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Volumn 53, Issue 47, 2014, Pages 12676-12694

The Principle of Membrane Fusion in the Cell (Nobel Lecture)

Author keywords

cellular biology; membrane fusion; Nobel lecture; SNARE; vesicle transport

Indexed keywords

ANIMAL; AWARDS AND PRIZES; CELLS; CYTOLOGY; HUMAN; MEMBRANE FUSION; METABOLISM;

EID: 84935457039     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201402380     Document Type: Article
Times cited : (123)

References (53)
  • 1
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein synthesis
    • "Intracellular aspects of the process of protein synthesis":, G. Palade, Science 1975, 189, 347-358.
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.1
  • 2
    • 0000636835 scopus 로고
    • Yolk protein uptake in the oocyte of the mosquito Aedes Aegypti L.
    • "Yolk protein uptake in the oocyte of the mosquito Aedes Aegypti L.":, T. Roth, K. Porter, J. Cell Biol. 1964, 20, 313-332.
    • (1964) J. Cell Biol. , vol.20 , pp. 313-332
    • Roth, T.1    Porter, K.2
  • 3
    • 0006496113 scopus 로고
    • Clathrin: A unique protein associated with intracellular transfer of membrane by coated vesicles
    • "Clathrin: A unique protein associated with intracellular transfer of membrane by coated vesicles":, B. Pearse, Proc. Natl. Acad. Sci. USA 1976, 73, 1255-1259.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 1255-1259
    • Pearse, B.1
  • 4
    • 0019866089 scopus 로고
    • Transient activity of Golgi-like membranes as donors of vesicular stomatitis viral glycoprotein in vitro
    • "Transient activity of Golgi-like membranes as donors of vesicular stomatitis viral glycoprotein in vitro":, E. Fries, J. Rothman, J. Cell Biol. 1981, 90, 697-704.
    • (1981) J. Cell Biol. , vol.90 , pp. 697-704
    • Fries, E.1    Rothman, J.2
  • 5
    • 0009355284 scopus 로고
    • Transport of vesicular stomatitis virus glycoprotein in a cell-free extract
    • "Transport of vesicular stomatitis virus glycoprotein in a cell-free extract":, E. Fries, J. Rothman, Proc. Natl. Acad. Sci. USA 1980, 77, 3870-3874.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 3870-3874
    • Fries, E.1    Rothman, J.2
  • 7
    • 0018930046 scopus 로고
    • The identification of 23 complementation groups required for post-translocational events in the yeast secretory pathway
    • "The identification of 23 complementation groups required for post-translocational events in the yeast secretory pathway":, P. Novick, C. Field, R. Schekman, Cell 1980, 21, 205-215.
    • (1980) Cell , vol.21 , pp. 205-215
    • Novick, P.1    Field, C.2    Schekman, R.3
  • 8
    • 0021738607 scopus 로고
    • Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine
    • "Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine":, W. Balch, W. Dunphy, W. Braell, J. Rothman, Cell 1984, 39, 405-416.
    • (1984) Cell , vol.39 , pp. 405-416
    • Balch, W.1    Dunphy, W.2    Braell, W.3    Rothman, J.4
  • 9
    • 0021741764 scopus 로고
    • Sequential intermediates in the pathway of intercompartmental transport in a cell-free system
    • "Sequential intermediates in the pathway of intercompartmental transport in a cell-free system":, W. Balch, B. Glick, J. Rothman, Cell 1984, 39, 525-536.
    • (1984) Cell , vol.39 , pp. 525-536
    • Balch, W.1    Glick, B.2    Rothman, J.3
  • 10
    • 0021713454 scopus 로고
    • The glycoprotein that is transported between successive compartments of the Golgi in a cell-free system resides in stacks of cisternae
    • "The glycoprotein that is transported between successive compartments of the Golgi in a cell-free system resides in stacks of cisternae":, W. Braell, W. Balch, D. Dobbertin, J. Rothman, Cell 1984, 39, 511-524.
    • (1984) Cell , vol.39 , pp. 511-524
    • Braell, W.1    Balch, W.2    Dobbertin, D.3    Rothman, J.4
  • 11
    • 0024966027 scopus 로고
    • Dissection of a single round of vesicular transport: Sequential intermediates for intercisternal movement in the Golgi stack
    • "Dissection of a single round of vesicular transport: Sequential intermediates for intercisternal movement in the Golgi stack":, L. Orci, V. Malhotra, M. Amherdt, T. Serafini, J. Rothman, Cell 1989, 56, 357-368.
    • (1989) Cell , vol.56 , pp. 357-368
    • Orci, L.1    Malhotra, V.2    Amherdt, M.3    Serafini, T.4    Rothman, J.5
  • 12
    • 0023052287 scopus 로고
    • A new type of coated vesicular carrier that ap-pears not to contain clathrin: Its possible role in protein transport within the Golgi stack
    • "A new type of coated vesicular carrier that ap-pears not to contain clathrin: Its possible role in protein transport within the Golgi stack":, L. Orci, B. Glick, J. Rothman, Cell 1986, 46, 171-184.
