메뉴 건너뛰기




Volumn 66, Issue 3, 2009, Pages 460-469

Progress in understanding the neuronal SNARE function and its regulation

Author keywords

Complexin; Membrane fusion; Neurotransmitter release; Single molecule study; SNARE; Synaptotagmin 1

Indexed keywords

SNARE PROTEIN; SYNAPTOTAGMIN I;

EID: 59349117350     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-008-8372-z     Document Type: Review
Times cited : (14)

References (86)
  • 1
    • 0038290760 scopus 로고    scopus 로고
    • Protein-lipid interplay in fusion and fission of biological membranes
    • Chernomordik, L. V. and Kozlov, M. M. (2003). Protein-lipid interplay in fusion and fission of biological membranes. Annu. Rev. Biochem. 72, 175-207.
    • (2003) Annu. Rev. Biochem , vol.72 , pp. 175-207
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 2
    • 2942635759 scopus 로고    scopus 로고
    • The energetics of membrane fusion from binding, through hemifusion, pore formation, and pore enlargement
    • Cohen, F. S. and Melikyan, G. B. (2004). The energetics of membrane fusion from binding, through hemifusion, pore formation, and pore enlargement. J. Membr. Biol. 199, 1-14.
    • (2004) J. Membr. Biol , vol.199 , pp. 1-14
    • Cohen, F.S.1    Melikyan, G.B.2
  • 3
    • 2942556680 scopus 로고    scopus 로고
    • The synaptic vesicle cycle
    • Sudhof, T. C. (2004). The synaptic vesicle cycle. Annu. Rev. Neurosci. 27, 509-547.
    • (2004) Annu. Rev. Neurosci , vol.27 , pp. 509-547
    • Sudhof, T.C.1
  • 5
    • 0033607288 scopus 로고    scopus 로고
    • SNARE proteins mediate lipid bilayer fusion
    • Bock, J. B. and Scheller, R. H. (1999). SNARE proteins mediate lipid bilayer fusion. Proc. Natl. Acad. Sci. U S A 96, 12227-12229.
    • (1999) Proc. Natl. Acad. Sci. U S A , vol.96 , pp. 12227-12229
    • Bock, J.B.1    Scheller, R.H.2
  • 6
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
    • Fasshauer, D., Sutton, R. B., Brunger, A. T. and Jahn, R. (1998). Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc. Natl. Acad. Sci. U S A 95, 15781-15786.
    • (1998) Proc. Natl. Acad. Sci. U S A , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brunger, A.T.3    Jahn, R.4
  • 8
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
    • Sutton, R. B., Fasshauer, D., Jahn, R. and Brunger, A. T. (1998). Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature 395, 347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 9
    • 0030807735 scopus 로고    scopus 로고
    • Structural organization of the synaptic exocytosis core complex
    • Lin, R. C. and Scheller, R. H. (1997). Structural organization of the synaptic exocytosis core complex. Neuron 19, 1087-1094.
    • (1997) Neuron , vol.19 , pp. 1087-1094
    • Lin, R.C.1    Scheller, R.H.2
  • 10
    • 0029075363 scopus 로고
    • The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin
    • Hanson, P. I., Otto, H., Barton, N. and Jahn, R. (1995). The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin. J. Biol. Chem. 270, 16955-16961.
    • (1995) J. Biol. Chem , vol.270 , pp. 16955-16961
    • Hanson, P.I.1    Otto, H.2    Barton, N.3    Jahn, R.4
  • 12
    • 0034631955 scopus 로고    scopus 로고
    • Close is not enough: SNARE-dependent membrane fusion requires an active mechanism that transduces force to membrane anchors
    • McNew, J. A., Weber, T., Parlati, F., Johnston, R. J., Melia, T. J., Sollner, T. H. and Rothman, J. E. (2000). Close is not enough: SNARE-dependent membrane fusion requires an active mechanism that transduces force to membrane anchors. J. Cell Biol. 150, 105-117.
    • (2000) J. Cell Biol , vol.150 , pp. 105-117
    • McNew, J.A.1    Weber, T.2    Parlati, F.3    Johnston, R.J.4    Melia, T.J.5    Sollner, T.H.6    Rothman, J.E.7
  • 13
    • 34247169946 scopus 로고    scopus 로고
    • The role of transmembrane domains in membrane fusion
    • Langosch, D., Hofmann, M. and Ungermann, C. (2007). The role of transmembrane domains in membrane fusion. Cell. Mol. Life Sci. 64, 850-864.
