    • (2006) J. Cell Biol. , vol.172 , pp. 453-467
    • Schubert, V.1    Da Silva, J.S.2    Dotti, C.G.3
  • 118
    • 33644827036 scopus 로고    scopus 로고
    • Activation of N-methyl-d-aspartate receptor induces a shift of drebrin distribution: disappearance from dendritic spines and appearance in dendritic shafts
    • Sekino Y., Tanaka S., Hanamura K., Yamazaki H., Sasagawa Y., Xue Y., Hayashi K., and Shirao T. Activation of N-methyl-d-aspartate receptor induces a shift of drebrin distribution: disappearance from dendritic spines and appearance in dendritic shafts. Mol. Cell. Neurosci. 31 (2006) 493-504
    • (2006) Mol. Cell. Neurosci. , vol.31 , pp. 493-504
    • Sekino, Y.1    Tanaka, S.2    Hanamura, K.3    Yamazaki, H.4    Sasagawa, Y.5    Xue, Y.6    Hayashi, K.7    Shirao, T.8
  • 119
    • 0034677906 scopus 로고    scopus 로고
    • Myosins: a diverse superfamily
    • Sellers J.R. Myosins: a diverse superfamily. Biochim. Biophys. Acta 1496 (2000) 3-22
    • (2000) Biochim. Biophys. Acta , vol.1496 , pp. 3-22
    • Sellers, J.R.1
  • 120
  • 121
    • 0037166050 scopus 로고    scopus 로고
    • Drebrin, a dendritic spine protein, is manifold decreased in brains of patients with Alzheimer's disease and Down syndrome
    • Shim K.S., and Lubec G. Drebrin, a dendritic spine protein, is manifold decreased in brains of patients with Alzheimer's disease and Down syndrome. Neurosci. Lett. 324 (2002) 209-212
    • (2002) Neurosci. Lett. , vol.324 , pp. 209-212
    • Shim, K.S.1    Lubec, G.2
  • 122
    • 85047673845 scopus 로고
    • The roles of microfilament-associated proteins, drebrins, in brain morphogenesis: a review
    • Shirao T. The roles of microfilament-associated proteins, drebrins, in brain morphogenesis: a review. J. Biochem. (Tokyo) 117 (1995) 231-236
    • (1995) J. Biochem. (Tokyo) , vol.117 , pp. 231-236
    • Shirao, T.1
  • 123
    • 0021964771 scopus 로고
    • Two acidic proteins associated with brain development in chick embryo
    • Shirao T., and Obata K. Two acidic proteins associated with brain development in chick embryo. J. Neurochem. 44 (1985) 1210-1216
    • (1985) J. Neurochem. , vol.44 , pp. 1210-1216
    • Shirao, T.1    Obata, K.2
  • 124
    • 0022797037 scopus 로고
    • Immunochemical homology of 3 developmentally regulated brain proteins and their developmental change in neuronal distribution
    • Shirao T., and Obata K. Immunochemical homology of 3 developmentally regulated brain proteins and their developmental change in neuronal distribution. Brain Res. 394 (1986) 233-244
    • (1986) Brain Res. , vol.394 , pp. 233-244
    • Shirao, T.1    Obata, K.2
  • 125
    • 0035058882 scopus 로고    scopus 로고
    • Clustering and anchoring mechanisms of molecular constituents of postsynaptic scaffolds in dendritic spines
    • Shirao T., and Sekino Y. Clustering and anchoring mechanisms of molecular constituents of postsynaptic scaffolds in dendritic spines. Neurosci. Res. 40 (2001) 1-7
    • (2001) Neurosci. Res. , vol.40 , pp. 1-7
    • Shirao, T.1    Sekino, Y.2
  • 126
    • 0023243989 scopus 로고
    • Localization of a developmentally regulated neuron-specific protein S54 in dendrites as revealed by immunoelectron microscopy.
