메뉴 건너뛰기




Volumn 17, Issue 11, 2006, Pages 4709-4719

Synaptic vesicle mobility and presynaptic F-actin are disrupted in a N-ethylmaleimide-sensitive factor allele of Drosophila

Author keywords

[No Author keywords available]

Indexed keywords

F ACTIN; N ETHYLMALEIMIDE SENSITIVE FACTOR; N ETHYLMALEIMIDE SENSITIVE FACTOR 2; UNCLASSIFIED DRUG;

EID: 33750521346     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E06-03-0253     Document Type: Article
Times cited : (31)

References (57)
  • 2
    • 0031884084 scopus 로고    scopus 로고
    • Actin disassembles reversibly during electrically induced recycling of synaptic vesicles in cultured neurons
    • Bernstein, B. W., DeWit, M., and Bamburg, J. R. (1998). Actin disassembles reversibly during electrically induced recycling of synaptic vesicles in cultured neurons. Mol. Brain Res. 53, 236-250.
    • (1998) Mol. Brain Res. , vol.53 , pp. 236-250
    • Bernstein, B.W.1    Dewit, M.2    Bamburg, J.R.3
  • 3
    • 0000930533 scopus 로고
    • Purification of an N-ethylmaleimide-sensitive protein catalyzing vesicular transport
    • Block, M. R., Glick, B. S., Wilcox, C. A., Wieland, F. T., and Rothman, J. E. (1988). Purification of an N-ethylmaleimide-sensitive protein catalyzing vesicular transport. Proc. Natl. Acad. Sci. USA 85, 7852-7856.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7852-7856
    • Block, M.R.1    Glick, B.S.2    Wilcox, C.A.3    Wieland, F.T.4    Rothman, J.E.5
  • 4
    • 0029087488 scopus 로고
    • Identification of a second homolog of N-ethylmaleimide-sensitive fusion protein that is expressed in the nervous system and secretory tissues of Drosophila
    • Boulianne, G. L., and Trimble, W. S. (1995). Identification of a second homolog of N-ethylmaleimide-sensitive fusion protein that is expressed in the nervous system and secretory tissues of Drosophila. Proc. Natl. Acad. Sci. USA 92, 7095-7099.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7095-7099
    • Boulianne, G.L.1    Trimble, W.S.2
  • 5
    • 0028967310 scopus 로고
    • Swinholide-A microfilament disrupting marine toxin that stabilizes actin dimers and severs actin-filaments
    • Bubb, M. R., Spector, I., Bershadsky, A. D., and Korn, E. D. (1995). Swinholide-A microfilament disrupting marine toxin that stabilizes actin dimers and severs actin-filaments. J. Biol. Chem. 270, 3463-3466.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3463-3466
    • Bubb, M.R.1    Spector, I.2    Bershadsky, A.D.3    Korn, E.D.4
  • 6
    • 0034659515 scopus 로고    scopus 로고
    • Disruption of actin impedes transmitter release in snake motor terminals
    • Cole, J. C., Villa, B. R., and Wilkinson, R. S. (2000). Disruption of actin impedes transmitter release in snake motor terminals. J. Physiol. 525(Pt 3), 579-586.
    • (2000) J. Physiol. , vol.525 , Issue.PART 3 , pp. 579-586
    • Cole, J.C.1    Villa, B.R.2    Wilkinson, R.S.3
  • 7
    • 0035977051 scopus 로고    scopus 로고
    • Binding of the beta2 adrenergic receptor to N-ethylmaleimide-sensitive factor regulates receptor recycling
    • Cong, M., Perry, S. J., Hu, L. A., Hanson, P. I., Claing, A., and Lefkowitz, R. J. (2001). Binding of the beta2 adrenergic receptor to N-ethylmaleimide-sensitive factor regulates receptor recycling. J. Biol. Chem. 276, 45145-45152.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45145-45152
    • Cong, M.1    Perry, S.J.2    Hu, L.A.3    Hanson, P.I.4    Claing, A.5    Lefkowitz, R.J.6
  • 8
    • 0034045608 scopus 로고    scopus 로고
    • The actin cytoskeleton and neurotransmitter release: An overview
    • Doussau, F., and Augustine, G. J. (2000). The actin cytoskeleton and neurotransmitter release: an overview. Biochimie 82, 353-363.
