메뉴 건너뛰기




Volumn 30, Issue 7, 2005, Pages 367-372

SNARE complexes and neuroexocytosis: How many, how close?

Author keywords

[No Author keywords available]

Indexed keywords

BOTULINUM TOXIN; SNARE PROTEIN; SYNAPTOBREVIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNTAXIN;

EID: 21744457054     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2005.05.002     Document Type: Article
Times cited : (147)

References (48)
  • 1
    • 0027413655 scopus 로고
    • SNAP receptors implicated in vesicle targeting and fusion
    • T. Sollner SNAP receptors implicated in vesicle targeting and fusion Nature 362 1993 318 324
    • (1993) Nature , vol.362 , pp. 318-324
    • Sollner, T.1
  • 2
    • 0034018885 scopus 로고    scopus 로고
    • Neurotoxins affecting neuroexocytosis
    • G. Schiavo Neurotoxins affecting neuroexocytosis Physiol. Rev. 80 2000 717 766
    • (2000) Physiol. Rev. , vol.80 , pp. 717-766
    • Schiavo, G.1
  • 3
    • 1342323663 scopus 로고    scopus 로고
    • Identification of the major steps in botulinum toxin action
    • L.L. Simpson Identification of the major steps in botulinum toxin action Annu. Rev. Pharmacol. Toxicol. 44 2004 167 193
    • (2004) Annu. Rev. Pharmacol. Toxicol. , vol.44 , pp. 167-193
    • Simpson, L.L.1
  • 4
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • J.S. Bonifacino, and B.S. Glick The mechanisms of vesicle budding and fusion Cell 116 2004 153 166
    • (2004) Cell , vol.116 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 5
    • 0037459076 scopus 로고    scopus 로고
    • Membrane fusion
    • R. Jahn Membrane fusion Cell 112 2003 519 533
    • (2003) Cell , vol.112 , pp. 519-533
    • Jahn, R.1
  • 6
    • 0029114846 scopus 로고
    • The present status of tetanus and tetanus vaccination
    • A. Galazka, and F. Gasse The present status of tetanus and tetanus vaccination Curr. Top. Microbiol. Immunol. 195 1995 31 53
    • (1995) Curr. Top. Microbiol. Immunol. , vol.195 , pp. 31-53
    • Galazka, A.1    Gasse, F.2
  • 7
    • 0042744682 scopus 로고    scopus 로고
    • What is the role of SNARE proteins in membrane fusion?
    • J.G. Duman, and J.G. Forte What is the role of SNARE proteins in membrane fusion? Am. J. Physiol. Cell Physiol. 285 2003 C237 C249
    • (2003) Am. J. Physiol. Cell Physiol. , vol.285
    • Duman, J.G.1    Forte, J.G.2
  • 8
    • 0037377234 scopus 로고    scopus 로고
    • Vesicle trafficking: Pleasure and pain from SM genes
    • R.F.G. Toonen, and M. Verhage Vesicle trafficking: pleasure and pain from SM genes Trends Cell Biol. 13 2003 177 186
    • (2003) Trends Cell Biol. , vol.13 , pp. 177-186
    • Toonen, R.F.G.1    Verhage, M.2
  • 9
    • 0742272120 scopus 로고    scopus 로고
    • A complete set of SNAREs in yeast
    • L. Burri, and T. Lithgow A complete set of SNAREs in yeast Traffic 5 2004 45 52
    • (2004) Traffic , vol.5 , pp. 45-52
    • Burri, L.1    Lithgow, T.2
  • 10
    • 1242297081 scopus 로고    scopus 로고
    • 2+/calmodulin transfers the membrane-proximal lipid-binding domain of the v-SNARE synaptobrevin from cis to trans bilayers
    • 2+/calmodulin transfers the membrane-proximal lipid-binding domain of the v-SNARE synaptobrevin from cis to trans bilayers Proc. Natl. Acad. Sci. U. S. A. 101 2004 1578 1583
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 1578-1583
    • De Haro, L.1
  • 11
    • 8344255773 scopus 로고    scopus 로고
    • Tracking SNARE complex formation in live endocrine cells
