메뉴 건너뛰기




Volumn 14, Issue 4, 2002, Pages 488-495

Membrane fusion

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; LIPID; PROTEIN; SNARE PROTEIN; MEMBRANE PROTEIN; VESICULAR TRANSPORT PROTEIN;

EID: 0036702301     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(02)00356-3     Document Type: Review
Times cited : (173)

References (75)
  • 1
    • 0030807735 scopus 로고    scopus 로고
    • Structural organization of the synaptic exocytosis core complex
    • Lin R.C., Scheller R.H. 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
  • 2
    • 0033790619 scopus 로고    scopus 로고
    • Yeast homotypic vacuole fusion: A window on organelle trafficking mechanisms
    • Wickner W., Haas A. Yeast homotypic vacuole fusion: a window on organelle trafficking mechanisms. Annu Rev Biochem. 69:2000;247-275.
    • (2000) Annu Rev Biochem , vol.69 , pp. 247-275
    • Wickner, W.1    Haas, A.2
  • 3
    • 0033637985 scopus 로고    scopus 로고
    • The synaptic vesicle cycle revisited
    • Südhof T.C. The synaptic vesicle cycle revisited. Neuron. 28:2000;317-320.
    • (2000) Neuron , vol.28 , pp. 317-320
    • Südhof, T.C.1
  • 4
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel J.J., Wiley D.C. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu Rev Biochem. 69:2000;531-569.
    • (2000) Annu Rev Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 6
    • 0035912729 scopus 로고    scopus 로고
    • A quantitative model for membrane fusion based on low-energy intermediates
    • Kuzmin P.I., Zimmerberg J., Chizmadzhev Y.A., Cohen F.S. A quantitative model for membrane fusion based on low-energy intermediates. Proc Natl Acad Sci USA. 98:2001;7235-7240. See annotation Kozlovsky and Kozlov (2002) [7•].
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 7235-7240
    • Kuzmin, P.I.1    Zimmerberg, J.2    Chizmadzhev, Y.A.3    Cohen, F.S.4
  • 7
    • 0036154247 scopus 로고    scopus 로고
    • Stalk model of membrane fusion: Solution of energy crisis
    • Kozlovsky Y., Kozlov M.M. Stalk model of membrane fusion: solution of energy crisis. Biophys J. 82:2002;882-895. This and the preceding paper (Kuzmin et al. 2001 [6•] ) describe extended continuum models, which include local tilting and out-of-plane motion of lipid molecules and are energetically feasible.
    • (2002) Biophys J , vol.82 , pp. 882-895
    • Kozlovsky, Y.1    Kozlov, M.M.2
  • 8
    • 0034682861 scopus 로고    scopus 로고
    • Formation, stability, and breakup of nanojets
    • Moseler M., Landman U. Formation, stability, and breakup of nanojets. Science. 289:2000;1165-1169.
    • (2000) Science , vol.289 , pp. 1165-1169
    • Moseler, M.1    Landman, U.2
  • 9
    • 0030735760 scopus 로고    scopus 로고
    • Configurations of fluid membranes and vesicles
    • Seifert U. Configurations of fluid membranes and vesicles. Adv Physics. 46:1997;131-137.
    • (1997) Adv Physics , vol.46 , pp. 131-137
    • Seifert, U.1
  • 10
    • 0001666878 scopus 로고    scopus 로고
    • From molecular dynamics to dissipative particle dynamics
    • Flekkoy E.G., Coveney P.V. From molecular dynamics to dissipative particle dynamics. Phys Rev Lett. 83:1999;1775-1778.
    • (1999) Phys Rev Lett , vol.83 , pp. 1775-1778
    • Flekkoy, E.G.1    Coveney, P.V.2
  • 12
    • 0000283071 scopus 로고    scopus 로고
    • Mobility and elasticity of self-assembled membranes
    • Goetz R., Gompper G., Lipowsky R. Mobility and elasticity of self-assembled membranes. Phys Rev Lett. 82:1999;221-224.