    • (2000) Biochimie , vol.82 , pp. 353-363
    • Doussau, F.1    Augustine, G.J.2
  • 9
    • 0034663146 scopus 로고    scopus 로고
    • F-actin is concentrated in nonrelease domains at frog neuromuscular junctions
    • Dunaevsky, A., and Connor, E. A. (2000). F-actin is concentrated in nonrelease domains at frog neuromuscular junctions. J. Neurosci. 20, 6007-6012.
    • (2000) J. Neurosci. , vol.20 , pp. 6007-6012
    • Dunaevsky, A.1    Connor, E.A.2
  • 10
    • 0031281917 scopus 로고    scopus 로고
    • GFP-moesin illuminates actin cytoskeleton dynamics in living tissue and demonstrates cell shape changes during morphogenesis in Drosophila
    • Edwards, K. A., Demsky, M., Montague, R. A., Weymouth, N., and Kiehart, D. P. (1997). GFP-moesin illuminates actin cytoskeleton dynamics in living tissue and demonstrates cell shape changes during morphogenesis in Drosophila. Dev. Biol. 191, 103-117.
    • (1997) Dev. Biol. , vol.191 , pp. 103-117
    • Edwards, K.A.1    Demsky, M.2    Montague, R.A.3    Weymouth, N.4    Kiehart, D.P.5
  • 11
    • 0037389872 scopus 로고    scopus 로고
    • Control of growth cone motility and morphology by LIM kinase and Slingshot via phosphorylation and dephosphorylation of cofilin
    • Endo, M., Ohashi, K., Sasaki, Y., Goshima, Y., Niwa, R., Uemura, T., and Mizuno, K. (2003). Control of growth cone motility and morphology by LIM kinase and Slingshot via phosphorylation and dephosphorylation of cofilin. J. Neurosci. 23, 2527-2537.
    • (2003) J. Neurosci. , vol.23 , pp. 2527-2537
    • Endo, M.1    Ohashi, K.2    Sasaki, Y.3    Goshima, Y.4    Niwa, R.5    Uemura, T.6    Mizuno, K.7
  • 12
    • 0034052830 scopus 로고    scopus 로고
    • Synaptic localization and restricted diffusion of a Drosophila neuronal synaptobrevin-green fluorescent protein chimera in vivo
    • Estes, P. S., Ho, G. L., Narayanan, R., and Ramaswami, M. (2000). Synaptic localization and restricted diffusion of a Drosophila neuronal synaptobrevin-green fluorescent protein chimera in vivo. J. Neurogenet. 23, 233-255.
    • (2000) J. Neurogenet. , vol.23 , pp. 233-255
    • Estes, P.S.1    Ho, G.L.2    Narayanan, R.3    Ramaswami, M.4
  • 13
    • 0038348755 scopus 로고    scopus 로고
    • Small-molecule inhibitors of actin dynamics and cell motility
    • Fenteany, G., and Zhu, S. T. (2003). Small-molecule inhibitors of actin dynamics and cell motility. Curr. Topics Med. Chem. 3, 593-616.
    • (2003) Curr. Topics Med. Chem. , vol.3 , pp. 593-616
    • Fenteany, G.1    Zhu, S.T.2
  • 15
    • 3843100611 scopus 로고    scopus 로고
    • Flies lacking all synapsins are unexpectedly healthy but are impaired in complex behaviour
    • Godenschwege, T. A., et al. (2004). Flies lacking all synapsins are unexpectedly healthy but are impaired in complex behaviour. Eur. J. Neurosci. 20, 611-622.
    • (2004) Eur. J. Neurosci. , vol.20 , pp. 611-622
    • Godenschwege, T.A.1
  • 16
    • 0035023269 scopus 로고    scopus 로고
    • Partitioning of N-ethylmaleimide-sensitive fusion (NSF) protein function in Drosophila melanogaster: DNSF1 is required in the nervous system, and dNSF2 is required in mesoderm
    • Golby, J. A., Tolar, L. A., and Pallanck, L. (2001). Partitioning of N-ethylmaleimide-sensitive fusion (NSF) protein function in Drosophila melanogaster: dNSF1 is required in the nervous system, and dNSF2 is required in mesoderm. Genetics 158, 265-278.
    • (2001) Genetics , vol.158 , pp. 265-278
    • Golby, J.A.1    Tolar, L.A.2    Pallanck, L.3
  • 17
    • 0034668855 scopus 로고    scopus 로고
    • Identification of Rab6 as an N-ethylmaleimide-sensitive fusion protein-binding protein
    • Han, S. Y., Park, D. Y., Park, S. D., and Hong, S. H. (2000). Identification of Rab6 as an N-ethylmaleimide-sensitive fusion protein-binding protein. Biochem. J. 352(Pt 1), 165-173.
