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Volumn 112, Issue 18, 2015, Pages E2290-E2297

Sec17 can trigger fusion of trans-SNARE paired membranes without Sec18

Author keywords

Membrane fusion; NSF; SNAREs; SNAP

Indexed keywords

ADENOSINE DIPHOSPHATE; HYBRID PROTEIN; PROTEIN; PROTEOLIPOSOME; SEC17 PROTEIN; SEC18 PROTEIN; SNARE PROTEIN; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATASE; LIPID; LIPID BILAYER; LIPOSOME; PROTEIN BINDING; PROTEOLIPID; PROTEOLIPOSOMES; SACCHAROMYCES CEREVISIAE PROTEIN; SEC17 PROTEIN, S CEREVISIAE; SEC18 PROTEIN, S CEREVISIAE; SOLUBLE N ETHYLMALEIMIDE SENSITIVE FACTOR ATTACHMENT PROTEIN; VESICULAR TRANSPORT PROTEIN;

EID: 84928905805     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1506409112     Document Type: Article
Times cited : (47)

References (53)
  • 1
    • 33747066132 scopus 로고    scopus 로고
    • Rabs and their effectors: Achieving specificity in membrane traffic
    • Grosshans BL, Ortiz D, Novick P (2006) Rabs and their effectors: Achieving specificity in membrane traffic. Proc Natl Acad Sci USA 103(32):11821-11827.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.32 , pp. 11821-11827
    • Grosshans, B.L.1    Ortiz, D.2    Novick, P.3
  • 2
    • 84870232182 scopus 로고    scopus 로고
    • The membrane fusion enigma: SNAREs, Sec1/Munc18 proteins, and their accomplices - Guilty as charged?
    • Rizo J, Südhof TC (2012) The membrane fusion enigma: SNAREs, Sec1/Munc18 proteins, and their accomplices - Guilty as charged? Annu Rev Cell Dev Biol 28:279-308.
    • (2012) Annu Rev Cell Dev Biol , vol.28 , pp. 279-308
    • Rizo, J.1    Südhof, T.C.2
  • 3
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
    • Fasshauer D, Sutton RB, Brunger AT, Jahn R (1998) Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc Natl Acad Sci USA 95(26):15781-15786.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.26 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brunger, A.T.3    Jahn, R.4
  • 4
    • 84881449435 scopus 로고    scopus 로고
    • Processive ATP-driven substrate disassembly by the N-ethylmaleimide-sensitive factor (NSF) molecular machine
    • Cipriano DJ, et al. (2013) Processive ATP-driven substrate disassembly by the N-ethylmaleimide-sensitive factor (NSF) molecular machine. J Biol Chem 288(32):23436-23445.
    • (2013) J Biol Chem , vol.288 , Issue.32 , pp. 23436-23445
    • Cipriano, D.J.1
  • 5
    • 0030682481 scopus 로고    scopus 로고
    • Stimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosis
    • Barnard RJ, Morgan A, Burgoyne RD (1997) Stimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosis. J Cell Biol 139(4):875-883.
    • (1997) J Cell Biol , vol.139 , Issue.4 , pp. 875-883
    • Barnard, R.J.1    Morgan, A.2    Burgoyne, R.D.3
  • 6
    • 0026629819 scopus 로고
    • Genes for directing vacuolar morphogenesis in Saccharomyces cerevisiae. I. Isolation and characterization of two classes of vam mutants
    • Wada Y, Ohsumi Y, Anraku Y (1992) Genes for directing vacuolar morphogenesis in Saccharomyces cerevisiae. I. Isolation and characterization of two classes of vam mutants. J Biol Chem 267(26):18665-18670.
    • (1992) J Biol Chem , vol.267 , Issue.26 , pp. 18665-18670
    • Wada, Y.1    Ohsumi, Y.2    Anraku, Y.3
  • 7
    • 0027083496 scopus 로고
    • Morphological classification of the yeast vacuolar protein sorting mutants: Evidence for a prevacuolar compartment in class E vps mutants