    • (1999) Phys Rev Lett , vol.82 , pp. 221-224
    • Goetz, R.1    Gompper, G.2    Lipowsky, R.3
  • 13
    • 0035475929 scopus 로고    scopus 로고
    • Self-assembly of amphiphiles into vesicles: A Brownian dynamics simulation
    • Noguchi H., Takasu M. Self-assembly of amphiphiles into vesicles: a Brownian dynamics simulation. Physical Rev E. 64:2001;041913.
    • (2001) Physical Rev E , vol.64 , pp. 041913
    • Noguchi, H.1    Takasu, M.2
  • 14
    • 0034499269 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the kinetics of spontaneous micelle formation
    • Marrink S.J., Tieleman D.P., Mark A.E. Molecular dynamics simulation of the kinetics of spontaneous micelle formation. J Phys Chem B. 104:2000;12165-12173.
    • (2000) J Phys Chem B , vol.104 , pp. 12165-12173
    • Marrink, S.J.1    Tieleman, D.P.2    Mark, A.E.3
  • 15
    • 0034909360 scopus 로고    scopus 로고
    • Mesoscopic simulation of cell membrane damage, morphology change and rupture by nonionic surfactants
    • Groot R.D., Rabone K.L. Mesoscopic simulation of cell membrane damage, morphology change and rupture by nonionic surfactants. Biophys J. 81:2001;725-736.
    • (2001) Biophys J , vol.81 , pp. 725-736
    • Groot, R.D.1    Rabone, K.L.2
  • 16
    • 0035935803 scopus 로고    scopus 로고
    • Fusion pathways of vesicles: A Brownian dynamics simulation
    • Noguchi H., Takasu M. Fusion pathways of vesicles: a Brownian dynamics simulation. J Chem Phys. 115:2001;9547-9551. This is the first coarse grained/Brownian dynamics simulation of vesicle fusion, showing spontaneous stalk formation. A modified stalk model is supported by the simulations, in which the pore is induced by contact between the distal monolayers.
    • (2001) J Chem Phys , vol.115 , pp. 9547-9551
    • Noguchi, H.1    Takasu, M.2
  • 17
    • 0037040015 scopus 로고    scopus 로고
    • New mechanism of membrane fusion
    • Müller M., Katsov K., Schick M. New mechanism of membrane fusion. J Chem Phys. 116:2002;2342-2345.
    • (2002) J Chem Phys , vol.116 , pp. 2342-2345
    • Müller, M.1    Katsov, K.2    Schick, M.3
  • 18
    • 0035861430 scopus 로고    scopus 로고
    • Reality simulation - Observe while it happens
    • Berendsen H.J.C. Reality simulation - observe while it happens. Science. 294:2001;2304-2305.
    • (2001) Science , vol.294 , pp. 2304-2305
    • Berendsen, H.J.C.1
  • 19
    • 0033637459 scopus 로고    scopus 로고
    • Molecular dynamics generation of nonarbitrary membrane models reveals lipid orientational correlations
    • Takaoka Y., Pasenkiewicz-Gierula M., Miyagawa H., Kitamura K., Tamura Y., Kusumi A. Molecular dynamics generation of nonarbitrary membrane models reveals lipid orientational correlations. Biophys J. 79:2000;3118-3138.
    • (2000) Biophys J , vol.79 , pp. 3118-3138
    • Takaoka, Y.1    Pasenkiewicz-Gierula, M.2    Miyagawa, H.3    Kitamura, K.4    Tamura, Y.5    Kusumi, A.6
  • 20
    • 0033758069 scopus 로고    scopus 로고
    • Molecular dynamics simulations of lipid bilayers
    • Feller S.E. Molecular dynamics simulations of lipid bilayers. Curr Opin Colloid Interface Sci. 5:2000;217-223.
    • (2000) Curr Opin Colloid Interface Sci , vol.5 , pp. 217-223
    • Feller, S.E.1
  • 23
    • 0036200766 scopus 로고    scopus 로고
    • Calculating the bulk modulus for a lipid bilayer with nonequilibrium molecular dynamics simulation
    • Ayton G., Smondyrev A.M., Bardenhagen S.G., McMurtry P., Voth G.A. Calculating the bulk modulus for a lipid bilayer with nonequilibrium molecular dynamics simulation. Biophys J. 82:2002;1226-1238.
