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Volumn 60, Issue 6, 2000, Pages 743-753

The mechanism of the neurotransmitter release in growth cones

Author keywords

latrotoxin; rab3A; Exocytosis; Growth cone; Rabphilin; SNARE mechanism

Indexed keywords

ALPHA LATROTOXIN; RAB PROTEIN; RABPHILIN; SNARE PROTEIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; UNCLASSIFIED DRUG;

EID: 0034660191     PISSN: 03604012     EISSN: None     Source Type: Journal    
DOI: 10.1002/1097-4547(20000615)60:6<743::AID-JNR6>3.0.CO;2-T     Document Type: Article
Times cited : (9)

References (50)
  • 1
    • 0032917551 scopus 로고    scopus 로고
    • Distribution of neurotransmitter secretion in growing axons
    • Antonov I, Chang S, Zakharenko S, Popov SV. 1999. Distribution of neurotransmitter secretion in growing axons. Neuroscience 90:975-984.
    • (1999) Neuroscience , vol.90 , pp. 975-984
    • Antonov, I.1    Chang, S.2    Zakharenko, S.3    Popov, S.V.4
  • 2
    • 0026032612 scopus 로고
    • Microtubule-dissociating drugs and A23187 reveal differences in the inhibition of synaptosomal transmitter release by botulinum neurotoxins types A and B
    • Ashton AC, Dolly JO. 1991. Microtubule-dissociating drugs and A23187 reveal differences in the inhibition of synaptosomal transmitter release by botulinum neurotoxins types A and B. J Neurochem 56:827-835.
    • (1991) J Neurochem , vol.56 , pp. 827-835
    • Ashton, A.C.1    Dolly, J.O.2
  • 3
    • 0030786774 scopus 로고    scopus 로고
    • Better late than never: A role for rabs late in exocytosis
    • Bean AJ, Scheller RH. 1997. Better late than never: a role for rabs late in exocytosis. Neuron 19:751-754.
    • (1997) Neuron , vol.19 , pp. 751-754
    • Bean, A.J.1    Scheller, R.H.2
  • 4
    • 0032054866 scopus 로고    scopus 로고
    • Analysis of regulated exocytosis in adrenal chromaffin cells: Insights into NSF/SNAP/SNARE
    • Burgoyne RD, Morgan A. 1998. Analysis of regulated exocytosis in adrenal chromaffin cells: insights into NSF/SNAP/SNARE. BioEssays 20:328-335.
    • (1998) BioEssays , vol.20 , pp. 328-335
    • Burgoyne, R.D.1    Morgan, A.2
  • 5
    • 0028149342 scopus 로고
    • Specific interaction of Mss4 with members of the rab GTPase subfamily
    • Burton JL, Burns ME, Gatti E, Augustine GJ, De Camilli P. 1994. Specific interaction of Mss4 with members of the rab GTPase subfamily. EMBO J 13:5547-5558.
    • (1994) EMBO J , vol.13 , pp. 5547-5558
    • Burton, J.L.1    Burns, M.E.2    Gatti, E.3    Augustine, G.J.4    De Camilli, P.5
  • 8
    • 0031915371 scopus 로고    scopus 로고
    • N-Ethylmaleimide-sensitive factor-dependent α-SNAP release, An early event in the docking/fusion process, is not regulated by rab GTPases
    • Colombo MI, Gelberman SC, Whiteheart SW, Stahl PD. 1998. N-Ethylmaleimide-sensitive factor-dependent α-SNAP release, an early event in the docking/fusion process, is not regulated by rab GTPases. J Biol Chem 273:1334-1338.
    • (1998) J Biol Chem , vol.273 , pp. 1334-1338
    • Colombo, M.I.1    Gelberman, S.C.2    Whiteheart, S.W.3    Stahl, P.D.4
  • 13
    • 0031898897 scopus 로고    scopus 로고
    • Rab3 and synaptotagmin: The yin and yang of synaptic membrane fusion
    • Geppert M, Südhof TC. 1998. Rab3 and synaptotagmin: the yin and yang of synaptic membrane fusion. Ann Rev Neurosci 21:97-126.
    • (1998) Ann Rev Neurosci , vol.21 , pp. 97-126
    • Geppert, M.1    Südhof, T.C.2
  • 14
    • 0027480289 scopus 로고
    • Synaptic structure and development: The neuromuscular junction
    • Hall ZW, Sanes JR. 1993. Synaptic structure and development: the neuromuscular junction. Cell 72/Neuron 10:99-121.
    • (1993) Cell 72/Neuron , vol.10 , pp. 99-121
    • Hall, Z.W.1    Sanes, J.R.2
  • 15
    • 0030846539 scopus 로고    scopus 로고
    • Neurotransmitter release-four years of SNARE complexes
    • Hanson J, Heuser JE, Jahn R. 1997. Neurotransmitter release-four years of SNARE complexes. Curr Opin Neurobiol 7:310-315.
    • (1997) Curr Opin Neurobiol , vol.7 , pp. 310-315
    • Hanson, J.1    Heuser, J.E.2    Jahn, R.3
  • 16