    • (2000) Biochem. J. , vol.352 , Issue.PART 1 , pp. 165-173
    • Han, S.Y.1    Park, D.Y.2    Park, S.D.3    Hong, S.H.4
  • 18
    • 0029885396 scopus 로고    scopus 로고
    • Synaptic vesicle movements monitored by fluorescence recovery after photobleaching in nerve terminals stained with FM1-43
    • Henkel, A. W., Simpson, L. L., Ridge, R. M., and Betz, W. J. (1996). Synaptic vesicle movements monitored by fluorescence recovery after photobleaching in nerve terminals stained with FM1-43. J. Neurosci. 16, 3960-3967.
    • (1996) J. Neurosci. , vol.16 , pp. 3960-3967
    • Henkel, A.W.1    Simpson, L.L.2    Ridge, R.M.3    Betz, W.J.4
  • 20
    • 1242310783 scopus 로고    scopus 로고
    • High mobility of vesicles supports continuous exocytosis at a ribbon synapse
    • Holt, M., Cooke, A., Neef, A., and Lagnado, L. (2004). High mobility of vesicles supports continuous exocytosis at a ribbon synapse. Curr. Biol. 14, 173-183.
    • (2004) Curr. Biol. , vol.14 , pp. 173-183
    • Holt, M.1    Cooke, A.2    Neef, A.3    Lagnado, L.4
  • 21
    • 0029911064 scopus 로고    scopus 로고
    • Kinesin mutations cause motor neuron disease phenotypes by disrupting fast axonal transport in Drosophila
    • Hurd, D. D., and Saxton, W. M. (1996). Kinesin mutations cause motor neuron disease phenotypes by disrupting fast axonal transport in Drosophila. Genetics 244, 1075-1085.
    • (1996) Genetics , vol.244 , pp. 1075-1085
    • Hurd, D.D.1    Saxton, W.M.2
  • 22
    • 0032535040 scopus 로고    scopus 로고
    • Synaptic physiology and ultrastructure in comatose mutants define an in vivo role for NSF in neurotransmitter release
    • Kawasaki, F., Mattiuz, A. M., and Ordway, R. W. (1998). Synaptic physiology and ultrastructure in comatose mutants define an in vivo role for NSF in neurotransmitter release. J. Neurosci. 18, 10241-10249.
    • (1998) J. Neurosci. , vol.18 , pp. 10241-10249
    • Kawasaki, F.1    Mattiuz, A.M.2    Ordway, R.W.3
  • 23
    • 3242680909 scopus 로고    scopus 로고
    • Dap160/intersectin acts as a stabilizing scaffold required for synaptic development and vesicle endocytosis
    • Koh, T. W., Verstreken, P., and Bellen, H. J. (2004). Dap160/intersectin acts as a stabilizing scaffold required for synaptic development and vesicle endocytosis. Neuron 43, 193-205.
    • (2004) Neuron , vol.43 , pp. 193-205
    • Koh, T.W.1    Verstreken, P.2    Bellen, H.J.3
  • 24
    • 0029812769 scopus 로고    scopus 로고
    • Mobility of synaptic vesicles in nerve endings monitored by recovery from photobleaching of synaptic vesicle-associated fluorescence
    • Kraszewski, K., Daniell, L., Mundigl, O., and DeCamilli, P. (1996). Mobility of synaptic vesicles in nerve endings monitored by recovery from photobleaching of synaptic vesicle-associated fluorescence. J. Neurosci. 16, 5905-5913.
    • (1996) J. Neurosci. , vol.16 , pp. 5905-5913
    • Kraszewski, K.1    Daniell, L.2    Mundigl, O.3    Decamilli, P.4
  • 25
    • 0032077286 scopus 로고    scopus 로고
    • Two distinct pools of synaptic vesicles in single presynaptic boutons in a temperature-sensitive Drosophila mutant, shibire
    • Kuromi, H., and Kidokoro, Y. (1998). Two distinct pools of synaptic vesicles in single presynaptic boutons in a temperature-sensitive Drosophila mutant, shibire. Neuron 20, 917-925.