    • (2002) Biophys J , vol.82 , pp. 1226-1238
    • Ayton, G.1    Smondyrev, A.M.2    Bardenhagen, S.G.3    McMurtry, P.4    Voth, G.A.5
  • 24
    • 0035201782 scopus 로고    scopus 로고
    • Molecular simulation of dioleoylphosphatidylcholine lipid bilayers at differing levels of hydration
    • Mashl R.J., Scott H.L., Subramaniam S., Jakobsson E. Molecular simulation of dioleoylphosphatidylcholine lipid bilayers at differing levels of hydration. Biophys J. 81:2001;3005-3015.
    • (2001) Biophys J , vol.81 , pp. 3005-3015
    • Mashl, R.J.1    Scott, H.L.2    Subramaniam, S.3    Jakobsson, E.4
  • 25
    • 0035852017 scopus 로고    scopus 로고
    • Molecular dynamics simulation of a lipid diamond cubic phase
    • Marrink S.J., Tieleman D.P. Molecular dynamics simulation of a lipid diamond cubic phase. J Am Chem Soc. 123:2001;12383-12391.
    • (2001) J Am Chem Soc , vol.123 , pp. 12383-12391
    • Marrink, S.J.1    Tieleman, D.P.2
  • 26
    • 0035073937 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the structure of dimyristoyl phosphatidylcholine bilayers with cholesterol, ergosterol, and lanosterol
    • Smondyrev A.M., Berkowitz M.L. Molecular dynamics simulation of the structure of dimyristoyl phosphatidylcholine bilayers with cholesterol, ergosterol, and lanosterol. Biophys J. 80:2001;1649-1658.
    • (2001) Biophys J , vol.80 , pp. 1649-1658
    • Smondyrev, A.M.1    Berkowitz, M.L.2
  • 27
    • 0037116518 scopus 로고    scopus 로고
    • Polyunsaturated fatty acids in lipid bilayers: Intrinsic and environmental contributions to their unique physical properties
    • Feller S.E., Gawrisch K., MacKerell A.D. Polyunsaturated fatty acids in lipid bilayers: Intrinsic and environmental contributions to their unique physical properties. J Am Chem Soc. 124:2002;318-326.
    • (2002) J Am Chem Soc , vol.124 , pp. 318-326
    • Feller, S.E.1    Gawrisch, K.2    MacKerell, A.D.3
  • 28
    • 0034091671 scopus 로고    scopus 로고
    • Protein-induced membrane disorder: A molecular dynamics study of melittin in a dipalmitoylphosphatidyl-choline bilayer
    • Bachar M., Becker O.M. Protein-induced membrane disorder: a molecular dynamics study of melittin in a dipalmitoylphosphatidyl-choline bilayer. Biophys J. 78:2000;1359-1375.
    • (2000) Biophys J , vol.78 , pp. 1359-1375
    • Bachar, M.1    Becker, O.M.2
  • 29
    • 0035812110 scopus 로고    scopus 로고
    • Effect of undulations on surface tension in simulated bilayers
    • Marrink S.J., Mark A.E. Effect of undulations on surface tension in simulated bilayers. J Phys Chem B. 105:2001;6122-6127. This work describes atomistic simulations of a bilayer patch that is large enough (20 nm) to show undulations. In the long wavelength limit, contact to continuum models could be made.
    • (2001) J Phys Chem B , vol.105 , pp. 6122-6127
    • Marrink, S.J.1    Mark, A.E.2
  • 30
    • 0035861454 scopus 로고    scopus 로고
    • Water permeation across biological membranes: Mechanism and dynamics of aquaporin-1 and GlpF
    • de Groot B.L., Grubmüller H. Water permeation across biological membranes: mechanism and dynamics of aquaporin-1 and GlpF. Science. 294:2001;2353-2357.