    • 0033558032 scopus 로고    scopus 로고
    • The sec6/8 complex is localized at neurite outgrowth and axonal synapse-assembly domains
    • Hazuka CD, Foletti DL, Hsu S-C, Kee Y, Hopf FW, Scheller RH. 1999. The sec6/8 complex is localized at neurite outgrowth and axonal synapse-assembly domains. J Neurosci 19:1324-1334.
    • (1999) J Neurosci , vol.19 , pp. 1324-1334
    • Hazuka, C.D.1    Foletti, D.L.2    Hsu, S.-C.3    Kee, Y.4    Hopf, F.W.5    Scheller, R.H.6
  • 18
    • 0342506130 scopus 로고    scopus 로고
    • Significance of the snare mechanism in growth cone functions
    • Fujisawa H, editor. Basel: Karger.
    • Igarashi M. 1997. Significance of the SNARE mechanism in growth cone functions. In: Fujisawa H, editor. Molecular basis of axon growth and nerve pattern formation. Basel: Karger. p 107-120.
    • (1997) Molecular Basis of Axon Growth and Nerve Pattern Formation , pp. 107-120
    • Igarashi, M.1
  • 19
    • 0029949638 scopus 로고    scopus 로고
    • Growth cone collapse and inhibition of neurite growth induced by botulinum neurotoxin C1: A t-SNARE is involved in axonal growth
    • Igarashi M, Kozaki S, Terakawa S, Kawano S, Ide C, Komiya Y. 1996. Growth cone collapse and inhibition of neurite growth induced by botulinum neurotoxin C1: a t-SNARE is involved in axonal growth. J Cell Biol 134:205-215
    • (1996) J Cell Biol , vol.134 , pp. 205-215
    • Igarashi, M.1    Kozaki, S.2    Terakawa, S.3    Kawano, S.4    Ide, C.5    Komiya, Y.6
  • 20
    • 0031017149 scopus 로고    scopus 로고
    • The SNARE complex in growth cones: Molecular aspects of the axon terminal development
    • Igarashi M, Tagaya M, Komiya Y. 1997. The SNARE complex in growth cones: molecular aspects of the axon terminal development. J Neurosci 17:1460-1470.
    • (1997) J Neurosci , vol.17 , pp. 1460-1470
    • Igarashi, M.1    Tagaya, M.2    Komiya, Y.3
  • 21
    • 0027370160 scopus 로고
    • Rab3A GTP-ase activating protein-inhibiting activity of rabphilin-3A, A putative rab3A target protein
    • Kishida S, Shirataki H, Sasaki T, Kato M, Kaibuchi K, Takai Y. 1993. Rab3A GTP-ase activating protein-inhibiting activity of rabphilin-3A, a putative rab3A target protein. J Biol Chem 268:22259-22261.
    • (1993) J Biol Chem , vol.268 , pp. 22259-22261
    • Kishida, S.1    Shirataki, H.2    Sasaki, T.3    Kato, M.4    Kaibuchi, K.5    Takai, Y.6
  • 26
    • 0029785081 scopus 로고    scopus 로고
    • Role of the rab3A-binding domain in targeting of rabphilin-3A to vesicle membranes of PC12 cells
    • McKiernan CJ Stabila PF, Macara IG. 1996. Role of the rab3A-binding domain in targeting of rabphilin-3A to vesicle membranes of PC12 cells. Mol Cell Biol 16:4985-4995.
    • (1996) Mol Cell Biol , vol.16 , pp. 4985-4995
    • McKiernan, C.J.1    Stabila, P.F.2    Macara, I.G.3
  • 28
    • 0028268948 scopus 로고
    • Molecular mechanisms of clostridial neurotoxins
    • Niemann H, Blasi J, Jahn R. 1994. Molecular mechanisms of clostridial neurotoxins. Trends Cell Biol 4:179-184.
    • (1994) Trends Cell Biol , vol.4 , pp. 179-184
    • Niemann, H.1    Blasi, J.2    Jahn, R.3
  • 33
    • 0033525215 scopus 로고    scopus 로고
    • Structural basis of rab effector specificity: Crystal structure of the small G protein rab3A complexed with the effector domain of rabphilin-3A
    • Ostermeier C, Brunger AT. 1999. Structural basis of rab effector specificity: crystal structure of the small G protein rab3A complexed with the effector domain of rabphilin-3A. Cell 96:363-374.
    • (1999) Cell , vol.96 , pp. 363-374
    • Ostermeier, C.1    Brunger, A.T.2
  • 34
    • 0027254029 scopus 로고
    • α-latrotoxin receptor
    • Petrenko, AG. 1993. α-latrotoxin receptor. FEBS Lett 325:81-85.
    • (1993) FEBS Lett , vol.325 , pp. 81-85
    • Petrenko, A.G.1
  • 36
    • 0001956792 scopus 로고    scopus 로고
    • Isolation of synaptosomes, growth cones and their subcellular components
    • Turner AJ, Bachelard HS, editors. London: IRL Press.
