메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages

The trans-SNARE-regulating function of Munc18-1 is essential to synaptic exocytosis

Author keywords

[No Author keywords available]

Indexed keywords

MUNC18 PROTEIN; SNARE PROTEIN; LIPOSOME; STXBP1 PROTEIN, MOUSE; SYNAPTOBREVIN 2; VESICLE-ASSOCIATED MEMBRANE PROTEIN 2, MOUSE;

EID: 84947225124     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms9852     Document Type: Article
Times cited : (49)

References (70)
  • 1
    • 58849092285 scopus 로고    scopus 로고
    • Membrane fusion: Grappling with SNARE and SM proteins
    • Sudhof, T. C. & Rothman, J. E. Membrane fusion: grappling with SNARE and SM proteins. Science (New York, NY) 323, 474-477 (2009).
    • (2009) Science (New York, NY) , vol.323 , pp. 474-477
    • Sudhof, T.C.1    Rothman, J.E.2
  • 2
    • 0027413655 scopus 로고
    • SNAP receptors implicated in vesicle targeting and fusion
    • Sollner, T. et al. SNAP receptors implicated in vesicle targeting and fusion. Nature 362, 318-324 (1993).
    • (1993) Nature , vol.362 , pp. 318-324
    • Sollner, T.1
  • 3
    • 0032549708 scopus 로고    scopus 로고
    • SNAREpins: Minimal machinery for membrane fusion
    • Weber, T. et al. SNAREpins: minimal machinery for membrane fusion. Cell 92, 759-772 (1998).
    • (1998) Cell , vol.92 , pp. 759-772
    • Weber, T.1
  • 6
    • 84866132236 scopus 로고    scopus 로고
    • Single reconstituted neuronal SNARE complexes zipper in three distinct stages
    • Gao, Y. et al. Single reconstituted neuronal SNARE complexes zipper in three distinct stages. Science 337, 1340-1343 (2012).
    • (2012) Science , vol.337 , pp. 1340-1343
    • Gao, Y.1
  • 7
    • 0037008962 scopus 로고    scopus 로고
    • Regulation of membrane fusion by the membrane-proximal coil of the t-SNARE during zippering of SNAREpins
    • Melia, T. J. et al. Regulation of membrane fusion by the membrane-proximal coil of the t-SNARE during zippering of SNAREpins. J. Cell Biol. 158, 929-940 (2002).
    • (2002) J. Cell Biol. , vol.158 , pp. 929-940
    • Melia, T.J.1
  • 8
    • 84885860678 scopus 로고    scopus 로고
    • Lipid-anchored SNAREs lacking transmembrane regions fully support membrane fusion during neurotransmitter release
    • Zhou, P., Bacaj, T., Yang, X., Pang, Z. P. & Sudhof, T. C. Lipid-anchored SNAREs lacking transmembrane regions fully support membrane fusion during neurotransmitter release. Neuron 80, 470-483 (2013).
    • (2013) Neuron , vol.80 , pp. 470-483
    • Zhou, P.1    Bacaj, T.2    Yang, X.3    Pang, Z.P.4    Sudhof, T.C.5
  • 9
    • 80054811004 scopus 로고    scopus 로고
    • A lipid-anchored SNARE supports membrane fusion
    • Xu, H., Zick, M., Wickner, W. T. & Jun, Y. A lipid-anchored SNARE supports membrane fusion. Proc. Natl Acad. Sci. USA 108, 17325-17330 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 17325-17330
    • Xu, H.1    Zick, M.2    Wickner, W.T.3    Jun, Y.4
  • 10
    • 0026778460 scopus 로고
    • Syntaxin: A synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones
    • Bennett, M. K., Calakos, N. & Scheller, R. H. Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Science 257, 255-259 (1992).
    • (1992) Science , vol.257 , pp. 255-259
    • Bennett, M.K.1    Calakos, N.2    Scheller, R.H.3
  • 11
    • 0024308501 scopus 로고
    • Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system
    • Elferink, L. A., Trimble, W. S. & Scheller, R. H. Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system. J. Biol. Chem. 264, 11061-11064 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 11061-11064
    • Elferink, L.A.1    Trimble, W.S.2    Scheller, R.H.3
  • 12
    • 0024828306 scopus 로고
    • The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations
    • Oyler, G. A. et al. The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations. J. Cell Biol. 109, 3039-3052 (1989).