    • S.J. An, and W. Almers Tracking SNARE complex formation in live endocrine cells Science 306 2004 1042 1046
    • (2004) Science , vol.306 , pp. 1042-1046
    • An, S.J.1    Almers, W.2
  • 12
    • 0347683439 scopus 로고    scopus 로고
    • High affinity interaction of syntaxin and SNAP-25 on the plasma membrane is abolished by botulinum toxin e
    • C. Rickman High affinity interaction of syntaxin and SNAP-25 on the plasma membrane is abolished by botulinum toxin E J. Biol. Chem. 279 2004 644 651
    • (2004) J. Biol. Chem. , vol.279 , pp. 644-651
    • Rickman, C.1
  • 13
    • 1542286172 scopus 로고    scopus 로고
    • The C2 domains of synaptotagmin - Partners in exocytosis
    • J. Bai, and E.R. Chapman The C2 domains of synaptotagmin - partners in exocytosis Trends Biochem. Sci. 29 2004 143 151
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 143-151
    • Bai, J.1    Chapman, E.R.2
  • 14
    • 0038107577 scopus 로고    scopus 로고
    • Differential control of the releasable vesicle pools by SNAP-25 splice variants and SNAP-23
    • J.B. Sorensen Differential control of the releasable vesicle pools by SNAP-25 splice variants and SNAP-23 Cell 114 2003 75 86
    • (2003) Cell , vol.114 , pp. 75-86
    • Sorensen, J.B.1
  • 15
    • 0030807735 scopus 로고    scopus 로고
    • Structural organization of the synaptic exocytosis core complex
    • R.C. Lin, and R.H. Scheller Structural organization of the synaptic exocytosis core complex Neuron 19 1997 1087 1094
    • (1997) Neuron , vol.19 , pp. 1087-1094
    • Lin, R.C.1    Scheller, R.H.2
  • 16
    • 0032549708 scopus 로고    scopus 로고
    • SNAREpins: Minimal machinery for membrane fusion
    • T. Weber SNAREpins: minimal machinery for membrane fusion Cell 92 1998 759 772
    • (1998) Cell , vol.92 , pp. 759-772
    • Weber, T.1
  • 17
    • 16344389389 scopus 로고    scopus 로고
    • Single molecule observation of liposome-bilayer fusion thermally induced by soluble N-ethyl maleimide sensitive-factor attachment protein receptors (SNAREs)
    • M.E. Bowen Single molecule observation of liposome-bilayer fusion thermally induced by soluble N-ethyl maleimide sensitive-factor attachment protein receptors (SNAREs) Biophys. J. 87 2004 3569 3584
    • (2004) Biophys. J. , vol.87 , pp. 3569-3584
    • Bowen, M.E.1
  • 18
    • 0028130728 scopus 로고
    • Synaptic vesicle membrane fusion complex: Action of clostridial neurotoxins on assembly
    • T. Hayashi Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly EMBO J. 13 1994 5051 5061
    • (1994) EMBO J. , vol.13 , pp. 5051-5061
    • Hayashi, T.1
  • 19
    • 0032079715 scopus 로고    scopus 로고
    • Protease resistance of syntaxin-SNAP-25-VAMP complexes. Implications for assembly and structure
    • M.A. Poirier Protease resistance of syntaxin-SNAP-25-VAMP complexes. Implications for assembly and structure J. Biol. Chem. 273 1998 11370 11377
    • (1998) J. Biol. Chem. , vol.273 , pp. 11370-11377
    • Poirier, M.A.1
  • 20
    • 0032555126 scopus 로고    scopus 로고
    • Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly
    • D. Fasshauer Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly Biochemistry 37 1998 10354 10362
    • (1998) Biochemistry , vol.37 , pp. 10354-10362
    • Fasshauer, D.1
  • 21
    • 0034407116 scopus 로고    scopus 로고
    • A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function
    • W. Antonin A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function EMBO J. 19 2000 6453 6464
