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Volumn 6, Issue 2, 2003, Pages 127-135

Actin has a molecular scaffolding, not propulsive, role in presynaptic function

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; GREEN FLUORESCENT PROTEIN; LATRUNCULIN A;

EID: 0037317392     PISSN: 10976256     EISSN: None     Source Type: Journal    
DOI: 10.1038/nn1002     Document Type: Article
Times cited : (268)

References (40)
  • 2
    • 0028840159 scopus 로고
    • Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosis
    • Vitale, M.L., Seward, E.P. & Trifaro, J.M. Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosis. Neuron 14, 353-363 (1995).
    • (1995) Neuron , vol.14 , pp. 353-363
    • Vitale, M.L.1    Seward, E.P.2    Trifaro, J.M.3
  • 3
    • 0030921711 scopus 로고    scopus 로고
    • Brain myosin V is a synaptic vesicle-associated motor protein: Evidence for a Ca2+-dependent interaction with the synaptobrevin-synaptophysin complex
    • Prekeris, R. & Terrian, D.M. Brain myosin V is a synaptic vesicle-associated motor protein: evidence for a Ca2+-dependent interaction with the synaptobrevin-synaptophysin complex. J. Cell Biol. 137, 1589-1601 (1997).
    • (1997) J. Cell Biol. , vol.137 , pp. 1589-1601
    • Prekeris, R.1    Terrian, D.M.2
  • 4
    • 0031819385 scopus 로고    scopus 로고
    • Vesicle-associated brain myosin-V can be activated to catalyze actin-based transport
    • Evans, L.L., Lee, A.J., Bridgman, P.C. & Mooseker, M.S. Vesicle-associated brain myosin-V can be activated to catalyze actin-based transport. J. Cell Sci. 111, 2055-2066 (1998).
    • (1998) J. Cell Sci. , vol.111 , pp. 2055-2066
    • Evans, L.L.1    Lee, A.J.2    Bridgman, P.C.3    Mooseker, M.S.4
  • 5
    • 0035067475 scopus 로고    scopus 로고
    • Phagocytosis and the actin cytoskeleton
    • May, R.C. & Machesky, L.M. Phagocytosis and the actin cytoskeleton. J. Cell Sci. 114, 1061-1077 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 1061-1077
    • May, R.C.1    Machesky, L.M.2
  • 6
    • 0035199154 scopus 로고    scopus 로고
    • Actin-based motility of intracellular microbial pathogens
    • Goldberg, M.B. Actin-based motility of intracellular microbial pathogens. Microbiol. Mol. Biol. Rev. 65, 595-626 (2001).
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 595-626
    • Goldberg, M.B.1
  • 7
    • 0033126054 scopus 로고    scopus 로고
    • Endocytic vesicles move at the tips of actin tails in cultured mast cells
    • Merrifield, C.J. et al. Endocytic vesicles move at the tips of actin tails in cultured mast cells. Nat. Cell Biol. 1, 72-74 (1999).
    • (1999) Nat. Cell Biol. , vol.1 , pp. 72-74
    • Merrifield, C.J.1
  • 8
    • 0024595352 scopus 로고
    • The cytoskeletal architecture of the presynaptic terminal and molecular structure of synapsin 1
    • Hirokawa, N., Sobue, K., Kanda, K., Harada, A. & Yorifuji, H. The cytoskeletal architecture of the presynaptic terminal and molecular structure of synapsin 1. J. Cell Biol. 108, 111-126 (1989).
    • (1989) J. Cell Biol. , vol.108 , pp. 111-126
    • Hirokawa, N.1    Sobue, K.2    Kanda, K.3    Harada, A.4    Yorifuji, H.5
  • 9
    • 0024002576 scopus 로고
    • The organization of the cytoplasm at the presynaptic active zone of a central nervous system synapse
    • Landis, D.M.D., Hall, A.K., Weinstein, L.A. & Reese, T.S. The organization of the cytoplasm at the presynaptic active zone of a central nervous system synapse. Neuron 1, 201-209 (1988).
    • (1988) Neuron , vol.1 , pp. 201-209
    • Landis, D.M.D.1    Hall, A.K.2    Weinstein, L.A.3    Reese, T.S.4
  • 10
    • 0026093409 scopus 로고
    • Cytoplasmic architecture of the axon terminal: Filamentous strands specifically associated with synaptic vesicles
    • Gotow, T., Miyaguchi, K. & Hashimoto, P.H. Cytoplasmic architecture of the axon terminal: filamentous strands specifically associated with synaptic vesicles. Neuroscience 40, 587-598 (1991).