    • (1989) J. Cell Biol. , vol.109 , pp. 3039-3052
    • Oyler, G.A.1
  • 13
    • 0024659539 scopus 로고
    • A synaptic vesicle membrane protein is conserved from mammals to Drosophila
    • Sudhof, T. C., Baumert, M., Perin, M. S. & Jahn, R. A synaptic vesicle membrane protein is conserved from mammals to Drosophila. Neuron 2, 1475-1481 (1989).
    • (1989) Neuron , vol.2 , pp. 1475-1481
    • Sudhof, T.C.1    Baumert, M.2    Perin, M.S.3    Jahn, R.4
  • 14
    • 0027364502 scopus 로고
    • Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin
    • Hata, Y., Slaughter, C. A. & Sudhof, T. C. Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin. Nature 366, 347-351 (1993).
    • (1993) Nature , vol.366 , pp. 347-351
    • Hata, Y.1    Slaughter, C.A.2    Sudhof, T.C.3
  • 15
    • 0000756130 scopus 로고
    • Secretion and cell-surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae
    • Novick, P. & Schekman, R. Secretion and cell-surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA 76, 1858-1862 (1979).
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 1858-1862
    • Novick, P.1    Schekman, R.2
  • 16
  • 18
    • 78049408948 scopus 로고    scopus 로고
    • At the junction of SNARE and SM protein function
    • Carr, C. M. & Rizo, J. At the junction of SNARE and SM protein function. Curr. Opin. Cell Biol. 22, 488-495 (2010).
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 488-495
    • Carr, C.M.1    Rizo, J.2
  • 19
    • 58549112408 scopus 로고    scopus 로고
    • The functions of Munc18-1 in regulated exocytosis
    • Burgoyne, R. D. et al. The functions of Munc18-1 in regulated exocytosis. Ann. N. Y. Acad. Sci. 1152, 76-86 (2009).
    • (2009) Ann. N. Y. Acad. Sci. , vol.1152 , pp. 76-86
    • Burgoyne, R.D.1
  • 20
    • 35748984692 scopus 로고    scopus 로고
    • Munc18-1 in secretion: Lonely Munc joins SNARE team and takes control
    • Toonen, R. F. & Verhage, M. Munc18-1 in secretion: lonely Munc joins SNARE team and takes control. Trends Neurosci. 30, 564-572 (2007).
    • (2007) Trends Neurosci. , vol.30 , pp. 564-572
    • Toonen, R.F.1    Verhage, M.2
  • 21
    • 0034603030 scopus 로고    scopus 로고
    • Synaptic assembly of the brain in the absence of neurotransmitter secretion
    • Verhage, M. et al. Synaptic assembly of the brain in the absence of neurotransmitter secretion. Science 287, 864-869 (2000).
    • (2000) Science , vol.287 , pp. 864-869
    • Verhage, M.1
  • 22
    • 0141542671 scopus 로고    scopus 로고
    • Defects in synaptic vesicle docking in unc-18 mutants
    • Weimer, R. M. et al. Defects in synaptic vesicle docking in unc-18 mutants. Nat. Neurosci. 6, 1023-1030 (2003).
    • (2003) Nat. Neurosci. , vol.6 , pp. 1023-1030
    • Weimer, R.M.1
  • 23
    • 0035974886 scopus 로고    scopus 로고
    • Munc18-1 promotes large dense-core vesicle docking
    • Voets, T. et al. Munc18-1 promotes large dense-core vesicle docking. Neuron 31, 581-591 (2001).
    • (2001) Neuron , vol.31 , pp. 581-591
    • Voets, T.1
  • 24
    • 0032472409 scopus 로고    scopus 로고
    • ROP, the Drosophila Sec1 homolog, interacts with syntaxin and regulates neurotransmitter release in a dosage-dependent manner
    • Wu, M. N., Littleton, J. T., Bhat, M. A., Prokop, A. & Bellen, H. J. ROP, the Drosophila Sec1 homolog, interacts with syntaxin and regulates neurotransmitter release in a dosage-dependent manner. EMBO J. 17, 127-139 (1998).
    • (1998) EMBO J. , vol.17 , pp. 127-139
    • Wu, M.N.1    Littleton, J.T.2    Bhat, M.A.3    Prokop, A.4    Bellen, H.J.5
  • 25
    • 0034704771 scopus 로고    scopus 로고
    • Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex
    • Misura, K. M., Scheller, R. H. & Weis, W. I. Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex. Nature 404, 355-362 (2000).