    • Shirao T., Inoue H.K., Kano Y., and Obata K. Localization of a developmentally regulated neuron-specific protein S54 in dendrites as revealed by immunoelectron microscopy. Brain Res. 413 (1987) 374-378
    • (1987) Brain Res. , vol.413 , pp. 374-378
    • Shirao, T.1    Inoue, H.K.2    Kano, Y.3    Obata, K.4
  • 127
    • 0023793340 scopus 로고
    • Molecular cloning of a cDNA for the developmentally regulated brain protein, drebrin
    • Shirao T., Kojima N., Kato Y., and Obata K. Molecular cloning of a cDNA for the developmentally regulated brain protein, drebrin. Brain Res. 464 (1988) 71-74
    • (1988) Brain Res. , vol.464 , pp. 71-74
    • Shirao, T.1    Kojima, N.2    Kato, Y.3    Obata, K.4
  • 128
    • 84993587051 scopus 로고
    • Two forms of drebrins, developmentally regulated brain proteins, in rat
    • Shirao T., Kojima N., Nabeta Y., and Obata K. Two forms of drebrins, developmentally regulated brain proteins, in rat. Proc. Jpn. Acad. 65 (1989) 169-172
    • (1989) Proc. Jpn. Acad. , vol.65 , pp. 169-172
    • Shirao, T.1    Kojima, N.2    Nabeta, Y.3    Obata, K.4
  • 129
    • 0026512294 scopus 로고
    • Cloning of drebrin A and induction of neurite-like processes in drebrin-transfected cells
    • Shirao T., Kojima N., and Obata K. Cloning of drebrin A and induction of neurite-like processes in drebrin-transfected cells. Neuroreport 3 (1992) 109-112
    • (1992) Neuroreport , vol.3 , pp. 109-112
    • Shirao, T.1    Kojima, N.2    Obata, K.3
  • 130
    • 0025025759 scopus 로고
    • Expression of three drebrin isoforms in the developing nervous system
    • Shirao T., Kojima N., Terada S., and Obata K. Expression of three drebrin isoforms in the developing nervous system. Neurosci. Res. Suppl. 13 (1990) S106-S111
    • (1990) Neurosci. Res. Suppl. , vol.13
    • Shirao, T.1    Kojima, N.2    Terada, S.3    Obata, K.4
  • 131
  • 132
    • 0029000811 scopus 로고
    • Actin filament organization in the fish keratocyte lamellipodium
    • Small J.V., Herzog M., and Anderson K. Actin filament organization in the fish keratocyte lamellipodium. J. Cell Biol. 129 (1995) 1275-1286
    • (1995) J. Cell Biol. , vol.129 , pp. 1275-1286
    • Small, J.V.1    Herzog, M.2    Anderson, K.3
  • 134
    • 0036176244 scopus 로고    scopus 로고
    • Rapid turnover of actin in dendritic spines and its regulation by activity
    • Star E.N., Kwiatkowski D.J., and Murthy V.N. Rapid turnover of actin in dendritic spines and its regulation by activity. Nat. Neurosci. 5 (2002) 239-246
    • (2002) Nat. Neurosci. , vol.5 , pp. 239-246
    • Star, E.N.1    Kwiatkowski, D.J.2    Murthy, V.N.3
  • 135
    • 0033620689 scopus 로고    scopus 로고
    • Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia
    • Svitkina T.M., and Borisy G.G. Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell Biol. 145 (1999) 1009-1026
    • (1999) J. Cell Biol. , vol.145 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 136
    • 33646830444 scopus 로고    scopus 로고
    • Down-regulation of drebrin A expression suppresses synaptic targeting of NMDA receptors in developing hippocampal neurones
    • Takahashi H., Mizui T., and Shirao T. Down-regulation of drebrin A expression suppresses synaptic targeting of NMDA receptors in developing hippocampal neurones. J. Neurochem. 97 Suppl. 1 (2006) 110-115
    • (2006) J. Neurochem. , vol.97 , Issue.SUPPL. 1 , pp. 110-115
    • Takahashi, H.1    Mizui, T.2    Shirao, T.3
  • 137
    • 0041342023 scopus 로고    scopus 로고
    • Drebrin-dependent actin clustering in dendritic filopodia governs synaptic targeting of postsynaptic density-95 and dendritic spine morphogenesis
    • Takahashi H., Sekino Y., Tanaka S., Mizui T., Kishi S., and Shirao T. Drebrin-dependent actin clustering in dendritic filopodia governs synaptic targeting of postsynaptic density-95 and dendritic spine morphogenesis. J. Neurosci. 23 (2003) 6586-6595
    • (2003) J. Neurosci. , vol.23 , pp. 6586-6595
    • Takahashi, H.1    Sekino, Y.2    Tanaka, S.3    Mizui, T.4    Kishi, S.5    Shirao, T.6
  • 138
    • 0022930623 scopus 로고
    • Isolation and characterization of a 34,000 Da calmodulin- and F-actin-binding protein from chicken gizzard smooth muscle