    • (2000) EMBO J. , vol.19 , pp. 6453-6464
    • Antonin, W.1
  • 22
    • 0035830501 scopus 로고    scopus 로고
    • SNARE complex oligomerization by synaphin/complexin is essential for synaptic vesicle exocytosis
    • H. Tokumaru SNARE complex oligomerization by synaphin/complexin is essential for synaptic vesicle exocytosis Cell 104 2001 421 432
    • (2001) Cell , vol.104 , pp. 421-432
    • Tokumaru, H.1
  • 23
    • 0034733545 scopus 로고    scopus 로고
    • Selective interaction of complexin with the neuronal SNARE complex
    • S. Pabst Selective interaction of complexin with the neuronal SNARE complex J. Biol. Chem. 275 2000 19808 19818
    • (2000) J. Biol. Chem. , vol.275 , pp. 19808-19818
    • Pabst, S.1
  • 24
    • 0033057030 scopus 로고    scopus 로고
    • A stable interaction between syntaxin 1a and synaptobrevin 2 mediated by their transmembrane domains
    • M. Margittai A stable interaction between syntaxin 1a and synaptobrevin 2 mediated by their transmembrane domains FEBS Lett. 446 1999 40 44
    • (1999) FEBS Lett. , vol.446 , pp. 40-44
    • Margittai, M.1
  • 25
    • 0034625384 scopus 로고    scopus 로고
    • A conserved membrane-spanning amino acid motif drives homomeric and supports heteromeric assembly of presynaptic SNARE proteins
    • R. Laage A conserved membrane-spanning amino acid motif drives homomeric and supports heteromeric assembly of presynaptic SNARE proteins J. Biol. Chem. 275 2000 17481 17487
    • (2000) J. Biol. Chem. , vol.275 , pp. 17481-17487
    • Laage, R.1
  • 26
    • 0029898564 scopus 로고    scopus 로고
    • Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers
    • T. Danieli Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers J. Cell Biol. 133 1996 559 569
    • (1996) J. Cell Biol. , vol.133 , pp. 559-569
    • Danieli, T.1
  • 27
    • 1642540249 scopus 로고    scopus 로고
    • Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus
    • D.L. Gibbons Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus Nature 427 2004 320 325
    • (2004) Nature , vol.427 , pp. 320-325
    • Gibbons, D.L.1
  • 28
    • 0034946048 scopus 로고    scopus 로고
    • Three SNARE complexes cooperate to mediate membrane fusion
    • Y. Hua, and R.H. Scheller Three SNARE complexes cooperate to mediate membrane fusion Proc. Natl. Acad. Sci. U. S. A. 98 2001 8065 8070
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 8065-8070
    • Hua, Y.1    Scheller, R.H.2
  • 29
    • 1842429864 scopus 로고    scopus 로고
    • Transmembrane segments of syntaxin line the fusion pore of Ca-triggered exocytosis
    • X. Han Transmembrane segments of syntaxin line the fusion pore of Ca-triggered exocytosis Science 304 2004 289 292
    • (2004) Science , vol.304 , pp. 289-292
    • Han, X.1
  • 30
    • 0030901704 scopus 로고    scopus 로고
    • Botulinum neurotoxin serotype C: A novel effective botulinum toxin therapy in human
    • R. Eleopra Botulinum neurotoxin serotype C: a novel effective botulinum toxin therapy in human Neurosci. Lett. 224 1997 91 94
    • (1997) Neurosci. Lett. , vol.224 , pp. 91-94
    • Eleopra, R.1
  • 31
    • 0032515187 scopus 로고    scopus 로고
    • Different time courses of recovery after poisoning with botulinum neurotoxin serotypes a and e in humans
    • R. Eleopra Different time courses of recovery after poisoning with botulinum neurotoxin serotypes A and E in humans Neurosci. Lett. 256 1998 135 138