    • (2007) Cell. Mol. Life Sci , vol.64 , pp. 850-864
    • Langosch, D.1    Hofmann, M.2    Ungermann, C.3
  • 14
    • 45849152550 scopus 로고    scopus 로고
    • Mechanisms of membrane fusion: Disparate players and common principles
    • Martens, S. and McMahon, H. T. (2008). Mechanisms of membrane fusion: disparate players and common principles. Nat. Rev. Mol. Cell Biol. 9, 543-556.
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , pp. 543-556
    • Martens, S.1    McMahon, H.T.2
  • 15
    • 33747622293 scopus 로고    scopus 로고
    • SNAREs-engines for membrane fusion
    • Jahn, R. and Scheller, R. H. (2006). SNAREs-engines for membrane fusion. Nat. Rev. Mol. Cell Biol. 7, 631-643.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 631-643
    • Jahn, R.1    Scheller, R.H.2
  • 16
    • 33646185099 scopus 로고    scopus 로고
    • Fusion pores and fusion machines in Ca2+-triggered exocytosis
    • Jackson, M. B. and Chapman, E. R. (2006). Fusion pores and fusion machines in Ca2+-triggered exocytosis. Annu. Rev. Biophys. Biomol. Struct. 35, 135-160.
    • (2006) Annu. Rev. Biophys. Biomol. Struct , vol.35 , pp. 135-160
    • Jackson, M.B.1    Chapman, E.R.2
  • 17
    • 33644770187 scopus 로고    scopus 로고
    • Structure and function of SNARE and SNARE-interacting proteins
    • Brunger, A. T. (2005). Structure and function of SNARE and SNARE-interacting proteins. Q. Rev. Biophys. 38, 1-47.
    • (2005) Q. Rev. Biophys , vol.38 , pp. 1-47
    • Brunger, A.T.1
  • 19
    • 46049088692 scopus 로고    scopus 로고
    • The SNARE complex from yeast is partially unstructured on the membrane
    • Su, Z., Ishitsuka, Y., Ha, T. and Shin, Y. K. (2008). The SNARE complex from yeast is partially unstructured on the membrane. Structure 16, 1138-1146.
    • (2008) Structure , vol.16 , pp. 1138-1146
    • Su, Z.1    Ishitsuka, Y.2    Ha, T.3    Shin, Y.K.4
  • 20
    • 0033574464 scopus 로고    scopus 로고
    • SNARE complex formation is triggered by Ca2+ and drives membrane fusion
    • Chen, Y. A., Scales, S. J., Patel, S. M., Doung, Y. C. and Scheller, R. H. (1999). SNARE complex formation is triggered by Ca2+ and drives membrane fusion. Cell 97, 165-174.
    • (1999) Cell , vol.97 , pp. 165-174
    • Chen, Y.A.1    Scales, S.J.2    Patel, S.M.3    Doung, Y.C.4    Scheller, R.H.5
  • 21
    • 0031183646 scopus 로고    scopus 로고
    • Action of clostridial neurotoxins and mechanism of the membrane fusion of intracellular transport vesicles]
    • Hayashi, T. (1997). [Action of clostridial neurotoxins and mechanism of the membrane fusion of intracellular transport vesicles]. Nippon Saikingaku Zasshi 52, 583-592.
    • (1997) Nippon Saikingaku Zasshi , vol.52 , pp. 583-592
    • Hayashi, T.1
  • 22
    • 0029164314 scopus 로고
    • Poisoning by botulinum neurotoxin A does not inhibit formation or disassembly of the synaptosomal fusion complex
    • Otto, H., Hanson, P. I., Chapman, E. R., Blasi, J. and Jahn, R. (1995). Poisoning by botulinum neurotoxin A does not inhibit formation or disassembly of the synaptosomal fusion complex. Biochem. Biophys. Res. Commun. 212, 945-952.
