메뉴 건너뛰기




Volumn 91, Issue 8, 2006, Pages 2910-2918

Conical electron tomography of a chemical synapse: Vesicles docked to the active zone are hemi-fused

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CELL MEMBRANE; CONTROLLED STUDY; ELECTRON BEAM TOMOGRAPHY; MEMBRANE VESICLE; MOTOR CORTEX; NEOCORTEX; NONHUMAN; PRESYNAPTIC MEMBRANE; RAT; SYNAPTIC MEMBRANE;

EID: 33749525657     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.084814     Document Type: Article
Times cited : (74)

References (52)
  • 1
    • 0015216477 scopus 로고
    • Quantal mechanism of neural transmitter release
    • Katz, B. 1971. Quantal mechanism of neural transmitter release. Science. 173:123-126.
    • (1971) Science , vol.173 , pp. 123-126
    • Katz, B.1
  • 2
    • 0038290760 scopus 로고    scopus 로고
    • Protein-lipid interplay in fusion and fission of biological membranes
    • Chernomordik, L. V., and M. M. Kozlov. 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
  • 3
    • 2942635759 scopus 로고    scopus 로고
    • The energetic of membrane fusion from binding, through hemifusion, pore formation, and pore enlargement
    • Cohen, F. S., and G. B. Melikyan. 2004. The energetic 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
  • 4
    • 2142712534 scopus 로고    scopus 로고
    • Energetics of vesicle fusion intermediaries: Comparison of calculations with observed effects of osmotic and curvature stresses
    • Malinin, V. S., and B. R. Lentz. 2004. Energetics of vesicle fusion intermediaries: comparison of calculations with observed effects of osmotic and curvature stresses. Biophys. J. 86:2951-2964.
    • (2004) Biophys. J. , vol.86 , pp. 2951-2964
    • Malinin, V.S.1    Lentz, B.R.2
  • 5
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Sudhof, T. C. 1995. The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature. 375:645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Sudhof, T.C.1
  • 6
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn, R., and T. C. Sudhof. 1999. Membrane fusion and exocytosis. Annu. Rev. Biochem. 68:863-911.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 863-911
    • Jahn, R.1    Sudhof, T.C.2
  • 7
    • 0037459076 scopus 로고    scopus 로고
    • Membrane fusion
    • Jahn, R., T. Lang, and T. C. Sudhof. 2003. Membrane fusion. Cell. 112:519-533.
    • (2003) Cell , vol.112 , pp. 519-533
    • Jahn, R.1    Lang, T.2    Sudhof, T.C.3
  • 8
    • 0037672843 scopus 로고    scopus 로고
    • The molecular machinery of synaptic vesicle exocytosis
    • Li, L., and L.-S. Chin. 2003. The molecular machinery of synaptic vesicle exocytosis. Cell. Mol. Life Sci. 60:942-960.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 942-960
    • Li, L.1    Chin, L.-S.2
  • 9
    • 27544473312 scopus 로고    scopus 로고
    • Membrane hemifusion: Crossing a chasm in two leaps
    • Chernomordik, L. V., and M. M. Kozlov. 2005. Membrane hemifusion: crossing a chasm in two leaps. Neuron. 123:375-382.
    • (2005) Neuron , vol.123 , pp. 375-382
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 10
    • 0035252348 scopus 로고    scopus 로고
    • Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion
    • Peters, C., M. J. Bayer, S. Buhler, J. S. Andersen, M. Mann, and A. Mayer. 2001. Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion. Nature. 409:581-588.
    • (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
  • 12
    • 0029148061 scopus 로고
    • The hemifusion intermediary and its conversion to complete fusion: Regulation by membrane composition
    • Chernomordik, L., A. Chanturiya, J. Green, and J. Zimmerberg. 1995. The hemifusion intermediary and its conversion to complete fusion: regulation by membrane composition. Biophys. J. 69:922-929.
    • (1995) Biophys. J. , vol.69 , pp. 922-929
    • Chernomordik, L.1    Chanturiya, A.2    Green, J.3    Zimmerberg, J.4
  • 13
    • 0018889616 scopus 로고
    • Fusion of phospholipids vesicles with planar phospholipids bilayer membranes. II. Incorporation of a vesicular membrane marker into the planar membrane
    • Cohen, F. S., J. Zimmerberg, and A. Finkelstein. 1980. Fusion of phospholipids vesicles with planar phospholipids bilayer membranes. II. Incorporation of a vesicular membrane marker into the planar membrane. J. Gen. Physiol. 75:251-270.