    • (1991) Neuroscience , vol.40 , pp. 587-598
    • Gotow, T.1    Miyaguchi, K.2    Hashimoto, P.H.3
  • 11
    • 0032078861 scopus 로고    scopus 로고
    • Rapid actin-based plasticity in dendritic spines
    • Fischer, M., Kaech, S., Knutti, D. & Matus, A. Rapid actin-based plasticity in dendritic spines. Neuron 20, 847-854 (1998).
    • (1998) Neuron , vol.20 , pp. 847-854
    • Fischer, M.1    Kaech, S.2    Knutti, D.3    Matus, A.4
  • 12
    • 0035977120 scopus 로고    scopus 로고
    • Remodeling of synaptic actin induced by photoconductive stimulation
    • Colicos, M.A., Collins, B.E., Sailor, M.J. & Goda, Y. Remodeling of synaptic actin induced by photoconductive stimulation. Cell 107, 605-616 (2001).
    • (2001) Cell , vol.107 , pp. 605-616
    • Colicos, M.A.1    Collins, B.E.2    Sailor, M.J.3    Goda, Y.4
  • 13
    • 0033681170 scopus 로고    scopus 로고
    • Actin-dependent regulation of neurotransmitter release at central synapses
    • Morales, M., Colicos, M.A. & Goda, Y. Actin-dependent regulation of neurotransmitter release at central synapses. Neuron 27, 539-550 (2000).
    • (2000) Neuron , vol.27 , pp. 539-550
    • Morales, M.1    Colicos, M.A.2    Goda, Y.3
  • 14
    • 0030042310 scopus 로고    scopus 로고
    • Effect of cytochalasin treatment in short-term synaptic plasticity at developing neuromuscular junctions in frogs
    • Wang, X.H., Zheng, LQ. & Poo, M.M. Effect of cytochalasin treatment in short-term synaptic plasticity at developing neuromuscular junctions in frogs. J. Physiol. 491, 187-195 (1996).
    • (1996) J. Physiol. , vol.491 , pp. 187-195
    • Wang, X.H.1    Zheng, L.Q.2    Poo, M.M.3
  • 15
    • 0031884084 scopus 로고    scopus 로고
    • Actin disassembles reversibly during electrically induced recycling of synaptic vesicles in cultured neurons
    • Bernstein, B.W., DeWit, M. & Bamburg, J.R. Actin disassembles reversibly during electrically induced recycling of synaptic vesicles in cultured neurons. Brain Res. Mol. Brain Res. 53, 236-251 (1998).
    • (1998) Brain Res. Mol. Brain Res. , vol.53 , pp. 236-251
    • Bernstein, B.W.1    DeWit, M.2    Bamburg, J.R.3
  • 16
    • 0034659515 scopus 로고    scopus 로고
    • Disruption of actin impedes transmitter release in snake motor terminals
    • Cole, J.C., Villa, B.R. & Wilkinson, R.S. Disruption of actin impedes transmitter release in snake motor terminals. J. Physiol. 525, 579-586 (2000).
    • (2000) J. Physiol. , vol.525 , pp. 579-586
    • Cole, J.C.1    Villa, B.R.2    Wilkinson, R.S.3
  • 17
    • 0032077286 scopus 로고    scopus 로고
    • Two distinct pools of synaptic vesicles in single presynaptic boutons in temperature-sensitive drosophila mutant, shibire
    • Kuromi, H. & Kidokoro, Y. Two distinct pools of synaptic vesicles in single presynaptic boutons in temperature-sensitive drosophila mutant, shibire. Neuron 20, 917-925 (1998).
    • (1998) Neuron , vol.20 , pp. 917-925
    • Kuromi, H.1    Kidokoro, Y.2
  • 18
    • 0037195182 scopus 로고    scopus 로고
    • Impaired recycling of synaptic vesicles after acute perturbation of the presynaptic actin cytoskeleton
    • Shupliakov, O. et al. Impaired recycling of synaptic vesicles after acute perturbation of the presynaptic actin cytoskeleton. Proc. Natl. Acad. Sci. USA 99, 14476-14481 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14476-14481
    • Shupliakov, O.1
  • 19
    • 0032517822 scopus 로고    scopus 로고
    • Calcium and protein kinase C regulate the actin cytoskeleton in the synaptic terminal of retinal bipolar cells
    • Job, C. & Lagnado, L. Calcium and protein kinase C regulate the actin cytoskeleton in the synaptic terminal of retinal bipolar cells. J. Cell Biol. 143, 1661-1672 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 1661-1672
    • Job, C.1    Lagnado, L.2
  • 20
    • 0034964906 scopus 로고    scopus 로고
    • Homo-FRET microscopy in living cells to measure monomer-dimer transition of GFP-tagged proteins
    • Gautier, I. et al. Homo-FRET microscopy in living cells to measure monomer-dimer transition of GFP-tagged proteins. Biophys. J. 80, 3000-3008 (2001).