    • (1995) Biochem. Biophys. Res. Commun , vol.212 , pp. 945-952
    • Otto, H.1    Hanson, P.I.2    Chapman, E.R.3    Blasi, J.4    Jahn, R.5
  • 23
    • 0034946048 scopus 로고    scopus 로고
    • Three SNARE complexes cooperate to mediate membrane fusion
    • Hua, Y. and Scheller, R. H. (2001). Three SNARE complexes cooperate to mediate membrane fusion. Proc. Natl. Acad. Sci. U S A 98, 8065-8070.
    • (2001) Proc. Natl. Acad. Sci. U S A , vol.98 , pp. 8065-8070
    • Hua, Y.1    Scheller, R.H.2
  • 24
    • 22944485726 scopus 로고    scopus 로고
    • Trans-SNARE pairing can precede a hemifusion intermediate in intracellular membrane fusion
    • Reese, C., Heise, F. and Mayer, A. (2005). Trans-SNARE pairing can precede a hemifusion intermediate in intracellular membrane fusion. Nature 436, 410-414.
    • (2005) Nature , vol.436 , pp. 410-414
    • Reese, C.1    Heise, F.2    Mayer, A.3
  • 27
    • 46449090904 scopus 로고    scopus 로고
    • Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated membrane fusion
    • Lu, X., Zhang, Y. and Shin, Y. K. (2008). Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated membrane fusion. Nat. Struct. Mol. Biol. 15, 700-706.
    • (2008) Nat. Struct. Mol. Biol , vol.15 , pp. 700-706
    • Lu, X.1    Zhang, Y.2    Shin, Y.K.3
  • 28
    • 0347683439 scopus 로고    scopus 로고
    • High affinity interaction of syntaxin and SNAP-25 on the plasma membrane is abolished by botulinum toxin E
    • Rickman, C., Meunier, F. A., Binz, T. and Davletov, B. (2004). High affinity interaction of syntaxin and SNAP-25 on the plasma membrane is abolished by botulinum toxin E. J. Biol. Chem. 279, 644-651.
    • (2004) J. Biol. Chem , vol.279 , pp. 644-651
    • Rickman, C.1    Meunier, F.A.2    Binz, T.3    Davletov, B.4
  • 29
    • 8344255773 scopus 로고    scopus 로고
    • Tracking SNARE complex formation in live endocrine cells
    • An, S. J. and Almers, W. (2004). Tracking SNARE complex formation in live endocrine cells. Science 306, 1042-1046.
    • (2004) Science , vol.306 , pp. 1042-1046
    • An, S.J.1    Almers, W.2
  • 30
    • 0035918302 scopus 로고    scopus 로고
    • Homo- and heterooligomeric SNARE complexes studied by site-directed spin labeling
    • Margittai, M., Fasshauer, D., Pabst, S., Jahn, R. and Langen, R. (2001). Homo- and heterooligomeric SNARE complexes studied by site-directed spin labeling. J. Biol. Chem. 276, 13169-13177.
    • (2001) J. Biol. Chem , vol.276 , pp. 13169-13177
    • Margittai, M.1    Fasshauer, D.2    Pabst, S.3    Jahn, R.4    Langen, R.5
  • 31
    • 0030735370 scopus 로고    scopus 로고
    • Structural changes are associated with soluble N-ethylmaleimide- sensitive fusion protein attachment protein receptor complex formation
    • Fasshauer, D., Otto, H. , Eliason, W. K., Jahn, R. and Brunger, A. T. (1997). Structural changes are associated with soluble N-ethylmaleimide- sensitive fusion protein attachment protein receptor complex formation. J. Biol. Chem. 272, 28036-28041.
    • (1997) J. Biol. Chem , vol.272 , pp. 28036-28041
    • Fasshauer, D.1    Otto, H.2    Eliason, W.K.3    Jahn, R.4    Brunger, A.T.5
  • 32
    • 38949211822 scopus 로고    scopus 로고
    • Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin/SNAP-25 complex
    • Weninger, K., Bowen, M. E., Choi, U. B., Chu, S. and Brunger, A. T. (2008). Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin/SNAP-25 complex. Structure 16, 308-320.