    • (2001) Science , vol.294 , pp. 2353-2357
    • De Groot, B.L.1    Grubmüller, H.2
  • 31
    • 0034950491 scopus 로고    scopus 로고
    • Fast lipid disorientation at the onset of membrane fusion revealed by molecular dynamics simulations
    • Ohta-Iino S., Pasenkiewicz-Gierula M., Takaoka Y., Miyagawa H., Kitamura K., Kusumi A. Fast lipid disorientation at the onset of membrane fusion revealed by molecular dynamics simulations. Biophys J. 81:2001;217-224.
    • (2001) Biophys J , vol.81 , pp. 217-224
    • Ohta-Iino, S.1    Pasenkiewicz-Gierula, M.2    Takaoka, Y.3    Miyagawa, H.4    Kitamura, K.5    Kusumi, A.6
  • 32
    • 0035812426 scopus 로고    scopus 로고
    • Simulation of the spontaneous aggregation of phospholipids into bilayers
    • Marrink S.J., Lindahl E., Edholm O., Mark A.E. Simulation of the spontaneous aggregation of phospholipids into bilayers. J Am Chem Soc. 123:2001;8638-8639. In this landmark molecular dynamics simulation, spontaneous aggregation of randomly distributed lipids into a bilayer is seen for the first time. The time required for bilayer formation (15 ns) is remarkably short. A transient water pore is observed and identified as the rate-limiting step.
    • (2001) J Am Chem Soc , vol.123 , pp. 8638-8639
    • Marrink, S.J.1    Lindahl, E.2    Edholm, O.3    Mark, A.E.4
  • 33
    • 0029156059 scopus 로고
    • Structure and function of fusion pores in exocytosis and ectoplasmic membrane fusion
    • Lindau M., Almers W. Structure and function of fusion pores in exocytosis and ectoplasmic membrane fusion. Curr Opin Cell Biol. 7:1995;509-517.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 509-517
    • Lindau, M.1    Almers, W.2
  • 34
    • 0025284844 scopus 로고
    • Transmitter release from synapses: Does a preassembled fusion pore initiate exocytosis?
    • Almers W., Tse F.W. Transmitter release from synapses: Does a preassembled fusion pore initiate exocytosis? Neuron. 4:1990;813-818.
    • (1990) Neuron , vol.4 , pp. 813-818
    • Almers, W.1    Tse, F.W.2
  • 35
    • 0035478930 scopus 로고    scopus 로고
    • Regulation of kiss-and-run exocytosis: A switch or a maturation process?
    • Fesce R., Meldolesi J., Valtorta F. Regulation of kiss-and-run exocytosis: a switch or a maturation process? Trends Cell Biol. 11:2001;405.
    • (2001) Trends Cell Biol , vol.11 , pp. 405
    • Fesce, R.1    Meldolesi, J.2    Valtorta, F.3
  • 36
    • 0035252348 scopus 로고    scopus 로고
    • Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion
    • Peters C., Bayer M.J., Buhler S., Andersen J.S., Mann M., Mayer A. Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion. Nature. 409:2001;581-588.
    • (2001) Nature , vol.409 , pp. 581-588
    • Peters, C.1    Bayer, M.J.2    Buhler, S.3    Andersen, J.S.4    Mann, M.5    Mayer, A.6
  • 37
    • 0028353472 scopus 로고
    • The exocytotic fusion pore and neurotransmitter release
    • Monck J.R.F. The exocytotic fusion pore and neurotransmitter release. Neuron. 12:1995;707-716.
    • (1995) Neuron , vol.12 , pp. 707-716
    • Monck, J.R.F.1
  • 38
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson P.I., Roth R., Morisaki H., Jahn R., Heuser J.E. Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell. 90:1997;523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 39
    • 0034700998 scopus 로고    scopus 로고
    • The polar region consecutive to the HIV fusion peptide participates in membrane fusion
    • Peisajovich S.G., Epand R.F., Pritsker M., Shai Y., Epand R.M. The polar region consecutive to the HIV fusion peptide participates in membrane fusion. Biochemistry. 39:2000;1826-1833.