    • (2000) Nature , vol.404 , pp. 355-362
    • Misura, K.M.1    Scheller, R.H.2    Weis, W.I.3
  • 26
    • 84862561705 scopus 로고    scopus 로고
    • Low-resolution solution structures of Munc18:Syntaxin protein complexes indicate an open binding mode driven by the Syntaxin N-peptide
    • Christie, M. P. et al. Low-resolution solution structures of Munc18:Syntaxin protein complexes indicate an open binding mode driven by the Syntaxin N-peptide. Proc. Natl Acad. Sci. USA 109, 9816-9821 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 9816-9821
    • Christie, M.P.1
  • 27
    • 12844274908 scopus 로고    scopus 로고
    • Munc18-1 regulates early and late stages of exocytosis via syntaxin-independent protein interactions
    • Ciufo, L. F., Barclay, J. W., Burgoyne, R. D. & Morgan, A. Munc18-1 regulates early and late stages of exocytosis via syntaxin-independent protein interactions. Mol. Biol. Cell 16, 470-482 (2005).
    • (2005) Mol. Biol. Cell , vol.16 , pp. 470-482
    • Ciufo, L.F.1    Barclay, J.W.2    Burgoyne, R.D.3    Morgan, A.4
  • 28
    • 55549102680 scopus 로고    scopus 로고
    • UNC-18 promotes both the anterograde trafficking and synaptic function of syntaxin
    • McEwen, J. M. & Kaplan, J. M. UNC-18 promotes both the anterograde trafficking and synaptic function of syntaxin. Mol. Biol. Cell 19, 3836-3846 (2008).
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3836-3846
    • McEwen, J.M.1    Kaplan, J.M.2
  • 29
    • 84872802734 scopus 로고    scopus 로고
    • Reconstitution of the vital functions of Munc18 and Munc13 in neurotransmitter release
    • Ma, C., Su, L., Seven, A. B., Xu, Y. & Rizo, J. Reconstitution of the vital functions of Munc18 and Munc13 in neurotransmitter release. Science 339, 421-425 (2013).
    • (2013) Science , vol.339 , pp. 421-425
    • Ma, C.1    Su, L.2    Seven, A.B.3    Xu, Y.4    Rizo, J.5
  • 30
    • 85027945821 scopus 로고    scopus 로고
    • Munc13 mediates the transition from the closed syntaxin-Munc18 complex to the SNARE complex
    • Ma, C., Li, W., Xu, Y. & Rizo, J. Munc13 mediates the transition from the closed syntaxin-Munc18 complex to the SNARE complex. Nature Struct. Mol. Biol. 18, 542-549 (2011).
    • (2011) Nature Struct. Mol. Biol. , vol.18 , pp. 542-549
    • Ma, C.1    Li, W.2    Xu, Y.3    Rizo, J.4
  • 31
    • 84886998869 scopus 로고    scopus 로고
    • Neurotransmitter release: The last millisecond in the life of a synaptic vesicle
    • Sudhof, T. C. Neurotransmitter release: the last millisecond in the life of a synaptic vesicle. Neuron 80, 675-690 (2013).
    • (2013) Neuron , vol.80 , pp. 675-690
    • Sudhof, T.C.1
  • 32
    • 33845987734 scopus 로고    scopus 로고
    • Selective activation of cognate SNAREpins by Sec1/Munc18 proteins
    • Shen, J., Tareste, D. C., Paumet, F., Rothman, J. E. & Melia, T. J. Selective activation of cognate SNAREpins by Sec1/Munc18 proteins. Cell 128, 183-195 (2007).
    • (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
  • 33
    • 33847326814 scopus 로고    scopus 로고
    • Munc18-1 binds directly to the neuronal SNARE complex
    • Dulubova, I. et al. Munc18-1 binds directly to the neuronal SNARE complex. Proc. Natl Acad. Sci. USA 104, 2697-2702 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 2697-2702
    • Dulubova, I.1
  • 34
    • 77954715092 scopus 로고    scopus 로고
    • SNARE bundle and syntaxin N-peptide constitute a minimal complement for Munc18-1 activation of membrane fusion
    • Shen, J., Rathore, S., Khandan, L. & Rothman, J. E. SNARE bundle and syntaxin N-peptide constitute a minimal complement for Munc18-1 activation of membrane fusion. J. Cell Biol. 190, 55-63 (2010).