    • Raymond CK, Howald-Stevenson I, Vater CA, Stevens TH (1992) Morphological classification of the yeast vacuolar protein sorting mutants: Evidence for a prevacuolar compartment in class E vps mutants. Mol Biol Cell 3(12):1389-1402.
    • (1992) Mol Biol Cell , vol.3 , Issue.12 , pp. 1389-1402
    • Raymond, C.K.1    Howald-Stevenson, I.2    Vater, C.A.3    Stevens, T.H.4
  • 8
    • 0028333056 scopus 로고
    • G-protein ligands inhibit in vitro reactions of vacuole inheritance
    • Haas A, Conradt B, Wickner W (1994) G-protein ligands inhibit in vitro reactions of vacuole inheritance. J Cell Biol 126(1):87-97.
    • (1994) J Cell Biol , vol.126 , Issue.1 , pp. 87-97
    • Haas, A.1    Conradt, B.2    Wickner, W.3
  • 9
    • 49149131497 scopus 로고    scopus 로고
    • Reconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperones
    • Mima J, Hickey CM, Xu H, Jun Y, Wickner W (2008) Reconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperones. EMBO J 27(15):2031-2042.
    • (2008) EMBO J , vol.27 , Issue.15 , pp. 2031-2042
    • Mima, J.1    Hickey, C.M.2    Xu, H.3    Jun, Y.4    Wickner, W.5
  • 10
    • 70449560470 scopus 로고    scopus 로고
    • Minimal membrane docking requirements revealed by reconstitution of Rab GTPase-dependent membrane fusion from purified components
    • Stroupe C, Hickey CM, Mima J, Burfeind AS, Wickner W (2009) Minimal membrane docking requirements revealed by reconstitution of Rab GTPase-dependent membrane fusion from purified components. Proc Natl Acad Sci USA 106(42):17626-17633.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.42 , pp. 17626-17633
    • Stroupe, C.1    Hickey, C.M.2    Mima, J.3    Burfeind, A.S.4    Wickner, W.5
  • 11
    • 80054793989 scopus 로고    scopus 로고
    • Membrane fusion catalyzed by a Rab, SNAREs, and SNARE chaperones is accompanied by enhanced permeability to small molecules and by lysis
    • Zucchi PC, Zick M (2011) Membrane fusion catalyzed by a Rab, SNAREs, and SNARE chaperones is accompanied by enhanced permeability to small molecules and by lysis. Mol Biol Cell 22(23):4635-4646.
    • (2011) Mol Biol Cell , vol.22 , Issue.23 , pp. 4635-4646
    • Zucchi, P.C.1    Zick, M.2
  • 12
    • 0029980441 scopus 로고    scopus 로고
    • Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles
    • Mayer A, Wickner W, Haas A (1996) Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles. Cell 85(1):83-94.
    • (1996) Cell , vol.85 , Issue.1 , pp. 83-94
    • Mayer, A.1    Wickner, W.2    Haas, A.3
  • 13
    • 77954194779 scopus 로고    scopus 로고
    • HOPS initiates vacuole docking by tethering membranes before trans-SNARE complex assembly
    • Hickey CM, Wickner W (2010) HOPS initiates vacuole docking by tethering membranes before trans-SNARE complex assembly. Mol Biol Cell 21(13):2297-2305.
    • (2010) Mol Biol Cell , vol.21 , Issue.13 , pp. 2297-2305
    • Hickey, C.M.1    Wickner, W.2
  • 14
    • 33646128965 scopus 로고    scopus 로고
    • Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p
    • Stroupe C, Collins KM, Fratti RA, Wickner W (2006) Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p. EMBO J 25(8):1579-1589.
    • (2006) EMBO J , vol.25 , Issue.8 , pp. 1579-1589
    • Stroupe, C.1    Collins, K.M.2    Fratti, R.A.3    Wickner, W.4
  • 15
    • 79960303122 scopus 로고    scopus 로고
    • HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites
    • Krämer L, Ungermann C (2011) HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites. Mol Biol Cell 22(14):2601-2611.