    • (2000) Biochemistry , vol.39 , pp. 1826-1833
    • Peisajovich, S.G.1    Epand, R.F.2    Pritsker, M.3    Shai, Y.4    Epand, R.M.5
  • 40
    • 0034841836 scopus 로고    scopus 로고
    • Membrane fusion between liposomes composed of acidic phospholipids and neutral phospholipids induced by melittin: A differential scanning calorimetric study
    • Higashino Y., Matsui A., Ohki K. Membrane fusion between liposomes composed of acidic phospholipids and neutral phospholipids induced by melittin: a differential scanning calorimetric study. J Biochem. 130:2001;393-397.
    • (2001) J Biochem , vol.130 , pp. 393-397
    • Higashino, Y.1    Matsui, A.2    Ohki, K.3
  • 41
    • 0035838516 scopus 로고    scopus 로고
    • Solid-state nuclear magnetic resonance evidence for an extended beta strand conformation of the membrane-bound HIV-1 fusion peptide
    • Yang J., Gabrys C.M., Weliky D.P. Solid-state nuclear magnetic resonance evidence for an extended beta strand conformation of the membrane-bound HIV-1 fusion peptide. Biochemistry. 40:2001;8126-8137.
    • (2001) Biochemistry , vol.40 , pp. 8126-8137
    • Yang, J.1    Gabrys, C.M.2    Weliky, D.P.3
  • 42
    • 0037869962 scopus 로고    scopus 로고
    • Lipid headgroup spacing and peptide penetration, but not peptide oligomerization, modulate peptide-induced fusion
    • Pecheur E.I., Sainte-Marie J., Bienvenue A., Hoekstra D. Lipid headgroup spacing and peptide penetration, but not peptide oligomerization, modulate peptide-induced fusion. Biochemistry. 38:1999;364-373.
    • (1999) Biochemistry , vol.38 , pp. 364-373
    • Pecheur, E.I.1    Sainte-Marie, J.2    Bienvenue, A.3    Hoekstra, D.4
  • 43
    • 0034462310 scopus 로고    scopus 로고
    • Modulation of membrane curvature by peptides
    • Epand R.M., Epand R.F. Modulation of membrane curvature by peptides. Biopolymers. 55:2000;358-363.
    • (2000) Biopolymers , vol.55 , pp. 358-363
    • Epand, R.M.1    Epand, R.F.2
  • 44
    • 0033560750 scopus 로고    scopus 로고
    • Cytosolic ATPases, p97 and NSF, are sufficient to mediate rapid membrane fusion
    • Otter-Nilsson M., Hendriks R., Pecheur-Huet E.L., Hoekstra D., Nilsson T. Cytosolic ATPases, p97 and NSF, are sufficient to mediate rapid membrane fusion. EMBO J. 18:1999;2074-2083.
    • (1999) EMBO J , vol.18 , pp. 2074-2083
    • Otter-Nilsson, M.1    Hendriks, R.2    Pecheur-Huet, E.L.3    Hoekstra, D.4    Nilsson, T.5
  • 46
    • 0026510747 scopus 로고
    • A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
    • Blobel C.P., Wolfsbrg T.G., Turck C.W., Myles D.G., Primakoff P., White J.M. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature. 356:1992;248-252.
    • (1992) Nature , vol.356 , pp. 248-252
    • Blobel, C.P.1    Wolfsbrg, T.G.2    Turck, C.W.3    Myles, D.G.4    Primakoff, P.5    White, J.M.6
  • 48
    • 0035911963 scopus 로고    scopus 로고
    • UGO1 encodes an outer membrane protein required for mitochondrial fusion
    • Sesaki H., Jensen R.E. UGO1 encodes an outer membrane protein required for mitochondrial fusion. J Cell Biol. 152:2001;1123-1134.