    • (2010) J. Cell Biol. , vol.190 , pp. 55-63
    • Shen, J.1    Rathore, S.2    Khandan, L.3    Rothman, J.E.4
  • 35
    • 78651078463 scopus 로고    scopus 로고
    • Syntaxin N-terminal peptide motif is an initiation factor for the assembly of the SNARE-Sec1/Munc18 membrane fusion complex
    • Rathore, S. S. et al. Syntaxin N-terminal peptide motif is an initiation factor for the assembly of the SNARE-Sec1/Munc18 membrane fusion complex. Proc. Natl Acad. Sci. USA 107, 22399-22406 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 22399-22406
    • Rathore, S.S.1
  • 36
    • 0037112932 scopus 로고    scopus 로고
    • Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p
    • Bracher, A. & Weissenhorn, W. Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p. EMBO J. 21, 6114-6124 (2002).
    • (2002) EMBO J , vol.21 , pp. 6114-6124
    • Bracher, A.1    Weissenhorn, W.2
  • 37
    • 34547483062 scopus 로고    scopus 로고
    • Structure of the Munc18c/Syntaxin4 N-peptide complex defines universal features of the N-peptide binding mode of Sec1/Munc18 proteins
    • Hu, S. H., Latham, C. F., Gee, C. L., James, D. E. & Martin, J. L. Structure of the Munc18c/Syntaxin4 N-peptide complex defines universal features of the N-peptide binding mode of Sec1/Munc18 proteins. Proc. Natl Acad. Sci. USA 104, 8773-8778 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 8773-8778
    • Hu, S.H.1    Latham, C.F.2    Gee, C.L.3    James, D.E.4    Martin, J.L.5
  • 38
    • 45849152550 scopus 로고    scopus 로고
    • Mechanisms of membrane fusion: Disparate players and common principles
    • Martens, S. & McMahon, H. T. Mechanisms of membrane fusion: disparate players and common principles. Nat. Rev. Mol. Cell Biol. 9, 543-556 (2008).
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 543-556
    • Martens, S.1    McMahon, H.T.2
  • 39
    • 49149131497 scopus 로고    scopus 로고
    • Reconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperones
    • Mima, J., Hickey, C. M., Xu, H., Jun, Y. & Wickner, W. Reconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperones. EMBO J. 27, 2031-2042 (2008).
    • (2008) EMBO J. , vol.27 , pp. 2031-2042
    • Mima, J.1    Hickey, C.M.2    Xu, H.3    Jun, Y.4    Wickner, W.5
  • 40
    • 22944485726 scopus 로고    scopus 로고
    • Trans-SNARE pairing can precede a hemifusion intermediate in intracellular membrane fusion
    • Reese, C., Heise, F. & Mayer, A. Trans-SNARE pairing can precede a hemifusion intermediate in intracellular membrane fusion. Nature 436, 410-414 (2005).
    • (2005) Nature , vol.436 , pp. 410-414
    • Reese, C.1    Heise, F.2    Mayer, A.3
  • 41
    • 77749298991 scopus 로고    scopus 로고
    • Binding of Munc18-1 to synaptobrevin and to the SNARE four-helix bundle
    • Xu, Y., Su, L. & Rizo, J. Binding of Munc18-1 to synaptobrevin and to the SNARE four-helix bundle. Biochemistry 49, 1568-1576 (2010).
    • (2010) Biochemistry , vol.49 , pp. 1568-1576
    • Xu, Y.1    Su, L.2    Rizo, J.3
  • 42
    • 84883339791 scopus 로고    scopus 로고
    • Comparative studies of Munc18c and Munc18-1 reveal conserved and divergent mechanisms of Sec1/Munc18 proteins
    • Yu, H. et al. Comparative studies of Munc18c and Munc18-1 reveal conserved and divergent mechanisms of Sec1/Munc18 proteins. Proc. Natl Acad. Sci. USA 110, E3271-E3280 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. E3271-E3280
    • Yu, H.1
  • 43
    • 79960014755 scopus 로고    scopus 로고
    • Membrane bridging and hemifusion by denaturated Munc18
    • Xu, Y., Seven, A. B., Su, L., Jiang, Q. X. & Rizo, J. Membrane bridging and hemifusion by denaturated Munc18. PLoS ONE 6, e22012 (2011).