    • (1998) Neuron , vol.20 , pp. 917-925
    • Kuromi, H.1    Kidokoro, Y.2
  • 26
    • 20044396187 scopus 로고    scopus 로고
    • A generic screen for suppressors of Drosophila NSF2 neuromuscular junction overgrowth
    • Laviolette, M. J., Nunes, P., Peyre, J. B., Aigaki, T., and Stewart, B. A. (2005). A generic screen for suppressors of Drosophila NSF2 neuromuscular junction overgrowth. Genetics 170, 779-792.
    • (2005) Genetics , vol.170 , pp. 779-792
    • Laviolette, M.J.1    Nunes, P.2    Peyre, J.B.3    Aigaki, T.4    Stewart, B.A.5
  • 27
    • 33750496816 scopus 로고    scopus 로고
    • Novel putative targets of N-ethylmaleimide sensitive fusion protein (NSF) and alpha/beta soluble NSF attachment proteins (SNAPs) include the Pak-binding nudeotide exchange factor betaPIX
    • 10.100/jcb.20998
    • Martin, H. G., Henley, J. M., and Meyer, G. (2006). Novel putative targets of N-ethylmaleimide sensitive fusion protein (NSF) and alpha/beta soluble NSF attachment proteins (SNAPs) include the Pak-binding nudeotide exchange factor betaPIX. J. Cell. Biochem., 10.100/jcb.20998.
    • (2006) J. Cell. Biochem.
    • Martin, H.G.1    Henley, J.M.2    Meyer, G.3
  • 28
    • 0033574530 scopus 로고    scopus 로고
    • Identification of NSF as a beta-arrestin1-binding protein. Implications for beta2-adrenergic receptor regulation
    • McDonald, P. H., Cote, N. L., Lin, F. T., Premont, R. T., Pitcher, J. A., and Lefkowitz, R. J. (1999). Identification of NSF as a beta-arrestin1-binding protein. Implications for beta2-adrenergic receptor regulation. J. Biol. Chem. 274, 10677-10680.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10677-10680
    • McDonald, P.H.1    Cote, N.L.2    Lin, F.T.3    Premont, R.T.4    Pitcher, J.A.5    Lefkowitz, R.J.6
  • 30
    • 0033681170 scopus 로고    scopus 로고
    • Actin-dependent regulation of neurotransmitter release at central synapses
    • Morales, M., Colicos, M. A., and Goda, Y. (2000). Actin-dependent regulation of neurotransmitter release at central synapses. Neuron 27, 539-550.
    • (2000) Neuron , vol.27 , pp. 539-550
    • Morales, M.1    Colicos, M.A.2    Goda, Y.3
  • 31
    • 0037166941 scopus 로고    scopus 로고
    • Sequential SNARE disassembly and GATE-16-GOS-28 complex assembly mediated by distinct NSF activities drives Golgi membrane fusion
    • Muller, J. M., Shorter, J., Newman, R., Deinhardt, K., Sagiv, Y., Elazar, Z., Warren, G., and Shima, D. T. (2002). Sequential SNARE disassembly and GATE-16-GOS-28 complex assembly mediated by distinct NSF activities drives Golgi membrane fusion. J. Cell Biol. 157, 1161-1173.
    • (2002) J. Cell Biol. , vol.157 , pp. 1161-1173
    • Muller, J.M.1    Shorter, J.2    Newman, R.3    Deinhardt, K.4    Sagiv, Y.5    Elazar, Z.6    Warren, G.7    Shima, D.T.8
  • 33
    • 0029163609 scopus 로고
    • Distinct roles for N-ethylmaleimide-sensitive fusion protein (NSF) suggested by the identification of a second Drosophila NSF homolog
    • Pallanck, L., Ordway, R. W., Ramaswami, M., Chi, W. Y., Krishnan, K. S., and Ganetzky, B. (1995). Distinct roles for N-ethylmaleimide-sensitive fusion protein (NSF) suggested by the identification of a second Drosophila NSF homolog. J. Biol. Chem. 270, 18742-18744.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18742-18744
    • Pallanck, L.1    Ordway, R.W.2    Ramaswami, M.3    Chi, W.Y.4    Krishnan, K.S.5    Ganetzky, B.6
  • 34
    • 0033695839 scopus 로고    scopus 로고
    • Two endocytic recycling routes selectively fill two vesicle pools in frog motor nerve terminals
    • Richards, D. A., Guatimosim, C., and Betz, W. J. (2000). Two endocytic recycling routes selectively fill two vesicle pools in frog motor nerve terminals. Neuron 27, 551-559.