    • (2008) Structure , vol.16 , pp. 308-320
    • Weninger, K.1    Bowen, M.E.2    Choi, U.B.3    Chu, S.4    Brunger, A.T.5
  • 33
    • 0030661912 scopus 로고    scopus 로고
    • Dimerization of the synaptic vesicle protein synaptobrevin (vesicle-associated membrane protein) II depends on specific residues within the transmembrane segment
    • Laage, R. and Langosch, D. (1997). Dimerization of the synaptic vesicle protein synaptobrevin (vesicle-associated membrane protein) II depends on specific residues within the transmembrane segment. Eur. J. Biochem. 249, 540-546.
    • (1997) Eur. J. Biochem , vol.249 , pp. 540-546
    • Laage, R.1    Langosch, D.2
  • 34
    • 2142640821 scopus 로고    scopus 로고
    • Synaptobrevin transmembrane domain dimerization-revisited
    • Roy, R., Laage, R. and Langosch, D. (2004). Synaptobrevin transmembrane domain dimerization-revisited. Biochemistry 43, 4964-4970.
    • (2004) Biochemistry , vol.43 , pp. 4964-4970
    • Roy, R.1    Laage, R.2    Langosch, D.3
  • 35
    • 21244484757 scopus 로고    scopus 로고
    • Electrostatic interactions between the syntaxin membrane anchor and neurotransmitter passing through the fusion pore
    • Han, X. and Jackson, M. B. (2005). Electrostatic interactions between the syntaxin membrane anchor and neurotransmitter passing through the fusion pore. Biophys. J. 88, L20-22.
    • (2005) Biophys. J , vol.88
    • Han, X.1    Jackson, M.B.2
  • 36
    • 1842429864 scopus 로고    scopus 로고
    • Transmembrane segments of syntaxin line the fusion pore of Ca2+-triggered exocytosis
    • Han, X., Wang, C. T., Bai, J., Chapman, E. R. and Jackson, M. B. (2004). Transmembrane segments of syntaxin line the fusion pore of Ca2+-triggered exocytosis. Science 304, 289-292.
    • (2004) Science , vol.304 , pp. 289-292
    • Han, X.1    Wang, C.T.2    Bai, J.3    Chapman, E.R.4    Jackson, M.B.5
  • 37
    • 27544473312 scopus 로고    scopus 로고
    • Membrane hemifusion: Crossing a chasm in two leaps
    • Chernomordik, L. V. and Kozlov, M. M. (2005). Membrane hemifusion: crossing a chasm in two leaps. Cell 123, 375-382.
    • (2005) Cell , vol.123 , pp. 375-382
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 39
    • 24044530897 scopus 로고    scopus 로고
    • Membrane fusion induced by neuronal SNAREs transits through hemifusion
    • Lu, X., Zhang, F., McNew, J. A. and Shin, Y. K. (2005). Membrane fusion induced by neuronal SNAREs transits through hemifusion. J. Biol. Chem. 280, 30538-30541.
    • (2005) J. Biol. Chem , vol.280 , pp. 30538-30541
    • Lu, X.1    Zhang, F.2    McNew, J.A.3    Shin, Y.K.4
  • 41
    • 12644298688 scopus 로고    scopus 로고
    • A conserved domain is present in different families of vesicular fusion proteins: A new superfamily
    • Weimbs, T., Low, S. H., Chapin, S. J., Mostov, K. E., Bucher, P. and Hofmann, K. (1997). A conserved domain is present in different families of vesicular fusion proteins: a new superfamily. Proc. Natl. Acad. Sci. U S A 94, 3046-3051.
    • (1997) Proc. Natl. Acad. Sci. U S A , vol.94 , pp. 3046-3051
    • Weimbs, T.1    Low, S.H.2    Chapin, S.J.3    Mostov, K.E.4    Bucher, P.5    Hofmann, K.6
  • 42
    • 0032559801 scopus 로고    scopus 로고
    • The pathway of membrane fusion catalyzed by influenza hemagglutinin: Restriction of lipids, hemifusion, and lipidic fusion pore formation
    • Chernomordik, L. V., Frolov, V. A., Leikina, E., Bronk, P. and Zimmerberg, J. (1998). The pathway of membrane fusion catalyzed by influenza hemagglutinin: restriction of lipids, hemifusion, and lipidic fusion pore formation. J. Cell Biol. 140, 1369-1382.