    • (2011) PLoS ONE , vol.6
    • Xu, Y.1    Seven, A.B.2    Su, L.3    Jiang, Q.X.4    Rizo, J.5
  • 44
    • 41949130893 scopus 로고    scopus 로고
    • Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide
    • Burkhardt, P., Hattendorf, D. A., Weis, W. I. & Fasshauer, D. Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide. EMBO J. 27, 923-933 (2008).
    • (2008) EMBO J. , vol.27 , pp. 923-933
    • Burkhardt, P.1    Hattendorf, D.A.2    Weis, W.I.3    Fasshauer, D.4
  • 45
    • 12144288006 scopus 로고    scopus 로고
    • A resource for large-scale RNA-interference-based screens in mammals
    • Paddison, P. J. et al. A resource for large-scale RNA-interference-based screens in mammals. Nature 428, 427-431 (2004).
    • (2004) Nature , vol.428 , pp. 427-431
    • Paddison, P.J.1
  • 46
    • 0035798088 scopus 로고    scopus 로고
    • SNARE function analyzed in synaptobrevin/VAMP knockout mice
    • Schoch, S. et al. SNARE function analyzed in synaptobrevin/VAMP knockout mice. Science 294, 1117-1122 (2001).
    • (2001) Science , vol.294 , pp. 1117-1122
    • Schoch, S.1
  • 47
    • 33745800098 scopus 로고    scopus 로고
    • Structural determinants of synaptobrevin 2 function in synaptic vesicle fusion
    • Deak, F., Shin, O. H., Kavalali, E. T. & Sudhof, T. C. Structural determinants of synaptobrevin 2 function in synaptic vesicle fusion. J. Neurosci. 26, 6668-6676 (2006).
    • (2006) J. Neurosci. , vol.26 , pp. 6668-6676
    • Deak, F.1    Shin, O.H.2    Kavalali, E.T.3    Sudhof, T.C.4
  • 49
    • 44349096827 scopus 로고    scopus 로고
    • De novo mutations in the gene encoding STXBP1 (MUNC18-1) cause early infantile epileptic encephalopathy
    • Saitsu, H. et al. De novo mutations in the gene encoding STXBP1 (MUNC18-1) cause early infantile epileptic encephalopathy. Nat. Genet. 40, 782-788 (2008).
    • (2008) Nat. Genet. , vol.40 , pp. 782-788
    • Saitsu, H.1
  • 50
    • 80053529047 scopus 로고    scopus 로고
    • Paternal mosaicism of an STXBP1 mutation in OS
    • Saitsu, H. et al. Paternal mosaicism of an STXBP1 mutation in OS. Clin. Genet. 80, 484-488 (2010).
    • (2010) Clin. Genet. , vol.80 , pp. 484-488
    • Saitsu, H.1
  • 51
    • 67650090920 scopus 로고    scopus 로고
    • De novo STXBP1 mutations in mental retardation and nonsyndromic epilepsy
    • Hamdan, F. F. et al. De novo STXBP1 mutations in mental retardation and nonsyndromic epilepsy. Ann. Neurol. 65, 748-753 (2009).
    • (2009) Ann. Neurol. , vol.65 , pp. 748-753
    • Hamdan, F.F.1
  • 52
    • 80053564430 scopus 로고    scopus 로고
    • STXBP1-related encephalopathy presenting as infantile spasms and generalized tremor in three patients
    • Mignot, C. et al. STXBP1-related encephalopathy presenting as infantile spasms and generalized tremor in three patients. Epilepsia 52, 1820-1827 (2011).
    • (2011) Epilepsia , vol.52 , pp. 1820-1827
    • Mignot, C.1
  • 53
    • 78650017215 scopus 로고    scopus 로고
    • STXBP1 mutations cause not only Ohtahara syndrome but also West syndrome - Result of Japanese cohort study
    • Otsuka, M. et al. STXBP1 mutations cause not only Ohtahara syndrome but also West syndrome - result of Japanese cohort study. Epilepsia 51, 2449-2452 (2010).