    • (2000) Neuron , vol.27 , pp. 551-559
    • Richards, D.A.1    Guatimosim, C.2    Betz, W.J.3
  • 35
    • 2942689878 scopus 로고    scopus 로고
    • Effects of wortmannin and latrunculin a on slow endocytosis at the frog neuromuscular junction
    • Richards, D. A., Rizzoli, S. O., and Betz, W. J. (2004). Effects of wortmannin and latrunculin A on slow endocytosis at the frog neuromuscular junction. J. Physiol. 557, 77-91.
    • (2004) J. Physiol. , vol.557 , pp. 77-91
    • Richards, D.A.1    Rizzoli, S.O.2    Betz, W.J.3
  • 37
    • 0037320809 scopus 로고    scopus 로고
    • Involvement of actin polymerization in vesicle recruitment at the calyx of Held synapse
    • Sakaba, T., and Neher, E. (2003). Involvement of actin polymerization in vesicle recruitment at the calyx of Held synapse. J. Neurosci. 23, 837-846.
    • (2003) J. Neurosci. , vol.23 , pp. 837-846
    • Sakaba, T.1    Neher, E.2
  • 38
    • 0037317392 scopus 로고    scopus 로고
    • Actin has a molecular scaffolding, not propulsive, role in presynaptic function
    • Sankaranarayanan, S., Atluri, P. P., and Ryan, T. A. (2003). Actin has a molecular scaffolding, not propulsive, role in presynaptic function. Nat. Neurosci. 6, 127-135.
    • (2003) Nat. Neurosci. , vol.6 , pp. 127-135
    • Sankaranarayanan, S.1    Atluri, P.P.2    Ryan, T.A.3
  • 40
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Sollner, T., Bennett, M. K., Whiteheart, S. W., Scheller, R. H., and Rothman, J. E. (1993a). A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 75, 409-418.
    • (1993) Cell , vol.75 , pp. 409-418
    • Sollner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 42
    • 0032143945 scopus 로고    scopus 로고
    • Interaction of the N-ethylmaleimide-sensitive factor with AMPA receptors
    • Song, I., Kamboj, S., Xia, J., Dong, H., Liao, D., and Huganir, R. L. (1998). Interaction of the N-ethylmaleimide-sensitive factor with AMPA receptors. Neuron 21, 393-400.
    • (1998) Neuron , vol.21 , pp. 393-400
    • Song, I.1    Kamboj, S.2    Xia, J.3    Dong, H.4    Liao, D.5    Huganir, R.L.6
  • 43
    • 0032829103 scopus 로고    scopus 로고
    • New anti-actin drugs in the study of the organization and function of the actin cytoskeleton
    • Spector, I., Braet, F., Shochet, N. R., and Bubb, M. R. (1999). New anti-actin drugs in the study of the organization and function of the actin cytoskeleton. Microsc. Res. Tech. 47, 18-37.
    • (1999) Microsc. Res. Tech. , vol.47 , pp. 18-37
    • Spector, I.1    Braet, F.2    Shochet, N.R.3    Bubb, M.R.4
  • 44
    • 0028483237 scopus 로고
    • Improved stability of Drosophila larval neuromuscular preparations in haemolymph-like physiological solutions
    • Stewart, B. A., Atwood, H. L., Renger, J. J., Wang, J., and Wu, C. F. (1994). Improved stability of Drosophila larval neuromuscular preparations in haemolymph-like physiological solutions. J. Comp. Physiol. A 175, 179-191.
    • (1994) J. Comp. Physiol. A , vol.175 , pp. 179-191
    • Stewart, B.A.1    Atwood, H.L.2    Renger, J.J.3    Wang, J.4    Wu, C.F.5
  • 45
    • 0037096093 scopus 로고    scopus 로고
    • Dominant-negative NSF2 disrupts the structure and function of Drosophila neuromuscular synapses
    • Stewart, B. A., Mohtashami, M., Rivlin, P., Deitcher, D. L., Trimble, W. S., and Boulianne, G. L. (2002). Dominant-negative NSF2 disrupts the structure and function of Drosophila neuromuscular synapses. J. Neurobiol. 51, 261-271.