    • (1998) J. Cell Biol , vol.140 , pp. 1369-1382
    • Chernomordik, L.V.1    Frolov, V.A.2    Leikina, E.3    Bronk, P.4    Zimmerberg, J.5
  • 43
    • 33746319639 scopus 로고    scopus 로고
    • A clamping mechanism involved in SNARE-dependent exocytosis
    • Giraudo, C. G., Eng, W. S., Melia, T. J. and Rothman, J. E. (2006). A clamping mechanism involved in SNARE-dependent exocytosis. Science 313, 676-680.
    • (2006) Science , vol.313 , pp. 676-680
    • Giraudo, C.G.1    Eng, W.S.2    Melia, T.J.3    Rothman, J.E.4
  • 44
    • 34248209602 scopus 로고    scopus 로고
    • Putting the clamps on membrane fusion: How complexin sets the stage for calcium-mediated exocytosis
    • Melia, T. J., Jr. (2007). Putting the clamps on membrane fusion: how complexin sets the stage for calcium-mediated exocytosis. FEBS Lett. 581, 2131-2139.
    • (2007) FEBS Lett , vol.581 , pp. 2131-2139
    • Melia Jr., T.J.1
  • 45
    • 33746804075 scopus 로고    scopus 로고
    • Hemifusion arrest by complexin is relieved by Ca2+-synaptotagmin I
    • Schaub, J. R., Lu, X., Doneske, B., Shin, Y. K. and McNew, J. A. (2006). Hemifusion arrest by complexin is relieved by Ca2+-synaptotagmin I. Nat. Struct. Mol. Biol. 13, 748-750.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 748-750
    • Schaub, J.R.1    Lu, X.2    Doneske, B.3    Shin, Y.K.4    McNew, J.A.5
  • 48
    • 33746915109 scopus 로고    scopus 로고
    • N- to Cterminal SNARE complex assembly promotes rapid membrane fusion
    • Pobbati, A. V., Stein, A. and Fasshauer, D. (2006). N- to Cterminal SNARE complex assembly promotes rapid membrane fusion. Science 313, 673-676.
    • (2006) Science , vol.313 , pp. 673-676
    • Pobbati, A.V.1    Stein, A.2    Fasshauer, D.3
  • 49
    • 33646151867 scopus 로고    scopus 로고
    • Neuronal SNAREs do not trigger fusion between synthetic membranes but do promote PEG-mediated membrane fusion
    • Dennison, S. M., Bowen, M. E., Brunger, A. T. and Lentz, B. R. (2006). Neuronal SNAREs do not trigger fusion between synthetic membranes but do promote PEG-mediated membrane fusion. Biophys. J. 90, 1661-1675.
    • (2006) Biophys. J , vol.90 , pp. 1661-1675
    • Dennison, S.M.1    Bowen, M.E.2    Brunger, A.T.3    Lentz, B.R.4
  • 50
    • 33646007069 scopus 로고    scopus 로고
    • SNARE-mediated lipid mixing depends on the physical state of the vesicles
    • Chen, X., Arac, D., Wang, T. M., Gilpin, C. J., Zimmerberg, J. and Rizo, J. (2006). SNARE-mediated lipid mixing depends on the physical state of the vesicles. Biophys. J. 90, 2062-2074.
    • (2006) Biophys. J , vol.90 , pp. 2062-2074
    • Chen, X.1    Arac, D.2    Wang, T.M.3    Gilpin, C.J.4    Zimmerberg, J.5    Rizo, J.6
  • 51
    • 35348818630 scopus 로고    scopus 로고
    • Excess vacuolar SNAREs drive lysis and Rab bypass fusion
    • Starai, V. J., Jun, Y. and Wickner, W. (2007). Excess vacuolar SNAREs drive lysis and Rab bypass fusion. Proc. Natl. Acad. Sci. U S A 104, 13551-13558.
    • (2007) Proc. Natl. Acad. Sci. U S A , vol.104 , pp. 13551-13558
    • Starai, V.J.1    Jun, Y.2    Wickner, W.3
  • 53
    • 40649084835 scopus 로고    scopus 로고
    • SNAREpin/Munc18 promotes adhesion and fusion of large vesicles to giant membranes
    • Tareste, D., Shen, J., Melia, T. J. and Rothman, J. E. (2008). SNAREpin/Munc18 promotes adhesion and fusion of large vesicles to giant membranes. Proc. Natl. Acad. Sci. U S A 105, 2380-2385.