    • (1998) Neurosci. Lett. , vol.256 , pp. 135-138
    • Eleopra, R.1
  • 32
    • 0037428398 scopus 로고    scopus 로고
    • Evaluation of the therapeutic usefulness of botulinum neurotoxin B, C1, E, and F compared with the long lasting type A. Basis for distinct durations of inhibition of exocytosis in central neurons
    • P.G. Foran Evaluation of the therapeutic usefulness of botulinum neurotoxin B, C1, E, and F compared with the long lasting type A. Basis for distinct durations of inhibition of exocytosis in central neurons J. Biol. Chem. 278 2003 1363 1371
    • (2003) J. Biol. Chem. , vol.278 , pp. 1363-1371
    • Foran, P.G.1
  • 33
    • 0029118637 scopus 로고
    • Clostridial neurotoxins compromise the stability of a low energy SNARE complex mediating NSF activation of synaptic vesicle fusion
    • L.L. Pellegrini Clostridial neurotoxins compromise the stability of a low energy SNARE complex mediating NSF activation of synaptic vesicle fusion EMBO J. 14 1995 4705 4713
    • (1995) EMBO J. , vol.14 , pp. 4705-4713
    • Pellegrini, L.L.1
  • 34
    • 10044260742 scopus 로고    scopus 로고
    • A molecular basis underlying differences in the toxicity of botulinum serotypes a and e
    • M. Bajohrs A molecular basis underlying differences in the toxicity of botulinum serotypes A and E EMBO Rep. 5 2004 1090 1095
    • (2004) EMBO Rep. , vol.5 , pp. 1090-1095
    • Bajohrs, M.1
  • 35
    • 0029164314 scopus 로고
    • Poisoning by botulinum neurotoxin a does not inhibit formation or disassembly of the synaptosomal fusion complex
    • H. Otto Poisoning by botulinum neurotoxin A does not inhibit formation or disassembly of the synaptosomal fusion complex Biochem. Biophys. Res. Commun. 212 1995 945 952
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 945-952
    • Otto, H.1
  • 36
    • 0032776446 scopus 로고    scopus 로고
    • Persistence of botulinum neurotoxin action in cultured spinal cord cells
    • J.E. Keller Persistence of botulinum neurotoxin action in cultured spinal cord cells FEBS Lett. 456 1999 137 142
    • (1999) FEBS Lett. , vol.456 , pp. 137-142
    • Keller, J.E.1
  • 37
    • 0037396608 scopus 로고    scopus 로고
    • Dynamics of motor nerve terminal remodeling unveiled using SNARE-cleaving botulinum toxins: The extent and duration are dictated by the sites of SNAP-25 truncation
    • F.A. Meunier Dynamics of motor nerve terminal remodeling unveiled using SNARE-cleaving botulinum toxins: the extent and duration are dictated by the sites of SNAP-25 truncation Mol. Cell. Neurosci. 22 2003 454 466
    • (2003) Mol. Cell. Neurosci. , vol.22 , pp. 454-466
    • Meunier, F.A.1
  • 38
    • 0032230364 scopus 로고    scopus 로고
    • Truncated SNAP-25 (1-197), like botulinum neurotoxin A, can inhibit insulin secretion from HIT-T15 insulinoma cells
    • X. Huang Truncated SNAP-25 (1-197), like botulinum neurotoxin A, can inhibit insulin secretion from HIT-T15 insulinoma cells Mol. Endocrinol. 12 1998 1060 1070
    • (1998) Mol. Endocrinol. , vol.12 , pp. 1060-1070
    • Huang, X.1
  • 39
    • 0033594949 scopus 로고    scopus 로고
    • A single amino acid near the C terminus of the synaptosome-associated protein of 25 kDa (SNAP-25) is essential for exocytosis in chromaffin cells
    • M. Criado A single amino acid near the C terminus of the synaptosome-associated protein of 25 kDa (SNAP-25) is essential for exocytosis in chromaffin cells Proc. Natl. Acad. Sci. U. S. A. 96 1999 7256 7261