    • (2002) J. Neurobiol. , vol.51 , pp. 261-271
    • Stewart, B.A.1    Mohtashami, M.2    Rivlin, P.3    Deitcher, D.L.4    Trimble, W.S.5    Boulianne, G.L.6
  • 48
    • 20044389482 scopus 로고    scopus 로고
    • Disruption of synaptic development and ultrastructure by Drosophila NSF2 alleles
    • Stewart, B. A., Pearce, J., Bajec, M. R., and Khorana, R. (2005). Disruption of synaptic development and ultrastructure by Drosophila NSF2 alleles. J. Comp. Neurol. 488, 101-111.
    • (2005) J. Comp. Neurol. , vol.488 , pp. 101-111
    • Stewart, B.A.1    Pearce, J.2    Bajec, M.R.3    Khorana, R.4
  • 49
    • 0036745669 scopus 로고    scopus 로고
    • Cell polarity and locomotion, as well as endocytosis, depend on NSF
    • Thompson, C. R., and Bretscher, M. S. (2002). Cell polarity and locomotion, as well as endocytosis, depend on NSF. Development 129, 4185-4192.
    • (2002) Development , vol.129 , pp. 4185-4192
    • Thompson, C.R.1    Bretscher, M.S.2
  • 52
    • 0030042310 scopus 로고    scopus 로고
    • Effects of cytochalasin treatment on short-term synaptic plasticity at developing neuromuscular junctions in frogs
    • Wang, X. H., Zheng, J. Q., and Poo, M. M. (1996). Effects of cytochalasin treatment on short-term synaptic plasticity at developing neuromuscular junctions in frogs. J. Physiol. 491, 187-195.
    • (1996) J. Physiol. , vol.491 , pp. 187-195
    • Wang, X.H.1    Zheng, J.Q.2    Poo, M.M.3
  • 53
    • 0026720008 scopus 로고
    • Soluble N-ethylmaleimide-sensitive fusion attachment proteins (SNAPs) bind to a multi-SNAP receptor complex in Golgi membranes
    • Whiteheart, S. W., Brunner, M., Wilson, D. W., Wiedmann, M., and Rothman, J. E. (1992). Soluble N-ethylmaleimide-sensitive fusion attachment proteins (SNAPs) bind to a multi-SNAP receptor complex in Golgi membranes. J. Biol. Chem. 267, 12239-12243.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12239-12243
    • Whiteheart, S.W.1    Brunner, M.2    Wilson, D.W.3    Wiedmann, M.4    Rothman, J.E.5
  • 54
    • 0028132782 scopus 로고
    • N-ethylmaleimide-sensitive fusion protein: A trimeric ATPase whose hydrolysis of ATP is required for membrane fusion
    • Whiteheart, S. W., Rossnagel, K., Buhrow, S. A., Brunner, M., Jaenicke, R., and Rothman, J. E. (1994). N-ethylmaleimide-sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion. J. Cell Biol. 126, 945-954.
    • (1994) J. Cell Biol. , vol.126 , pp. 945-954
    • Whiteheart, S.W.1    Rossnagel, K.2    Buhrow, S.A.3    Brunner, M.4    Jaenicke, R.5    Rothman, J.E.6
  • 55
    • 0032568798 scopus 로고    scopus 로고
    • LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion
    • Xu, Z., Sato, K., and Wickner, W. (1998). LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion. Cell 93, 1125-1134.
    • (1998) Cell , vol.93 , pp. 1125-1134
    • Xu, Z.1    Sato, K.2    Wickner, W.3
  • 56
    • 0032441070 scopus 로고    scopus 로고
    • Synaptic vesicle size and number are regulated by a clathrin adaptor protein required for endocytosis
    • In Process Citation
    • Zhang, B., Koh, Y. H., Beckstead, R. B., Budnik, V., Ganetzky, B., and Bellen, H. J. (1998). Synaptic vesicle size and number are regulated by a clathrin adaptor protein required for endocytosis [In Process Citation]. Neuron 21, 1465-1475.
    • (1998) Neuron , vol.21 , pp. 1465-1475
    • Zhang, B.1    Koh, Y.H.2    Beckstead, R.B.3    Budnik, V.4    Ganetzky, B.5    Bellen, H.J.6
  • 57
    • 0036743680 scopus 로고    scopus 로고
    • Living synaptic vesicle marker: Synaptotagmin-GFP
    • Zhang, Y. Q., Rodesch, C. K., and Broadie, K. (2002). Living synaptic vesicle marker: synaptotagmin-GFP. Genesis 34, 142-145.
    • (2002) Genesis , vol.34 , pp. 142-145
    • Zhang, Y.Q.1    Rodesch, C.K.2    Broadie, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.