    • (2001) Biophys. J. , vol.80 , pp. 3000-3008
    • Gautier, I.1
  • 21
    • 0030909829 scopus 로고    scopus 로고
    • Transfected muscle and non-muscle actins are differentially sorted by cultured smooth muscle and non-muscle cells
    • Mounier, N., Perriard, J.C., Gabbiani, G. & Chaponnier, C. Transfected muscle and non-muscle actins are differentially sorted by cultured smooth muscle and non-muscle cells. J. Cell. Sci. 110, 839-846 (1997).
    • (1997) J. Cell. Sci. , vol.110 , pp. 839-846
    • Mounier, N.1    Perriard, J.C.2    Gabbiani, G.3    Chaponnier, C.4
  • 23
    • 0029062202 scopus 로고
    • Vesicle pool mobilization during action potential firing
    • Ryan, T.A. & Smith, S.J. Vesicle pool mobilization during action potential firing. Neuron, 14, 983-989 (1995).
    • (1995) Neuron , vol.14 , pp. 983-989
    • Ryan, T.A.1    Smith, S.J.2
  • 24
    • 0023142377 scopus 로고
    • Inhibition of actin polymerization by latrunculin A
    • Coue, M., Brenner, S.L., Spector, I. & Korn, E.D. Inhibition of actin polymerization by latrunculin A. FEBS Lett. 213, 316-318 (1987).
    • (1987) FEBS Lett. , vol.213 , pp. 316-318
    • Coue, M.1    Brenner, S.L.2    Spector, I.3    Korn, E.D.4
  • 25
    • 0024360298 scopus 로고
    • Latrunculins-novel marine macrolides that disrupt microfilament organization and affect cell growth: I. Comparison with cytochalasin D
    • Spector, I., Shochet, N.R., Blasberger, D. & Kashman, Y. Latrunculins-novel marine macrolides that disrupt microfilament organization and affect cell growth: I. Comparison with cytochalasin D. Cell Motil. Cytoskeleton 13, 127-144 (1989).
    • (1989) Cell Motil. Cytoskeleton , vol.13 , pp. 127-144
    • Spector, I.1    Shochet, N.R.2    Blasberger, D.3    Kashman, Y.4
  • 26
    • 0035229253 scopus 로고    scopus 로고
    • Jasplakinolide. An actin-specific reagent that promotes actin polymerization
    • Holzinger, A. Jasplakinolide. An actin-specific reagent that promotes actin polymerization. Methods Mol. Biol. 161, 109-120 (2001).
    • (2001) Methods Mol. Biol. , vol.161 , pp. 109-120
    • Holzinger, A.1
  • 27
    • 0032054473 scopus 로고    scopus 로고
    • Role of actin in anchoring postsynaptic receptors in culture hippocampal neurons: Differential attachment of NMDA versus AMPA receptors
    • Allison, D.W., Gelfand, V.I., Spector, I. & Craig, A.M. Role of actin in anchoring postsynaptic receptors in culture hippocampal neurons: differential attachment of NMDA versus AMPA receptors. J. Neurosci. 18, 2423-2436 (1998).
    • (1998) J. Neurosci. , vol.18 , pp. 2423-2436
    • Allison, D.W.1    Gelfand, V.I.2    Spector, I.3    Craig, A.M.4
  • 28
    • 0032500053 scopus 로고    scopus 로고
    • Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins
    • Miesenbock, G., De Angelis, D.A. & Rothman, J.E. Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins. Nature 394, 192-195 (1998).
    • (1998) Nature , vol.394 , pp. 192-195
    • Miesenbock, G.1    De Angelis, D.A.2    Rothman, J.E.3
  • 29
    • 0033803597 scopus 로고    scopus 로고
    • The use of pHluorins for optical detection of presynaptic activity
    • Sankaranarayanan, S., De Angelis, D., Rothman, J.E. & Ryan, T.A. The use of pHluorins for optical detection of presynaptic activity. Biophys. J. 79, 2199-2208 (2000).