    • (2001) J Cell Biol , vol.152 , pp. 1123-1134
    • Sesaki, H.1    Jensen, R.E.2
  • 49
    • 0035176257 scopus 로고    scopus 로고
    • Dynamics of peroxisome assembly and function
    • Titorenko V.I., Rachubinski R.A. Dynamics of peroxisome assembly and function. Trends Cell Biol. 11:2001;22-29.
    • (2001) Trends Cell Biol , vol.11 , pp. 22-29
    • Titorenko, V.I.1    Rachubinski, R.A.2
  • 50
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn R., Südhof T.C. Membrane fusion and exocytosis. Annu Rev Biochem. 68:1999;863-911.
    • (1999) Annu Rev Biochem , vol.68 , pp. 863-911
    • Jahn, R.1    Südhof, T.C.2
  • 52
    • 0035279058 scopus 로고    scopus 로고
    • SNAREs and the specificity of membrane fusion
    • Pelham H.R. SNAREs and the specificity of membrane fusion. Trends Cell Biol. 11:2001;99-101.
    • (2001) Trends Cell Biol , vol.11 , pp. 99-101
    • Pelham, H.R.1
  • 53
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a core synaptic fusion complex at 2.4 Å resolution
    • Sutton B., Fasshauer D., Jahn R., Brünger A.T. Crystal structure of a core synaptic fusion complex at 2.4 Å resolution. Nature. 395:1998;347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, B.1    Fasshauer, D.2    Jahn, R.3    Brünger, A.T.4
  • 54
    • 0036166318 scopus 로고    scopus 로고
    • Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs
    • Antonin W., Fasshauer D., Becker S., Jahn R., Schneider T.R. Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs. Nat Struct Biol. 9:2002;107-111. This paper contains a description of a second high-resolution structure of a SNARE complex showing an extraordinary degree of structural conservation despite limited sequence homology.
    • (2002) Nat Struct Biol , vol.9 , pp. 107-111
    • Antonin, W.1    Fasshauer, D.2    Becker, S.3    Jahn, R.4    Schneider, T.R.5
  • 55
    • 0036169077 scopus 로고    scopus 로고
    • SNARE assembly and disassembly exhibit a pronounced hysteresis
    • Fasshauer D., Antonin W., Subramaniam V., Jahn R. SNARE assembly and disassembly exhibit a pronounced hysteresis. Nat Struct Biol. 9:2002;144-151.
    • (2002) Nat Struct Biol , vol.9 , pp. 144-151
    • Fasshauer, D.1    Antonin, W.2    Subramaniam, V.3    Jahn, R.4
  • 56
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation and fusion
    • Söllner T., Bennet M.K., Whiteheart S.W., Scheller R.H., Rothman J.E. A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation and fusion. Cell. 75:1993;409-418.
    • (1993) Cell , vol.75 , pp. 409-418
    • Söllner, T.1    Bennet, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 58
    • 0037033997 scopus 로고    scopus 로고
    • Vesicular restriction of synaptobrevin suggests a role for calcium in membrane fusion
    • Hu K., Carroll J., Gedorovich S., Rickman C., Sukhodub A., Davletov B. Vesicular restriction of synaptobrevin suggests a role for calcium in membrane fusion. Nature. 415:2002;646-650. Purified synaptic vesicles fuse with liposomes carrying the SNAREs SNAP-25 and syntaxin 1 in a calcium- and SNARE-dependent manner. In this study, several elements of neuronal exocytosis have been reconstituted in an artificial system, setting the stage for more refined reconstitution experiments using predefined components.
    • (2002) Nature , vol.415 , pp. 646-650
    • Hu, K.1    Carroll, J.2    Gedorovich, S.3    Rickman, C.4    Sukhodub, A.5    Davletov, B.6
  • 59
    • 0034675978 scopus 로고    scopus 로고
    • Geranylgeranylated SNAREs are dominant inhibitors of membrane fusion
    • Grote E., Baba M., Ohsumi Y., Novick P.J. Geranylgeranylated SNAREs are dominant inhibitors of membrane fusion. J Cell Biol. 151:2000;453-466.