    • (2010) Epilepsia , vol.51 , pp. 2449-2452
    • Otsuka, M.1
  • 54
    • 0035830493 scopus 로고    scopus 로고
    • Crystal structures of neuronal squid Sec1 implicate inter-domain hinge movement in the release of t-SNAREs
    • Bracher, A. & Weissenhorn, W. Crystal structures of neuronal squid Sec1 implicate inter-domain hinge movement in the release of t-SNAREs. J. Mol. Biol. 306, 7-13 (2001).
    • (2001) J. Mol. Biol. , vol.306 , pp. 7-13
    • Bracher, A.1    Weissenhorn, W.2
  • 55
    • 79960301464 scopus 로고    scopus 로고
    • Topological arrangement of the intracellular membrane fusion machinery
    • Rathore, S. S., Ghosh, N., Ouyang, Y. & Shen, J. Topological arrangement of the intracellular membrane fusion machinery. Mol. Biol. Cell 22, 2612-2619 (2011).
    • (2011) Mol. Biol. Cell , vol.22 , pp. 2612-2619
    • Rathore, S.S.1    Ghosh, N.2    Ouyang, Y.3    Shen, J.4
  • 56
    • 80052247975 scopus 로고    scopus 로고
    • Resolving the function of distinct Munc18-1/SNARE protein interaction modes in a reconstituted membrane fusion assay
    • Schollmeier, Y., Krause, J. M., Kreye, S., Malsam, J. & Sollner, T. H. Resolving the function of distinct Munc18-1/SNARE protein interaction modes in a reconstituted membrane fusion assay. J. Biol. Chem. 286, 30582-30590 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 30582-30590
    • Schollmeier, Y.1    Krause, J.M.2    Kreye, S.3    Malsam, J.4    Sollner, T.H.5
  • 57
    • 58149361168 scopus 로고    scopus 로고
    • Munc18a scaffolds SNARE assembly to promote membrane fusion
    • Rodkey, T. L., Liu, S., Barry, M. & McNew, J. A. Munc18a scaffolds SNARE assembly to promote membrane fusion. Mol. Biol. Cell 19, 5422-5434 (2008).
    • (2008) Mol. Biol. Cell , vol.19 , pp. 5422-5434
    • Rodkey, T.L.1    Liu, S.2    Barry, M.3    McNew, J.A.4
  • 58
    • 80655128120 scopus 로고    scopus 로고
    • Dual roles of Munc18-1 rely on distinct binding modes of the central cavity with Stx1A and SNARE complex
    • Shi, L., Kummel, D., Coleman, J., Melia, T. J. & Giraudo, C. G. Dual roles of Munc18-1 rely on distinct binding modes of the central cavity with Stx1A and SNARE complex. Mol. Biol. Cell 22, 4150-4160 (2011).
    • (2011) Mol. Biol. Cell , vol.22 , pp. 4150-4160
    • Shi, L.1    Kummel, D.2    Coleman, J.3    Melia, T.J.4    Giraudo, C.G.5
  • 59
    • 40649084835 scopus 로고    scopus 로고
    • SNAREpin/Munc18 promotes adhesion and fusion of large vesicles to giant membranes
    • Tareste, D., Shen, J., Melia, T. J. & Rothman, J. E. SNAREpin/Munc18 promotes adhesion and fusion of large vesicles to giant membranes. Proc. Natl Acad. Sci. USA 105, 2380-2385 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 2380-2385
    • Tareste, D.1    Shen, J.2    Melia, T.J.3    Rothman, J.E.4
  • 60
    • 77951729758 scopus 로고    scopus 로고
    • Single-vesicle fusion assay reveals Munc18-1 binding to the SNARE core is sufficient for stimulating membrane fusion
    • Diao, J. et al. Single-vesicle fusion assay reveals Munc18-1 binding to the SNARE core is sufficient for stimulating membrane fusion. ACS Chem. Neurosci. 1, 168-174 (2010).
    • (2010) ACS Chem. Neurosci. , vol.1 , pp. 168-174
    • Diao, J.1
  • 61
    • 84901659418 scopus 로고    scopus 로고
    • In vitro assay using engineered yeast vacuoles for neuronal SNARE-mediated membrane fusion
    • Ko, Y. J., Lee, M., Kang, K., Song, W. K. & Jun, Y. In vitro assay using engineered yeast vacuoles for neuronal SNARE-mediated membrane fusion. Proc. Natl Acad. Sci. USA 111, 7677-7682 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 7677-7682
    • Ko, Y.J.1    Lee, M.2    Kang, K.3    Song, W.K.4    Jun, Y.5
  • 62
    • 5444219613 scopus 로고    scopus 로고
    • Sec1p directly stimulates SNARE-mediated membrane fusion in vitro
    • Scott, B. L. et al. Sec1p directly stimulates SNARE-mediated membrane fusion in vitro. J. Cell Biol. 167, 75-85 (2004).