    • (1980) J. Gen. Physiol. , vol.75 , pp. 251-270
    • Cohen, F.S.1    Zimmerberg, J.2    Finkelstein, A.3
  • 14
    • 0030943586 scopus 로고    scopus 로고
    • Evolution of lipidic structures during model membrane fusion and the relation of this process to cell membrane fusion
    • Lee, J., and B. R. Lentz. 1997. Evolution of lipidic structures during model membrane fusion and the relation of this process to cell membrane fusion. Biochemistry. 36:6251-6259.
    • (1997) Biochemistry , vol.36 , pp. 6251-6259
    • Lee, J.1    Lentz, B.R.2
  • 15
    • 0028179011 scopus 로고
    • Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion
    • Kemble, G. W., T. Danieli, and J. M. White. 1994. Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion. Cell. 76:383-391.
    • (1994) Cell , vol.76 , pp. 383-391
    • Kemble, G.W.1    Danieli, T.2    White, J.M.3
  • 16
    • 70449246410 scopus 로고
    • The ultrastructure of cell membranes and their derivatives
    • Robertson, J. D. 1959. The ultrastructure of cell membranes and their derivatives. Biochem. Soc. Symp. 16:3-43.
    • (1959) Biochem. Soc. Symp. , vol.16 , pp. 3-43
    • Robertson, J.D.1
  • 17
    • 0023085227 scopus 로고
    • The early days of electron microscopy of nerve tissue and membranes
    • Robertson, J. D. 1987. The early days of electron microscopy of nerve tissue and membranes. Int. Rev. Cytol. 100:129-201.
    • (1987) Int. Rev. Cytol. , vol.100 , pp. 129-201
    • Robertson, J.D.1
  • 18
    • 11144223254 scopus 로고    scopus 로고
    • Conical tomography of freeze-fracture replicas: A method for the study of integral membrane proteins inserted in phospholipid bilayers
    • Lanzavecchia, S., F. Cantele, P. L. Bellon, L. Zampighi, M. Kreman, E. M. Wright, and G. A. Zampighi. 2005. Conical tomography of freeze-fracture replicas: a method for the study of integral membrane proteins inserted in phospholipid bilayers. J. Struct. Biol. 149:87-98.
    • (2005) J. Struct. Biol. , vol.149 , pp. 87-98
    • Lanzavecchia, S.1    Cantele, F.2    Bellon, P.L.3    Zampighi, L.4    Kreman, M.5    Wright, E.M.6    Zampighi, G.A.7
  • 22
    • 0024312337 scopus 로고
    • The structural organization and protein composition of lens fiber junctions
    • Zampighi, G. A., J. E. Hall, G. R. Ehring, and S. A. Simon. 1989. The structural organization and protein composition of lens fiber junctions. J. Cell Biol. 108:2255-2275.
    • (1989) J. Cell Biol. , vol.108 , pp. 2255-2275
    • Zampighi, G.A.1    Hall, J.E.2    Ehring, G.R.3    Simon, S.A.4
  • 23
    • 0030788352 scopus 로고    scopus 로고
    • Polyhedral protein cages encase synaptic vesicles and mediate their docking to the pre-synaptic membrane
    • Zampighi, G. A., and R. S. Fisher. 1997. Polyhedral protein cages encase synaptic vesicles and mediate their docking to the pre-synaptic membrane. J. Struct. Biol. 119:347-359.
    • (1997) J. Struct. Biol. , vol.119 , pp. 347-359
    • Zampighi, G.A.1    Fisher, R.S.2
  • 24
    • 0014425842 scopus 로고
    • The interaction of aldehydes with collagen
    • Bowes, J. H., and C. W. Carter. 1968. The interaction of aldehydes with collagen. Biochim. Biophys. Acta. 168:322-341.
    • (1968) Biochim. Biophys. Acta , vol.168 , pp. 322-341
    • Bowes, J.H.1    Carter, C.W.2
  • 25
    • 0014310023 scopus 로고
    • Reaction of proteins with glutaraldehyde
    • Habeeb, A. F., and R. Hiramoto. 1968. Reaction of proteins with glutaraldehyde. Arch. Biochem. Biophys. 126:1-16.