    • Takahashi K., Hiwada K., and Kokubu T. Isolation and characterization of a 34,000 Da calmodulin- and F-actin-binding protein from chicken gizzard smooth muscle. Biochem. Biophys. Res. Commun. 141 (1986) 20-26
    • (1986) Biochem. Biophys. Res. Commun. , vol.141 , pp. 20-26
    • Takahashi, K.1    Hiwada, K.2    Kokubu, T.3
  • 139
    • 0034072958 scopus 로고    scopus 로고
    • The effects of neurotrophin-3 and brain-derived neurotrophic factor on cerebellar granule cell movement and neurite extension in vitro
    • Tanaka S., Sekino Y., and Shirao T. The effects of neurotrophin-3 and brain-derived neurotrophic factor on cerebellar granule cell movement and neurite extension in vitro. Neuroscience 97 (2000) 727-734
    • (2000) Neuroscience , vol.97 , pp. 727-734
    • Tanaka, S.1    Sekino, Y.2    Shirao, T.3
  • 140
    • 0025740949 scopus 로고
    • Actin microfilament dynamics in locomoting cells
    • Theriot J.A., and Mitchison T.J. Actin microfilament dynamics in locomoting cells. Nature 352 (1991) 126-131
    • (1991) Nature , vol.352 , pp. 126-131
    • Theriot, J.A.1    Mitchison, T.J.2
  • 141
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst L., and D'Souza-Schorey C. Rho GTPases and signaling networks. Genes Dev. 11 (1997) 2295-2322
    • (1997) Genes Dev. , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 143
    • 0027162413 scopus 로고
    • Affinity of alpha-actinin for actin determines the structure and mechanical properties of actin filament gels
    • Wachsstock D.H., Schwartz W.H., and Pollard T.D. Affinity of alpha-actinin for actin determines the structure and mechanical properties of actin filament gels. Biophys. J. 65 (1993) 205-214
    • (1993) Biophys. J. , vol.65 , pp. 205-214
    • Wachsstock, D.H.1    Schwartz, W.H.2    Pollard, T.D.3
  • 144
    • 0033520925 scopus 로고    scopus 로고
    • Tropomodulin increases the critical concentration of barbed end-capped actin filaments by converting ADP.P(i)-actin to ADP-actin at all pointed filament ends
    • Weber A., Pennise C.R., and Fowler V.M. Tropomodulin increases the critical concentration of barbed end-capped actin filaments by converting ADP.P(i)-actin to ADP-actin at all pointed filament ends. J. Biol. Chem. 274 (1999) 34637-34645
    • (1999) J. Biol. Chem. , vol.274 , pp. 34637-34645
    • Weber, A.1    Pennise, C.R.2    Fowler, V.M.3
  • 145
    • 0020484210 scopus 로고
    • Treadmilling of actin at physiological salt concentrations. An analysis of the critical concentrations of actin filaments
    • Wegner A. Treadmilling of actin at physiological salt concentrations. An analysis of the critical concentrations of actin filaments. J. Mol. Biol. 161 (1982) 607-615
    • (1982) J. Mol. Biol. , vol.161 , pp. 607-615
    • Wegner, A.1
  • 146
    • 0032479578 scopus 로고    scopus 로고
    • Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation
    • Welch M.D., Rosenblatt J., Skoble J., Portnoy D.A., and Mitchison T.J. Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation. Science 281 (1998) 105-108
    • (1998) Science , vol.281 , pp. 105-108
    • Welch, M.D.1    Rosenblatt, J.2    Skoble, J.3    Portnoy, D.A.4    Mitchison, T.J.5
  • 147
    • 0028584314 scopus 로고
    • Two domains of interaction with calcium binding proteins can be mapped using fragments of calponin
    • Wills F.L., McCubbin W.D., Gimona M., Strasser P., and Kay C.M. Two domains of interaction with calcium binding proteins can be mapped using fragments of calponin. Protein Sci. 3 (1994) 2311-2321
    • (1994) Protein Sci. , vol.3 , pp. 2311-2321
    • Wills, F.L.1    McCubbin, W.D.2    Gimona, M.3    Strasser, P.4    Kay, C.M.5
  • 148
  • 149
    • 0016826292 scopus 로고
    • Evidence for biased bidirectional polymerization of actin filaments using heavy meromyosin prepared by an improved method
    • Woodrum D.T., Rich S.A., and Pollard T.D. Evidence for biased bidirectional polymerization of actin filaments using heavy meromyosin prepared by an improved method. J. Cell Biol. 67 (1975) 231-237
    • (1975) J. Cell Biol. , vol.67 , pp. 231-237
    • Woodrum, D.T.1    Rich, S.A.2    Pollard, T.D.3
  • 150
    • 0032519871 scopus 로고    scopus 로고
    • Differential regional expression and ultrastructural localization of alpha-actinin-2, a putative NMDA receptor-anchoring protein, in rat brain