    • (2000) Biophys. J. , vol.79 , pp. 2199-2208
    • Sankaranarayanan, S.1    De Angelis, D.2    Rothman, J.E.3    Ryan, T.A.4
  • 30
    • 0033786834 scopus 로고    scopus 로고
    • Real-time measurements of vesicle-SNARE recycling in synapses of the central nervous system
    • Sankaranarayanan, S., & Ryan, T.A. Real-time measurements of vesicle-SNARE recycling in synapses of the central nervous system. Nat. Cell Biol. 2, 197-204 (2000).
    • (2000) Nat. Cell Biol. , vol.2 , pp. 197-204
    • Sankaranarayanan, S.1    Ryan, T.A.2
  • 31
    • 0035195395 scopus 로고    scopus 로고
    • Synapsin dispersion and reclustering during synaptic activity
    • Chi, P., Greengard, P. & Ryan, T.A. Synapsin dispersion and reclustering during synaptic activity. Nat. Neurosci. 4, 1187-1193 (2001).
    • (2001) Nat. Neurosci. , vol.4 , pp. 1187-1193
    • Chi, P.1    Greengard, P.2    Ryan, T.A.3
  • 32
    • 0033611709 scopus 로고    scopus 로고
    • Protein-protein interaction and protein modules in the control of neurotransmitter release
    • Benfenati, E, Onofri, E & Giovedi, S. Protein-protein interaction and protein modules in the control of neurotransmitter release. Phil. Trans. R. Soc. Lond. 354, 243-257 (1999).
    • (1999) Phil. Trans. R. Soc. Lond. , vol.354 , pp. 243-257
    • Benfenati, E.1    Onofri, E.2    Giovedi, S.3
  • 33
    • 0034614942 scopus 로고    scopus 로고
    • Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion
    • Chan, A.Y., Bailly, M., Zebda, N., Segall, J.E. & Condeelis, J.S. Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion. J. Cell Biol. 148, 531-542 (2000).
    • (2000) J. Cell Biol. , vol.148 , pp. 531-542
    • Chan, A.Y.1    Bailly, M.2    Zebda, N.3    Segall, J.E.4    Condeelis, J.S.5
  • 34
    • 0026045382 scopus 로고
    • Kinetic analysis of F-actin depolymerization in polymorphonuclear leukocyte lysates indicates that chemoattractant stimulation increases actin filament number without altering the filament length and distribution
    • Cano, M., Lauffenburger, D.A. & Zigmond, S.H. Kinetic analysis of F-actin depolymerization in polymorphonuclear leukocyte lysates indicates that chemoattractant stimulation increases actin filament number without altering the filament length and distribution. J. Cell Biol. 115, 677-687 (1995).
    • (1995) J. Cell Biol. , vol.115 , pp. 677-687
    • Cano, M.1    Lauffenburger, D.A.2    Zigmond, S.H.3
  • 36
    • 0035879063 scopus 로고    scopus 로고
    • Stages of synapse development defined by dependence on F-actin
    • Zhang, W. & Benson, D.L. Stages of synapse development defined by dependence on F-actin. J. Neurosci. 21, 5169-5181 (2001).
    • (2001) J. Neurosci. , vol.21 , pp. 5169-5181
    • Zhang, W.1    Benson, D.L.2
  • 37
    • 0033518315 scopus 로고    scopus 로고
    • The endocytic machinery in nerve terminals surrounds sites of exocytosis
    • Roos, J. & Kelly, R.B. The endocytic machinery in nerve terminals surrounds sites of exocytosis. Curr. Biol. 9, 1411-1414 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 1411-1414
    • Roos, J.1    Kelly, R.B.2
  • 38
    • 0032919866 scopus 로고    scopus 로고
    • Syndapin I a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein
    • Qualmann, B., Roos, J., DiGregorio, P.J. & Kelly, R.B. Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein. Mol. Biol. Cell 10, 501-513 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 501-513
    • Qualmann, B.1    Roos, J.2    DiGregorio, P.J.3    Kelly, R.B.4
  • 40
    • 0036468381 scopus 로고    scopus 로고
    • Coupling actin dynamics and membrane dynamics during endocytosis
    • Schafer, D.A. Coupling actin dynamics and membrane dynamics during endocytosis. Curr. Opin. Cell Biol. 14, 76-81 (2002).
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 76-81
    • Schafer, D.A.1


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