    • (2008) Proc. Natl. Acad. Sci. U S A , vol.105 , pp. 2380-2385
    • Tareste, D.1    Shen, J.2    Melia, T.J.3    Rothman, J.E.4
  • 54
    • 33845987734 scopus 로고    scopus 로고
    • Selective activation of cognate SNAREpins by Sec1/Munc18 proteins
    • Shen, J., Tareste, D. C., Paumet, F., Rothman, J. E. and Melia, T. J. (2007). Selective activation of cognate SNAREpins by Sec1/Munc18 proteins. Cell 128, 183-195.
    • (2007) Cell , vol.128 , pp. 183-195
    • Shen, J.1    Tareste, D.C.2    Paumet, F.3    Rothman, J.E.4    Melia, T.J.5
  • 55
    • 34249933061 scopus 로고    scopus 로고
    • How synaptotagmin promotes membrane fusion
    • Martens, S., Kozlov, M. M. and McMahon, H. T. (2007). How synaptotagmin promotes membrane fusion. Science 316, 1205-1208.
    • (2007) Science , vol.316 , pp. 1205-1208
    • Martens, S.1    Kozlov, M.M.2    McMahon, H.T.3
  • 56
    • 1942520207 scopus 로고    scopus 로고
    • Reconstitution of Ca2+-regulated membrane fusion by synaptotagmin and SNAREs
    • Tucker, W. C., Weber, T. and Chapman, E. R. (2004). Reconstitution of Ca2+-regulated membrane fusion by synaptotagmin and SNAREs. Science 304, 435-438.
    • (2004) Science , vol.304 , pp. 435-438
    • Tucker, W.C.1    Weber, T.2    Chapman, E.R.3
  • 57
    • 0034704771 scopus 로고    scopus 로고
    • Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex
    • Misura, K. M., Scheller, R. H. and Weis, W. I. (2000). Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex. Nature 404, 355-362.
    • (2000) Nature , vol.404 , pp. 355-362
    • Misura, K.M.1    Scheller, R.H.2    Weis, W.I.3
  • 59
    • 19544382047 scopus 로고    scopus 로고
    • Arachidonic acid allows SNARE complex formation in the presence of Munc18
    • Rickman, C. and Davletov, B. (2005). Arachidonic acid allows SNARE complex formation in the presence of Munc18. Chem Biol. 12, 545-553.
    • (2005) Chem Biol , vol.12 , pp. 545-553
    • Rickman, C.1    Davletov, B.2
  • 62
    • 0037040873 scopus 로고    scopus 로고
    • Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis
    • Pabst, S., Margittai, M., Vainius, D., Langen, R., Jahn, R. and Fasshauer, D. (2002). Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis. J. Biol. Chem. 277, 7838-7848.
    • (2002) J. Biol. Chem , vol.277 , pp. 7838-7848
    • Pabst, S.1    Margittai, M.2    Vainius, D.3    Langen, R.4    Jahn, R.5    Fasshauer, D.6
  • 65
    • 34250344617 scopus 로고    scopus 로고
    • Atomic force microscope studies of the fusion of floating lipid bilayers
    • Abdulreda, M. H. and Moy, V. T. (2007). Atomic force microscope studies of the fusion of floating lipid bilayers. Biophys. J. 92, 4369-4378.
    • (2007) Biophys. J , vol.92 , pp. 4369-4378
    • Abdulreda, M.H.1    Moy, V.T.2
  • 66
    • 0028587383 scopus 로고
    • Two components of transmitter release at a central synapse
    • Goda, Y. and Stevens, C. F. (1994). Two components of transmitter release at a central synapse. Proc. Natl. Acad. Sci. U S A 91, 12942-12946.
    • (1994) Proc. Natl. Acad. Sci. U S A , vol.91 , pp. 12942-12946
    • Goda, Y.1    Stevens, C.F.2
  • 67
    • 0033681867 scopus 로고    scopus 로고
    • Inhibitory transmission mediated by asynchronous transmitter release
    • Lu, T. and Trussell, L. O. (2000). Inhibitory transmission mediated by asynchronous transmitter release. Neuron 26, 683-694.