    • (1986) Cell , vol.46 , pp. 171-184
    • Orci, L.1    Glick, B.2    Rothman, J.3
  • 15
    • 0024340753 scopus 로고
    • Purification of a novel class of coated vesicles mediating biosynthetic protein transport through the Golgi stack
    • "Purification of a novel class of coated vesicles mediating biosynthetic protein transport through the Golgi stack":, V. Malhotra, T. Serafini, L. Orci, J. Shepherd, J. Rothman, Cell 1989, 58, 329-336.
    • (1989) Cell , vol.58 , pp. 329-336
    • Malhotra, V.1    Serafini, T.2    Orci, L.3    Shepherd, J.4    Rothman, J.5
  • 16
    • 0025957468 scopus 로고
    • Coatomer': A cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles
    • "'Coatomer': A cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles":, M. Waters, T. Serafini, J. Rothman, Nature 1991, 349, 248-251.
    • (1991) Nature , vol.349 , pp. 248-251
    • Waters, M.1    Serafini, T.2    Rothman, J.3
  • 17
    • 0026001029 scopus 로고
    • ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: A novel role for a GTP-binding protein
    • "ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: A novel role for a GTP-binding protein":, T. Serafini, L. Orci, M. Amherdt, M. Brunner, R. Kahn, J. Rothman, Cell 1991, 67, 239-253.
    • (1991) Cell , vol.67 , pp. 239-253
    • Serafini, T.1    Orci, L.2    Amherdt, M.3    Brunner, M.4    Kahn, R.5    Rothman, J.6
  • 18
    • 0027724473 scopus 로고
    • Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles
    • "Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles":, G. Tanigawa, L. Orci, M. Amherdt, M. Ravazzola, J. Helms, J. Rothman, J. Cell Biol. 1993, 123, 1365-1371.
    • (1993) J. Cell Biol. , vol.123 , pp. 1365-1371
    • Tanigawa, G.1    Orci, L.2    Amherdt, M.3    Ravazzola, M.4    Helms, J.5    Rothman, J.6
  • 20
    • 0027291429 scopus 로고
    • Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol
    • "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol":, L. Orci, D. Palmer, M. Amherdt, J. Rothman, Nature 1993, 364, 732-734.
    • (1993) Nature , vol.364 , pp. 732-734
    • Orci, L.1    Palmer, D.2    Amherdt, M.3    Rothman, J.4
  • 21
    • 0027155088 scopus 로고
    • The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein
    • "The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein":, M. Stamnes, J. Rothman, Cell 1993, 73, 999-1005.
    • (1993) Cell , vol.73 , pp. 999-1005
    • Stamnes, M.1    Rothman, J.2
  • 22
    • 0023091173 scopus 로고
    • A possible role for acyl-coenzyme A in intracellular protein transport
    • "A possible role for acyl-coenzyme A in intracellular protein transport":, B. Glick, J. Rothman, Nature 1987, 326, 309-312.
    • (1987) Nature , vol.326 , pp. 309-312
    • Glick, B.1    Rothman, J.2
  • 23
    • 0000930533 scopus 로고
    • Purification of an N-ethylmaleimide-sensitive protein catalyzing vesicular transport
    • "Purification of an N-ethylmaleimide-sensitive protein catalyzing vesicular transport":, M. Block, B. Glick, C. Wilcox, F. Wieland, J. Rothman, Proc. Natl. Acad. Sci. USA 1988, 85, 7852-7856.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7852-7856
    • Block, M.1    Glick, B.2    Wilcox, C.3    Wieland, F.4    Rothman, J.5
  • 24
    • 0023707176 scopus 로고
    • Role of an N-ethylmaleimide-sensitive transport component in promoting fusion of transport vesicles with cisternae of the Golgi stack
    • "Role of an N-ethylmaleimide-sensitive transport component in promoting fusion of transport vesicles with cisternae of the Golgi stack":, V. Malhotra, L. Orci, B. Glick, M. Block, J. Rothman, Cell 1988, 54, 221-227.
    • (1988) Cell , vol.54 , pp. 221-227
    • Malhotra, V.1    Orci, L.2    Glick, B.3    Block, M.4    Rothman, J.5
  • 25
    • 0025359065 scopus 로고
    • SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast
    • "SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast":, D. Clary, I. Griff, J. Rothman, Cell 1990, 61, 709-721.
    • (1990) Cell , vol.61 , pp. 709-721
    • Clary, D.1    Griff, I.2    Rothman, J.3
  • 27
    • 0024514664 scopus 로고
    • Binding of an N-ethylmaleimide-sensitive fusion protein to Golgi membranes requires both a soluble protein(s) and an integral membrane receptor
    • "Binding of an N-ethylmaleimide-sensitive fusion protein to Golgi membranes requires both a soluble protein(s) and an integral membrane receptor":, P. Weidman, P. Melancon, M. Block, J. Rothman, J. Cell Biol. 1989, 108, 1589-1596.
    • (1989) J. Cell Biol. , vol.108 , pp. 1589-1596
    • Weidman, P.1    Melancon, P.2    Block, M.3    Rothman, J.4
  • 29
    • 0026778460 scopus 로고
    • Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones
    • "Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones":, M. Bennett, N. Calakos, R. Scheller, Science 1992, 257, 255-259.
    • (1992) Science , vol.257 , pp. 255-259
    • Bennett, M.1    Calakos, N.2    Scheller, R.3
  • 30
    • 0026660586 scopus 로고
    • Cloning and sequence analysis of cDNA for a neuronal cell membrane antigen, HPC-1
    • "Cloning and sequence analysis of cDNA for a neuronal cell membrane antigen, HPC-1":, A. Inoue, K. Obata, K. Akagawa, J. Biol. Chem. 1992, 267, 10613-10619.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10613-10619
    • Inoue, A.1    Obata, K.2    Akagawa, K.3
  • 31
    • 0024828306 scopus 로고
    • The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations
    • "The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations":, G. Oyler, G. Higgins, R. Hart, E. Battenberg, M. Billingsley, F. Bloom, M. Wilson, J. Cell Biol. 1989, 109, 3039-3052.
    • (1989) J. Cell Biol. , vol.109 , pp. 3039-3052
    • Oyler, G.1    Higgins, G.2    Hart, R.3    Battenberg, E.4    Billingsley, M.5    Bloom, F.6    Wilson, M.7
  • 32
    • 0024366008 scopus 로고
    • Synaptobrevin: an integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain
    • "Synaptobrevin: an integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain":, M. Baumert, P. R. Maycox, F. Navone, P. DeCamilli, R. Jahn, EMBO J. 1989, 8, 379-384.
    • (1989) EMBO J. , vol.8 , pp. 379-384
    • Baumert, M.1    Maycox, P.R.2    Navone, F.3    DeCamilli, P.4    Jahn, R.5
  • 33
    • 0024308501 scopus 로고
    • Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system
    • "Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system":, L. Elferink, W. Trimble, R. Scheller, J. Biol. Chem. 1989, 264, 11061-11064.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11061-11064
    • Elferink, L.1    Trimble, W.2    Scheller, R.3
  • 34
    • 0027404604 scopus 로고
    • The molecular machinery for secretion is conserved from yeast to neurons
    • "The molecular machinery for secretion is conserved from yeast to neurons":, M. Bennett, R. Scheller, Proc. Natl. Acad. Sci. USA 1993, 90, 2559-2563.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2559-2563
    • Bennett, M.1    Scheller, R.2
  • 35
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • "A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion":, T. Söllner, M. Bennett, S. Whiteheart, R. Scheller, J. Rothman, Cell 1993, 75, 409-418.
    • (1993) Cell , vol.75 , pp. 409-418
    • Söllner, T.1    Bennett, M.2    Whiteheart, S.3    Scheller, R.4    Rothman, J.5
  • 36
    • 0029980441 scopus 로고    scopus 로고
    • Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles
    • "Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles":, A. Mayer, W. Wickner, A. Haas, Cell 1996, 85, 83-94.
    • (1996) Cell , vol.85 , pp. 83-94
    • Mayer, A.1    Wickner, W.2    Haas, A.3
  • 38
    • 0028130728 scopus 로고
    • Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly
    • "Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly":, T. Hayashi, H. McMahon, S. Yamasaki, T. Binz, Y. Hata, T. C. Südhof, H. Niemann, EMBO J. 1994, 13, 5051-5061.
    • (1994) EMBO J. , vol.13 , pp. 5051-5061
    • Hayashi, T.1    McMahon, H.2    Yamasaki, S.3    Binz, T.4    Hata, Y.5    Südhof, T.C.6    Niemann, H.7
  • 39
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • "Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy":, P. Hanson, R. Roth, H. Morisaki, R. Jahn, J. Heuser, Cell 1997, 90, 523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.5
  • 46
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4Å resolution
    • "Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4Å resolution":, R. Sutton, D. Fasshauer, R. Jahn, A. Brunger, Nature 1998, 395, 347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.4
  • 47
    • 58849092285 scopus 로고    scopus 로고
    • Membrane Fusion: Grappling with SNARE and SM Proteins
    • "Membrane Fusion: Grappling with SNARE and SM Proteins":, T. Südhof, J. Rothman, Science 2009, 323, 474-477.
    • (2009) Science , vol.323 , pp. 474-477
    • Südhof, T.1    Rothman, J.2
  • 48
  • 49
    • 0028880456 scopus 로고
    • Complexins: cytosolic proteins that regulate SNAP receptor function
    • "Complexins: cytosolic proteins that regulate SNAP receptor function":, H. McMahon, M. Missler, C. Li, T. Südhof, Cell 1995, 83, 111-119.
    • (1995) Cell , vol.83 , pp. 111-119
    • McMahon, H.1    Missler, M.2    Li, C.3    Südhof, T.4
  • 53
    • 0014221586 scopus 로고
    • The Making of a Scientist
    • "The Making of a Scientist":, H. Krebs, Nature 1967, 215, 1441-1445.
    • (1967) Nature , vol.215 , pp. 1441-1445
    • Krebs, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.