    • Phelan P, Gordon-Weeks PR. 1997. Isolation of synaptosomes, growth cones and their subcellular components. In: Turner AJ, Bachelard HS, editors. Neurochemistry, a practical approach, 2nd edition. London: IRL Press. p 1-38.
    • (1997) Neurochemistry, a Practical Approach, 2nd Edition. , pp. 1-38
    • Phelan, P.1    Gordon-Weeks, P.R.2
  • 39
    • 0029065036 scopus 로고
    • Delivery of protein into cells using polycationic liposomes
    • Sells MA, Li J, Chernoff J. 1995. Delivery of protein into cells using polycationic liposomes. BioTechniques 19:72-78.
    • (1995) BioTechniques , vol.19 , pp. 72-78
    • Sells, M.A.1    Li, J.2    Chernoff, J.3
  • 41
    • 0027997591 scopus 로고
    • GTP cleavage by the small GTP-binding protein rab3A is associated with exocytosis of synaptic vesicles induced by α-latrotoxin
    • Stahl B, Fischer von Mollard G, Walch-Solimena C, Jahn R. 1994. GTP cleavage by the small GTP-binding protein rab3A is associated with exocytosis of synaptic vesicles induced by α-latrotoxin. J Biol Chem 269:24770-24776.
    • (1994) J Biol Chem , vol.269 , pp. 24770-24776
    • Stahl, B.1    Fischer Von Mollard, G.2    Walch-Solimena, C.3    Jahn, R.4
  • 42
    • 0029935431 scopus 로고    scopus 로고
    • Rab3 reversibly recruits rabphilin to synaptic vesicles by a mechanism analogous to raf recruitment by ras
    • Stahl B, Chou JH, Li C, Südhof TC, Jahn R. 1996. Rab3 reversibly recruits rabphilin to synaptic vesicles by a mechanism analogous to raf recruitment by ras. EMBO J 15:1799-1809.
    • (1996) EMBO J , vol.15 , pp. 1799-1809
    • Stahl, B.1    Chou, J.H.2    Li, C.3    Südhof, T.C.4    Jahn, R.5
  • 43
    • 0032484023 scopus 로고    scopus 로고
    • α-latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an usual family of ubiquitous G-protein-linked receptors: G-protein coupling not required for triggering exocytosis
    • Sugita S, Ichtchenko K, Khvotchev M, Südhof TC. 1998. α-latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an usual family of ubiquitous G-protein-linked receptors: G-protein coupling not required for triggering exocytosis. J Biol Chem 273:32715-32724.
    • (1998) J Biol Chem , vol.273 , pp. 32715-32724
    • Sugita, S.1    Ichtchenko, K.2    Khvotchev, M.3    Südhof, T.C.4
  • 44
    • 0024391799 scopus 로고
    • Developmental changes in the calcium dependency of α-ammobutyric acid release from isolated growth cones: Correlation with growth cone morphology
    • Taylor J, Gordon-Weeks PR. 1989. Developmental changes in the calcium dependency of α-ammobutyric acid release from isolated growth cones: correlation with growth cone morphology. J Neurochem 53:834-843.
    • (1989) J Neurochem , vol.53 , pp. 834-843
    • Taylor, J.1    Gordon-Weeks, P.R.2
  • 46
    • 0031041373 scopus 로고    scopus 로고
    • Isolation and characterization of a GDP/GTP exchange protein specific for the rab3 subfamily small g proteins
    • Wada M, Nakanishi H, Satoh A, Hirano H, Obaishi H, Matsuura Y, Takai Y. 1997. Isolation and characterization of a GDP/GTP exchange protein specific for the rab3 subfamily small G proteins. J Biol Chem 272:3875-3878.
    • (1997) J Biol Chem , vol.272 , pp. 3875-3878
    • Wada, M.1    Nakanishi, H.2    Satoh, A.3    Hirano, H.4    Obaishi, H.5    Matsuura, Y.6    Takai, Y.7
  • 48
    • 0026667096 scopus 로고
    • Plasmalemmal insertion and modification of sodium channels at the nerve growth cone
    • Wood MR, DeBin J, Strichartz GR, Pfenninger KH. 1992. Plasmalemmal insertion and modification of sodium channels at the nerve growth cone. J Neurosci 12:2948-2959.
    • (1992) J Neurosci , vol.12 , pp. 2948-2959
    • Wood, M.R.1    DeBin, J.2    Strichartz, G.R.3    Pfenninger, K.H.4
  • 49
  • 50
    • 0032538996 scopus 로고    scopus 로고
    • Dynamics of axonal microtubules regulate the topology of new membrane insertion into the growing neuntes
    • Zakharenko S, Popov S. 1998. Dynamics of axonal microtubules regulate the topology of new membrane insertion into the growing neuntes. J Cell Biol 143:1077-1086.
    • (1998) J Cell Biol , vol.143 , pp. 1077-1086
    • Zakharenko, S.1    Popov, S.2


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