    • (2000) Neuron , vol.26 , pp. 683-694
    • Lu, T.1    Trussell, L.O.2
  • 68
    • 35348823114 scopus 로고    scopus 로고
    • Characterization of the role of the Synaptotagmin family as calcium sensors in facilitation and asynchronous neurotransmitter release
    • Saraswati, S., Adolfsen, B. and Littleton, J. T. (2007). Characterization of the role of the Synaptotagmin family as calcium sensors in facilitation and asynchronous neurotransmitter release. Proc. Natl. Acad. Sci. U S A 104, 14122-14127.
    • (2007) Proc. Natl. Acad. Sci. U S A , vol.104 , pp. 14122-14127
    • Saraswati, S.1    Adolfsen, B.2    Littleton, J.T.3
  • 69
    • 33748605056 scopus 로고    scopus 로고
    • A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis
    • Tang, J., Maximov, A., Shin, O. H., Dai, H., Rizo, J. and Sudhof, T. C. (2006). A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis. Cell 126, 1175-1187.
    • (2006) Cell , vol.126 , pp. 1175-1187
    • Tang, J.1    Maximov, A.2    Shin, O.H.3    Dai, H.4    Rizo, J.5    Sudhof, T.C.6
  • 70
    • 36749078085 scopus 로고    scopus 로고
    • A dual-Ca2+-sensor model for neurotransmitter release in a central synapse
    • Sun, J., Pang, Z. P., Qin, D., Fahim, A. T., Adachi, R. and Sudhof, T. C. (2007). A dual-Ca2+-sensor model for neurotransmitter release in a central synapse. Nature 450, 676-682.
    • (2007) Nature , vol.450 , pp. 676-682
    • Sun, J.1    Pang, Z.P.2    Qin, D.3    Fahim, A.T.4    Adachi, R.5    Sudhof, T.C.6
  • 71
    • 0028061861 scopus 로고
    • Synaptotagmin I: A major Ca2+ sensor for transmitter release at a central synapse
    • Geppert, M., Goda, Y., Hammer, R. E., Li, C., Rosahl, T. W., Stevens, C. F. and Sudhof, T. C. (1994). Synaptotagmin I: a major Ca2+ sensor for transmitter release at a central synapse. Cell 79, 717-727.
    • (1994) Cell , vol.79 , pp. 717-727
    • Geppert, M.1    Goda, Y.2    Hammer, R.E.3    Li, C.4    Rosahl, T.W.5    Stevens, C.F.6    Sudhof, T.C.7
  • 73
    • 3042796387 scopus 로고    scopus 로고
    • Synaptotagmin I synchronizes transmitter release in mouse hippocampal neurons
    • Nishiki, T. and Augustine, G. J. (2004). Synaptotagmin I synchronizes transmitter release in mouse hippocampal neurons. J. Neurosci. 24, 6127-6132.
    • (2004) J. Neurosci , vol.24 , pp. 6127-6132
    • Nishiki, T.1    Augustine, G.J.2
  • 74
    • 0037027739 scopus 로고    scopus 로고
    • Synaptotagmin I functions as a calcium sensor to synchronize neurotransmitter release
    • Yoshihara, M. and Littleton, J. T. (2002). Synaptotagmin I functions as a calcium sensor to synchronize neurotransmitter release. Neuron 36, 897-908.
    • (2002) Neuron , vol.36 , pp. 897-908
    • Yoshihara, M.1    Littleton, J.T.2
  • 75
    • 46449093538 scopus 로고    scopus 로고
    • How does synaptotagmin trigger neurotransmitter release?
    • Chapman, E. R. (2008). How does synaptotagmin trigger neurotransmitter release? Annu. Rev. Biochem. 77, 615-641.
    • (2008) Annu. Rev. Biochem , vol.77 , pp. 615-641
    • Chapman, E.R.1
  • 76
    • 33745938170 scopus 로고    scopus 로고
    • Unraveling the mechanisms of synaptotagmin and SNARE function in neurotransmitter release
    • Rizo, J., Chen, X. and Arac, D. (2006). Unraveling the mechanisms of synaptotagmin and SNARE function in neurotransmitter release. Trends Cell Biol. 16, 339-350.