    • (1968) Arch. Biochem. Biophys. , vol.126 , pp. 1-16
    • Habeeb, A.F.1    Hiramoto, R.2
  • 26
    • 0015361553 scopus 로고
    • Theoretical and practical aspects of glutaraldehyde fixation
    • Hopwood, D. 1972. Theoretical and practical aspects of glutaraldehyde fixation. Histochem. J. 4:99-127.
    • (1972) Histochem. J. , vol.4 , pp. 99-127
    • Hopwood, D.1
  • 27
    • 84975372121 scopus 로고
    • Osmium saure-ester alsmischerproducte beir oxidation
    • Criegee, R. 1936. Osmium saure-ester alsmischerproducte beir oxidation. [Osmium acid-ester as byproduct of oxidation.]. Ann. Chem. 522:75-96.
    • (1936) Ann. Chem. , vol.522 , pp. 75-96
    • Criegee, R.1
  • 28
    • 84966303964 scopus 로고
    • Zur kentniss der organischer osmium-verbinguen gen
    • Criegee, R., B. Marchand, and H. Wannowius. 1942. Zur kentniss der organischer osmium-verbinguen gen. [On organic osmium compounds.]. Ann. Chem. 550:99-133.
    • (1942) Ann. Chem. , vol.550 , pp. 99-133
    • Criegee, R.1    Marchand, B.2    Wannowius, H.3
  • 29
    • 0002580515 scopus 로고
    • Weighted back-projection methods
    • J. Frank, editor. Plenum Press, New York
    • Radermacher, M. 1992. Weighted back-projection methods. In Electron Tomography. J. Frank, editor. Plenum Press, New York.
    • (1992) Electron Tomography
    • Radermacher, M.1
  • 30
    • 0023090371 scopus 로고
    • Similarity measures between images
    • van Heel, M. 1987. Similarity measures between images. Ultramicroscopy. 21:95-100.
    • (1987) Ultramicroscopy , vol.21 , pp. 95-100
    • Van Heel, M.1
  • 31
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single particle reconstructions
    • Ludtke, S. J., P. R. Baldwin, and W. Chin. 1999. EMAN: semiautomated software for high-resolution single particle reconstructions. J. Struct. Biol. 128:82-97.
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chin, W.3
  • 32
    • 0035783171 scopus 로고    scopus 로고
    • BSOFT: Image and molecular processing in electron microscopy
    • Heyman, B. J. 2001. BSOFT: image and molecular processing in electron microscopy. J. Struct. Biol. 133:156-169.
    • (2001) J. Struct. Biol. , vol.133 , pp. 156-169
    • Heyman, B.J.1
  • 33
    • 0001339881 scopus 로고
    • Three-dimensional reconstruction of single particles from random and non-random tilt series
    • Radermacher, M. 1988. Three-dimensional reconstruction of single particles from random and non-random tilt series. J. Electron Microsc. Tech. 9:359-394.
    • (1988) J. Electron Microsc. Tech. , vol.9 , pp. 359-394
    • Radermacher, M.1
  • 34
    • 0000782743 scopus 로고
    • Ultrastructure of retinal rod synapses of Guinea-pig eye
    • Sjostrand, F. S. 1953. Ultrastructure of retinal rod synapses of Guinea-pig eye. J. Appl. Phys. 24:1422-1423.
    • (1953) J. Appl. Phys. , vol.24 , pp. 1422-1423
    • Sjostrand, F.S.1
  • 36
    • 0001209075 scopus 로고
    • The granule cells, mossy synapses and Purkinje spine synapses of the cerebellum: Light and electron microscope observations
    • Gray, E. G. 1963. The granule cells, mossy synapses and Purkinje spine synapses of the cerebellum: light and electron microscope observations. J. Anat. (Lond.). 97:101-106.
    • (1963) J. Anat. (Lond.) , vol.97 , pp. 101-106
    • Gray, E.G.1
  • 37
    • 0343006587 scopus 로고
    • Principaux criteres morphologiques et cytochimiques utilisables aujourd'hui pour definir les divers types de synapses
    • Couteaux, R. 1961. Principaux criteres morphologiques et cytochimiques utilisables aujourd'hui pour definir les divers types de synapses. [Principal morphological and cytochemical criteria to define the diverse types of synapses.]. Acta Neurophysiol. 3:143-173.