    • Wyszynski M., Kharazia V., Shanghvi R., Rao A., Beggs A.H., Craig A.M., Weinberg R., and Sheng M. Differential regional expression and ultrastructural localization of alpha-actinin-2, a putative NMDA receptor-anchoring protein, in rat brain. J. Neurosci. 18 (1998) 1383-1392
    • (1998) J. Neurosci. , vol.18 , 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
  • 151
    • 33744949077 scopus 로고    scopus 로고
    • The actin-depolymerizing factor homology and charged/helical domains of drebrin and mAbp1 direct membrane binding and localization via distinct interactions with actin
    • Xu W., and Stamnes M. The actin-depolymerizing factor homology and charged/helical domains of drebrin and mAbp1 direct membrane binding and localization via distinct interactions with actin. J. Biol. Chem. 281 (2006) 11826-11833
    • (2006) J. Biol. Chem. , vol.281 , pp. 11826-11833
    • Xu, W.1    Stamnes, M.2
  • 152
    • 0021827569 scopus 로고
    • Purification and characterization of an F-actin-bundling 55 kDa protein from HeLa cells
    • Yamashiro-Matsumura S., and Matsumura F. Purification and characterization of an F-actin-bundling 55 kDa protein from HeLa cells. J. Biol. Chem. 260 (1985) 5087-5097
    • (1985) J. Biol. Chem. , vol.260 , pp. 5087-5097
    • Yamashiro-Matsumura, S.1    Matsumura, F.2
  • 153
    • 0022535995 scopus 로고
    • Intracellular localization of the 55-kDa actin-bundling protein in cultured cells: spatial relationships with actin, alpha-actinin, tropomyosin, and fimbrin
    • Yamashiro-Matsumura S., and Matsumura F. Intracellular localization of the 55-kDa actin-bundling protein in cultured cells: spatial relationships with actin, alpha-actinin, tropomyosin, and fimbrin. J. Cell Biol. 103 (1986) 631-640
    • (1986) J. Cell Biol. , vol.103 , pp. 631-640
    • Yamashiro-Matsumura, S.1    Matsumura, F.2
  • 154
    • 0022403777 scopus 로고
    • pH control of actin polymerization by cofilin
    • Yonezawa N., Nishida E., and Sakai H. pH control of actin polymerization by cofilin. J. Biol. Chem. 260 (1985) 14410-14412
    • (1985) J. Biol. Chem. , vol.260 , pp. 14410-14412
    • Yonezawa, N.1    Nishida, E.2    Sakai, H.3
  • 155
    • 33751428390 scopus 로고    scopus 로고
    • Myosin-Va facilitates the accumulation of mRNA/protein complex in dendritic spines
    • Yoshimura A., Fujii R., Watanabe Y., Okabe S., Fukui K., and Takumi T. Myosin-Va facilitates the accumulation of mRNA/protein complex in dendritic spines. Curr. Biol. 16 (2006) 2345-2351
    • (2006) Curr. Biol. , vol.16 , pp. 2345-2351
    • Yoshimura, A.1    Fujii, R.2    Watanabe, Y.3    Okabe, S.4    Fukui, K.5    Takumi, T.6
  • 156
    • 16344390935 scopus 로고    scopus 로고
    • A GIT1/PIX/Rac/PAK signaling module regulates spine morphogenesis and synapse formation through MLC
    • Zhang H., Webb D.J., Asmussen H., Niu S., and Horwitz A.F. A GIT1/PIX/Rac/PAK signaling module regulates spine morphogenesis and synapse formation through MLC. J. Neurosci. 25 (2005) 3379-3388
    • (2005) J. Neurosci. , vol.25 , pp. 3379-3388
    • Zhang, H.1    Webb, D.J.2    Asmussen, H.3    Niu, S.4    Horwitz, A.F.5
  • 157
    • 0035879063 scopus 로고    scopus 로고
    • Stages of synapse development defined by dependence on F-actin
    • Zhang W., and Benson D.L. Stages of synapse development defined by dependence on F-actin. J. Neurosci. 21 (2001) 5169-5181
    • (2001) J. Neurosci. , vol.21 , pp. 5169-5181
    • Zhang, W.1    Benson, D.L.2
  • 159
    • 0027293382 scopus 로고
    • Recent quantitative studies of actin filament turnover during cell locomotion
    • Zigmond S.H. Recent quantitative studies of actin filament turnover during cell locomotion. Cell Motil. Cytoskeleton 25 (1993) 309-316
    • (1993) Cell Motil. Cytoskeleton , vol.25 , pp. 309-316
    • Zigmond, S.H.1
  • 160
    • 0030200393 scopus 로고    scopus 로고
    • Evidence for a role of dendritic filopodia in synaptogenesis and spine formation
    • Ziv N.E., and Smith S.J. Evidence for a role of dendritic filopodia in synaptogenesis and spine formation. Neuron 17 (1996) 91-102
    • (1996) Neuron , vol.17 , pp. 91-102
    • Ziv, N.E.1    Smith, S.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.