    • (2006) Trends Cell Biol , vol.16 , pp. 339-350
    • Rizo, J.1    Chen, X.2    Arac, D.3
  • 77
    • 27844499290 scopus 로고    scopus 로고
    • Autonomous function of synaptotagmin 1 in triggering synchronous release independent of asynchronous release
    • Maximov, A. and Sudhof, T. C. (2005). Autonomous function of synaptotagmin 1 in triggering synchronous release independent of asynchronous release. Neuron 48, 547-554.
    • (2005) Neuron , vol.48 , pp. 547-554
    • Maximov, A.1    Sudhof, T.C.2
  • 78
    • 0035798162 scopus 로고    scopus 로고
    • Synaptotagmin modulation of fusion pore kinetics in regulated exocytosis of dense-core vesicles
    • Wang, C. T., Grishanin, R., Earles, C. A., Chang, P. Y., Martin, T. F., Chapman, E. R. and Jackson, M. B. (2001). Synaptotagmin modulation of fusion pore kinetics in regulated exocytosis of dense-core vesicles. Science 294, 1111-1115.
    • (2001) Science , vol.294 , pp. 1111-1115
    • Wang, C.T.1    Grishanin, R.2    Earles, C.A.3    Chang, P.Y.4    Martin, T.F.5    Chapman, E.R.6    Jackson, M.B.7
  • 80
    • 0027432376 scopus 로고
    • Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin
    • Blasi, J., Chapman, E. R., Yamasaki, S., Binz, T., Niemann, H. and Jahn, R. (1993). Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin. Embo J. 12, 4821-4828.
    • (1993) Embo J , vol.12 , pp. 4821-4828
    • Blasi, J.1    Chapman, E.R.2    Yamasaki, S.3    Binz, T.4    Niemann, H.5    Jahn, R.6
  • 81
    • 33745029549 scopus 로고    scopus 로고
    • Ca(2+)-synaptotagmin directly regulates t-SNARE function during reconstituted membrane fusion
    • Bhalla, A., Chicka, M. C., Tucker, W. C. and Chapman, E. R. (2006). Ca(2+)-synaptotagmin directly regulates t-SNARE function during reconstituted membrane fusion. Nat. Struct. Mol. Biol. 13, 323-330.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 323-330
    • Bhalla, A.1    Chicka, M.C.2    Tucker, W.C.3    Chapman, E.R.4
  • 82
    • 34948827535 scopus 로고    scopus 로고
    • Synaptotagmin activates membrane fusion through a Ca2+-dependent trans interaction with phospholipids
    • Stein, A., Radhakrishnan, A., Riedel, D., Fasshauer, D. and Jahn, R. (2007). Synaptotagmin activates membrane fusion through a Ca2+-dependent trans interaction with phospholipids. Nat. Struct. Mol. Biol. 14, 904-911.
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 904-911
    • Stein, A.1    Radhakrishnan, A.2    Riedel, D.3    Fasshauer, D.4    Jahn, R.5
  • 83
    • 43449131873 scopus 로고    scopus 로고
    • Synaptic vesicles are constitutively active fusion machines that function independently of Ca2+
    • Holt, M., Riedel, D., Stein, A., Schuette, C. and Jahn, R. (2008). Synaptic vesicles are constitutively active fusion machines that function independently of Ca2+. Curr. Biol. 18, 715-722.
    • (2008) Curr. Biol , vol.18 , pp. 715-722
    • Holt, M.1    Riedel, D.2    Stein, A.3    Schuette, C.4    Jahn, R.5
  • 84
    • 0037157825 scopus 로고    scopus 로고
    • Calcium-independent stimulation of membrane fusion and SNAREpin formation by synaptotagmin I
    • Mahal, L. K., Sequeira, S. M., Gureasko, J. M. and Sollner, T. H. (2002). Calcium-independent stimulation of membrane fusion and SNAREpin formation by synaptotagmin I. J. Cell Biol. 158, 273-282.
    • (2002) J. Cell Biol , vol.158 , pp. 273-282
    • Mahal, L.K.1    Sequeira, S.M.2    Gureasko, J.M.3    Sollner, T.H.4
  • 86
    • 0842291506 scopus 로고    scopus 로고
    • PIP2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane
    • Bai, J., Tucker, W. C. and Chapman, E. R. (2004). PIP2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane. Nat. Struct. Mol. Biol. 11, 36-44.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 36-44
    • Bai, J.1    Tucker, W.C.2    Chapman, E.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.