    • (1961) Acta Neurophysiol. , vol.3 , pp. 143-173
    • Couteaux, R.1
  • 38
    • 0019424604 scopus 로고
    • Structural changes after transmitter release at the frog neuromuscular junction
    • Heuser, J. E., and T. S. Reese. 1981. Structural changes after transmitter release at the frog neuromuscular junction. J. Cell Biol. 88:564-580.
    • (1981) J. Cell Biol. , vol.88 , pp. 564-580
    • Heuser, J.E.1    Reese, T.S.2
  • 39
    • 0034517694 scopus 로고    scopus 로고
    • Size of vesicular pools, rates of mobilization, and recycling and neuromuscular synapses of a Drosophila mutant, shibire
    • Delgado, R., C. Maureira, C. Oliva, Y. Kidokoro, and P. Labarca. 2000. Size of vesicular pools, rates of mobilization, and recycling and neuromuscular synapses of a Drosophila mutant, shibire. Neuron. 28:941-953.
    • (2000) Neuron , vol.28 , pp. 941-953
    • Delgado, R.1    Maureira, C.2    Oliva, C.3    Kidokoro, Y.4    Labarca, P.5
  • 40
    • 0035095914 scopus 로고    scopus 로고
    • Molecular correlates of functionally defined synaptic vesicle populations
    • Schikorski, T., and C. F. Stevens. 2001. Molecular correlates of functionally defined synaptic vesicle populations. Nat. Neurosci. 4:391-395.
    • (2001) Nat. Neurosci. , vol.4 , pp. 391-395
    • Schikorski, T.1    Stevens, C.F.2
  • 42
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
    • Sutton, R. B., D. Fasshauser, R. Jahn, and A. T. Brunger. 1998. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution. Nature. 395:347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauser, D.2    Jahn, R.3    Brunger, A.T.4
  • 44
    • 24044530897 scopus 로고    scopus 로고
    • Membrane fusion induced by neuronal SNAREs transits through hemifusion
    • Lu, X., F. Zhang, J. A. McNew, and Y.-K. Shin. 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
  • 46
    • 33646151867 scopus 로고    scopus 로고
    • Neuronal SNAREs do not trigger fusion between synthetic membranes but do promote PEG-mediated membrane fusion
    • Dennison, M. S., M. E. Bowen, A. T. Brunger, and B. R. Lentz. 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, M.S.1    Bowen, M.E.2    Brunger, A.T.3    Lentz, B.R.4
  • 48
    • 22944485726 scopus 로고    scopus 로고
    • Trans-SNARE pairing can precede a hemifusion intermediary in intracellular membrane fusion
    • Reese, C., F. Heise, and A. Mayer. 2005. Trans-SNARE pairing can precede a hemifusion intermediary in intracellular membrane fusion. Nature. 436:410-414.
    • (2005) Nature , vol.436 , pp. 410-414
    • Reese, C.1    Heise, F.2    Mayer, A.3
  • 49
    • 0014026167 scopus 로고
    • Cytochemistry of synapses: A selective staining method for electron microscopy
    • Bloom, F. E., and G. K. Aghajanian. 1966. Cytochemistry of synapses: a selective staining method for electron microscopy. Science. 154:1575-1577.
    • (1966) Science , vol.154 , pp. 1575-1577
    • Bloom, F.E.1    Aghajanian, G.K.2
  • 50
    • 0015401816 scopus 로고
    • The fine structure of freeze-fractured presynaptic membranes
    • Pfenninger, K., K. Akert, H. Moor, and C. Sandri. 1972. The fine structure of freeze-fractured presynaptic membranes. J. Neurocytol. 1:129-149.
    • (1972) J. Neurocytol. , vol.1 , pp. 129-149
    • Pfenninger, K.1    Akert, K.2    Moor, H.3    Sandri, C.4
  • 52
    • 0036841175 scopus 로고    scopus 로고
    • Lipid intermediaries in membrane fusion: Formation, structure, and decay of the hemifusion diaphragm
    • Kozlovsky, Y., L. V. Chernomordik, and M. M. Kozlov. 2002. Lipid intermediaries in membrane fusion: formation, structure, and decay of the hemifusion diaphragm. Biophys. J. 83:882-895.
    • (2002) Biophys. J. , vol.83 , pp. 882-895
    • Kozlovsky, Y.1    Chernomordik, L.V.2    Kozlov, M.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.