    • (2004) J. Cell Biol. , vol.167 , pp. 75-85
    • Scott, B.L.1
  • 63
    • 33746319639 scopus 로고    scopus 로고
    • A clamping mechanism involved in SNARE-dependent exocytosis
    • Giraudo, C. G., Eng, W. S., Melia, T. J. & Rothman, J. E. A clamping mechanism involved in SNARE-dependent exocytosis. Science 313, 676-680 (2006).
    • (2006) Science , vol.313 , pp. 676-680
    • Giraudo, C.G.1    Eng, W.S.2    Melia, T.J.3    Rothman, J.E.4
  • 64
    • 46449093538 scopus 로고    scopus 로고
    • How does synaptotagmin trigger neurotransmitter release?
    • Chapman, E. R. How does synaptotagmin trigger neurotransmitter release? Annu. Rev. Biochem. 77, 615-641 (2008).
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 615-641
    • Chapman, E.R.1
  • 65
    • 70350436474 scopus 로고    scopus 로고
    • CAPS drives trans-SNARE complex formation and membrane fusion through syntaxin interactions
    • James, D. J., Kowalchyk, J., Daily, N., Petrie, M. & Martin, T. F. CAPS drives trans-SNARE complex formation and membrane fusion through syntaxin interactions. Proc. Natl Acad. Sci. USA 106, 17308-17313 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 17308-17313
    • James, D.J.1    Kowalchyk, J.2    Daily, N.3    Petrie, M.4    Martin, T.F.5
  • 66
    • 36148956730 scopus 로고    scopus 로고
    • PKA activation bypasses the requirement for UNC-31 in the docking of dense core vesicles from C. elegans neurons
    • Zhou, K. M. et al. PKA activation bypasses the requirement for UNC-31 in the docking of dense core vesicles from C. elegans neurons. Neuron 56, 657-669 (2007).
    • (2007) Neuron , vol.56 , pp. 657-669
    • Zhou, K.M.1
  • 67
    • 79961024212 scopus 로고    scopus 로고
    • Complexin cross-links prefusion SNAREs into a zigzag array
    • Kummel, D. et al. Complexin cross-links prefusion SNAREs into a zigzag array. Nature Struct. Mol. Biol. 18, 927-933 (2011).
    • (2011) Nature Struct. Mol. Biol. , vol.18 , pp. 927-933
    • Kummel, D.1
  • 68
    • 84881514823 scopus 로고    scopus 로고
    • Synaptic proteins promote calcium-triggered fast transition from point contact to full fusion
    • Diao, J. et al. Synaptic proteins promote calcium-triggered fast transition from point contact to full fusion. Elife 1, e00109 (2012).
    • (2012) Elife , vol.1
    • Diao, J.1
  • 69
    • 84879586340 scopus 로고    scopus 로고
    • Synip arrests SNARE-dependent membrane fusion as a selective t-SNARE-binding inhibitor
    • Yu, H., Rathore, S. S. & Shen, J. Synip arrests SNARE-dependent membrane fusion as a selective t-SNARE-binding inhibitor. J Biol Chem 288, 18885-18893 (2013).
    • (2013) J Biol Chem , vol.288 , pp. 18885-18893
    • Yu, H.1    Rathore, S.S.2    Shen, J.3
  • 70
    • 84876565914 scopus 로고    scopus 로고
    • Doc2b promotes GLUT4 exocytosis by activating the SNARE-mediated fusion reaction in a calcium- and membrane bending-dependent manner
    • Yu, H., Rathore, S. S., Davis, E. M., Ouyang, Y. & Shen, J. Doc2b promotes GLUT4 exocytosis by activating the SNARE-mediated fusion reaction in a calcium- and membrane bending-dependent manner. Mol. Biol. Cell 24, 1176-1184 (2013).
    • (2013) Mol. Biol. Cell , vol.24 , pp. 1176-1184
    • Yu, H.1    Rathore, S.S.2    Davis, E.M.3    Ouyang, Y.4    Shen, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.