    • (2000) J Cell Biol , vol.151 , pp. 453-466
    • Grote, E.1    Baba, M.2    Ohsumi, Y.3    Novick, P.J.4
  • 60
    • 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., Rothman J.E. Close is not enough: SNARE-dependent membrane fusion requires an active mechanism that transduces force to membrane anchors. J Cell Biol. 150:2000;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
  • 61
    • 0033197735 scopus 로고    scopus 로고
    • The length of the flexible SNAREpin juxtamembrane region is a critical determinant of SNARE-dependent fusion
    • McNew J.A., Weber T., Engelman D.M., Sollner T.H., Rothman J.E. The length of the flexible SNAREpin juxtamembrane region is a critical determinant of SNARE-dependent fusion. Mol Cell. 4:1999;415-421.
    • (1999) Mol Cell , vol.4 , pp. 415-421
    • McNew, J.A.1    Weber, T.2    Engelman, D.M.3    Sollner, T.H.4    Rothman, J.E.5
  • 62
    • 0035943407 scopus 로고    scopus 로고
    • Peptide mimics of SNARE transmembrane segments drive membrane fusion depending on their conformational plasticity
    • Langosch D., Crane J.M., Brosig B., Hellwig A., Tamm L.K., Reed J. Peptide mimics of SNARE transmembrane segments drive membrane fusion depending on their conformational plasticity. J Mol Biol. 311:2001;709-721. Peptides corresponding to the transmembrane regions of SNAREs are shown to induce the fusion of liposomes. Although the biological significance of these findings remains to be established, they document that the role of the transmembrane domains may not be confined to anchoring the proteins in the membrane. Instead, they may be directly involved in the fusion reaction, lending further support to the view that the SNAREs are functioning as fusion proteins.
    • (2001) J Mol Biol , vol.311 , pp. 709-721
    • Langosch, D.1    Crane, J.M.2    Brosig, B.3    Hellwig, A.4    Tamm, L.K.5    Reed, J.6
  • 63
    • 0033790619 scopus 로고    scopus 로고
    • Yeast homotypic vacuole fusion: A window on organelle trafficking mechanisms
    • Wickner W., Haas A. Yeast homotypic vacuole fusion: a window on organelle trafficking mechanisms. Annu Rev Biochem. 69:2000;247-275.
    • (2000) Annu Rev Biochem , vol.69 , pp. 247-275
    • Wickner, W.1    Haas, A.2
  • 65
    • 0032506349 scopus 로고    scopus 로고
    • 2+/calmodulin signals the completion docking and triggers a late step of vacuole fusion
    • 2+/calmodulin signals the completion docking and triggers a late step of vacuole fusion. Nature. 396:1998;575-580.
    • (1998) Nature , vol.396 , pp. 575-580
    • Peters, C.1    Mayer, A.2
  • 66
    • 0035876373 scopus 로고    scopus 로고
    • Vac8p release from the SNARE complex and its palmitoylation are coupled and essential for vacuole fusion
    • Veit M., Laage R., Dietrich L., Wang L., Ungermann C. Vac8p release from the SNARE complex and its palmitoylation are coupled and essential for vacuole fusion. EMBO J. 20:2001;3145-3155.
    • (2001) EMBO J , vol.20 , pp. 3145-3155
    • Veit, M.1    Laage, R.2    Dietrich, L.3    Wang, L.4    Ungermann, C.5
  • 67
    • 0035860689 scopus 로고    scopus 로고
    • Fusion of docked membranes requires the armadillo repeat protein Vac8p
    • Wang Y.X., Kauffman E.J., Duex J.E., Weisman L.S. Fusion of docked membranes requires the armadillo repeat protein Vac8p. J Biol Chem. 276:2001;35133-35140.
    • (2001) J Biol Chem , vol.276 , pp. 35133-35140
    • Wang, Y.X.1    Kauffman, E.J.2    Duex, J.E.3    Weisman, L.S.4
  • 68
    • 0032506543 scopus 로고    scopus 로고
    • Defining the functions of trans-SNARE pairs
    • Ungermann C., Sato K., Wickner W. Defining the functions of trans-SNARE pairs. Nature. 396:1998;543-548.