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 7256-7261
    • Criado, M.1
  • 40
    • 0036629350 scopus 로고    scopus 로고
    • 2+-induced changes in SNAREs and synaptotagmin I correlate with triggered exocytosis from chromaffin cells: Insights gleaned into the signal transduction using trypsin and botulinum toxins
    • 2+-induced changes in SNAREs and synaptotagmin I correlate with triggered exocytosis from chromaffin cells: insights gleaned into the signal transduction using trypsin and botulinum toxins J. Cell Sci. 115 2002 2791 2800
    • (2002) J. Cell Sci. , vol.115 , pp. 2791-2800
    • Lawrence, G.W.1    Dolly, J.O.2
  • 41
    • 0031030099 scopus 로고    scopus 로고
    • A peptide that mimics the C-terminal sequence of SNAP-25 inhibits secretory vesicle docking in chromaffin cells
    • L.M. Gutierrez A peptide that mimics the C-terminal sequence of SNAP-25 inhibits secretory vesicle docking in chromaffin cells J. Biol. Chem. 272 1997 2634 2639
    • (1997) J. Biol. Chem. , vol.272 , pp. 2634-2639
    • Gutierrez, L.M.1
  • 42
    • 0035918270 scopus 로고    scopus 로고
    • The role of the synaptic protein SNAP-25 in the potency of botulinum neurotoxin type a
    • J.E. Keller, and E.A. Neale The role of the synaptic protein SNAP-25 in the potency of botulinum neurotoxin type A J. Biol. Chem. 276 2001 13476 13482
    • (2001) J. Biol. Chem. , vol.276 , pp. 13476-13482
    • Keller, J.E.1    Neale, E.A.2
  • 43
    • 0345832207 scopus 로고    scopus 로고
    • Uptake of botulinum neurotoxin into cultured neurons
    • J.E. Keller Uptake of botulinum neurotoxin into cultured neurons Biochemistry 43 2004 526 532
    • (2004) Biochemistry , vol.43 , pp. 526-532
    • Keller, J.E.1
  • 44
    • 0031901958 scopus 로고    scopus 로고
    • Presynaptic protein interactions in vivo: Evidence from botulinum A, C, D and e action at frog neuromuscular junction
    • D.A. Raciborska Presynaptic protein interactions in vivo: evidence from botulinum A, C, D and E action at frog neuromuscular junction Eur. J. Neurosci. 10 1998 2617 2628
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 2617-2628
    • Raciborska, D.A.1
  • 45
    • 12144291021 scopus 로고    scopus 로고
    • Plasma membrane localization signals in the light chain of botulinum neurotoxin
    • E. Fernandez-Salas Plasma membrane localization signals in the light chain of botulinum neurotoxin Proc. Natl. Acad. Sci. U. S. A. 101 2004 3208 3213
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 3208-3213
    • Fernandez-Salas, E.1
  • 46
    • 33644681150 scopus 로고    scopus 로고
    • Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity
    • T. Xu Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity Nat. Neurosci. 1 1998 192 200
    • (1998) Nat. Neurosci. , vol.1 , pp. 192-200
    • Xu, T.1
  • 47
    • 0033598965 scopus 로고    scopus 로고
    • Inhibition of SNARE complex assembly differentially affects kinetic components of exocytosis
    • T. Xu Inhibition of SNARE complex assembly differentially affects kinetic components of exocytosis Cell 99 1999 713 722
    • (1999) Cell , vol.99 , pp. 713-722
    • Xu, T.1
  • 48
    • 0037204076 scopus 로고    scopus 로고
    • Three-dimensional structure of the complexin/snare complex
    • X. Chen Three-dimensional structure of the complexin/snare complex Neuron 33 2002 397 409
    • (2002) Neuron , vol.33 , pp. 397-409
    • Chen, X.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.