    • (1998) Nature , vol.396 , pp. 543-548
    • Ungermann, C.1    Sato, K.2    Wickner, W.3
  • 69
    • 0035860689 scopus 로고    scopus 로고
    • Fusion of docked membranes requires the armadillo repeat protein Vac8p
    • Wang Y.X., Kauffman E.J., Duex J.E., Weisman L.S. Fusion of docked membranes requires the armadillo repeat protein Vac8p. J Biol Chem. 276:2001;35133-35140.
    • (2001) J Biol Chem , vol.276 , pp. 35133-35140
    • Wang, Y.X.1    Kauffman, E.J.2    Duex, J.E.3    Weisman, L.S.4
  • 70
    • 0035860783 scopus 로고    scopus 로고
    • Genetic interactions with the yeast Q-SNARE VTI1 reveal novel functions for the R-SNARE YKT6
    • Dilcher M., Kohler B., von Mollard G.F. Genetic interactions with the yeast Q-SNARE VTI1 reveal novel functions for the R-SNARE YKT6. J Biol Chem. 276:2001;34537-34544.
    • (2001) J Biol Chem , vol.276 , pp. 34537-34544
    • Dilcher, M.1    Kohler, B.2    Von Mollard, G.F.3
  • 71
    • 0034623062 scopus 로고    scopus 로고
    • Assembly of SNARE core complexes prior to neurotransmitter release sets the readily releasable pool of synaptic vesicles
    • Lonart G., Südhof T.C. Assembly of SNARE core complexes prior to neurotransmitter release sets the readily releasable pool of synaptic vesicles. J Biol Chem. 275:2000;27703-27707.
    • (2000) J Biol Chem , vol.275 , pp. 27703-27707
    • Lonart, G.1    Südhof, T.C.2
  • 72
    • 0033598965 scopus 로고    scopus 로고
    • Inhibition of SNARE complex assembly differentially affects kinetic components of exocytosis
    • Xu T., Rammner B., Margittai M., Artalejo A.R., Neher E., Jahn R. 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    Rammner, B.2    Margittai, M.3    Artalejo, A.R.4    Neher, E.5    Jahn, R.6
  • 73
    • 0028815501 scopus 로고
    • Targeted expression of tetanus toxin light chain in Drosophila specifically eliminates synaptic transmission and causes behavioral defects
    • Sweeney S.T., Broadie K., Keane J., Niemann H., O'Kane C.J. Targeted expression of tetanus toxin light chain in Drosophila specifically eliminates synaptic transmission and causes behavioral defects. Neuron. 14:1995;341-351.
    • (1995) Neuron , vol.14 , pp. 341-351
    • Sweeney, S.T.1    Broadie, K.2    Keane, J.3    Niemann, H.4    O'Kane, C.J.5
  • 75
    • 0036138744 scopus 로고    scopus 로고
    • Genetic ablation of the t-SNARE SNAP-25 distinguishes mechanisms of neuroexocytosis
    • Washbourne P., Thompson P.M., Carta M., Costa E.T., Mathews J.R., Lopez-Bendito G., Molnar Z., Becher M.W., Valenzuela C.F., Partridge L.D., Wilson M.C. Genetic ablation of the t-SNARE SNAP-25 distinguishes mechanisms of neuroexocytosis. Nat Neurosci. 5:2002;19-26. This and the preceeding paper (Schoch et al. 2001 [74•] ) describe the effects of deleting synaptobrevin and SNAP-25, two SNAREs functioning in neuronal exocytosis, in mice. Although evoked transmitter release is abolished, some fusion activity remains.
    • (2002) Nat Neurosci , vol.5 , pp. 19-26
    • Washbourne, P.1    Thompson, P.M.2    Carta, M.3    Costa, E.T.4    Mathews, J.R.5    Lopez-Bendito, G.6    Molnar, Z.7    Becher, M.W.8    Valenzuela, C.F.9    Partridge, L.D.10    Wilson, M.C.11


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.