    • (2011) Mol Biol Cell , vol.22 , Issue.14 , pp. 2601-2611
    • Krämer, L.1    Ungermann, C.2
  • 16
    • 84870502774 scopus 로고    scopus 로고
    • Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex
    • Lobingier BT, Merz AJ (2012) Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex. Mol Biol Cell 23(23):4611-4622.
    • (2012) Mol Biol Cell , vol.23 , Issue.23 , pp. 4611-4622
    • Lobingier, B.T.1    Merz, A.J.2
  • 17
    • 84888997394 scopus 로고    scopus 로고
    • The tethering complex HOPS catalyzes assembly of the soluble SNARE Vam7 into fusogenic trans-SNARE complexes
    • Zick M, Wickner W (2013) The tethering complex HOPS catalyzes assembly of the soluble SNARE Vam7 into fusogenic trans-SNARE complexes. Mol Biol Cell 24(23):3746-3753.
    • (2013) Mol Biol Cell , vol.24 , Issue.23 , pp. 3746-3753
    • Zick, M.1    Wickner, W.2
  • 18
    • 34547464792 scopus 로고    scopus 로고
    • trans-SNARE complex assembly and yeast vacuole membrane fusion
    • Collins KM, Wickner WT (2007) trans-SNARE complex assembly and yeast vacuole membrane fusion. Proc Natl Acad Sci USA 104(21):8755-8760.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.21 , pp. 8755-8760
    • Collins, K.M.1    Wickner, W.T.2
  • 19
    • 77953608974 scopus 로고    scopus 로고
    • HOPS prevents the disassembly of trans-SNARE complexes by Sec17p/Sec18p during membrane fusion
    • Xu H, Jun Y, Thompson J, Yates J, Wickner W (2010) HOPS prevents the disassembly of trans-SNARE complexes by Sec17p/Sec18p during membrane fusion. EMBO J 29(12):1948-1960.
    • (2010) EMBO J , vol.29 , Issue.12 , pp. 1948-1960
    • Xu, H.1    Jun, Y.2    Thompson, J.3    Yates, J.4    Wickner, W.5
  • 20
    • 84920986272 scopus 로고    scopus 로고
    • A distinct tethering step is vital for vacuole membrane fusion
    • Zick M, Wickner WT (2014) A distinct tethering step is vital for vacuole membrane fusion. eLife 3:e03251.
    • (2014) eLife , vol.3 , pp. e03251
    • Zick, M.1    Wickner, W.T.2
  • 21
    • 65649153795 scopus 로고    scopus 로고
    • Capture and release of partially zipped trans-SNARE complexes on intact organelles
    • Schwartz ML, Merz AJ (2009) Capture and release of partially zipped trans-SNARE complexes on intact organelles. J Cell Biol 185(3):535-549.
    • (2009) J Cell Biol , vol.185 , Issue.3 , pp. 535-549
    • Schwartz, M.L.1    Merz, A.J.2
  • 23
    • 0034725579 scopus 로고    scopus 로고
    • The docking of primed vacuoles can be reversibly arrested by excess Sec17p (alpha-SNAP)
    • Wang L, Ungermann C, Wickner W (2000) The docking of primed vacuoles can be reversibly arrested by excess Sec17p (alpha-SNAP). J Biol Chem 275(30):22862-22867.
    • (2000) J Biol Chem , vol.275 , Issue.30 , pp. 22862-22867
    • Wang, L.1    Ungermann, C.2    Wickner, W.3
  • 24
    • 84920939501 scopus 로고    scopus 로고
    • Yeast vacuolar HOPS, regulated by its kinase, exploits affinities for acidic lipids and Rab:GTP for membrane binding and to catalyze tethering and fusion
    • Orr A, Wickner W, Rusin SF, Kettenbach AN, Zick M (2015) Yeast vacuolar HOPS, regulated by its kinase, exploits affinities for acidic lipids and Rab:GTP for membrane binding and to catalyze tethering and fusion. Mol Biol Cell 26(2):305-315.
    • (2015) Mol Biol Cell , vol.26 , Issue.2 , pp. 305-315
    • Orr, A.1    Wickner, W.2    Rusin, S.F.3    Kettenbach, A.N.4    Zick, M.5
  • 25
    • 84898767505 scopus 로고    scopus 로고
    • Membranes linked by trans-SNARE complexes require lipids prone to non-bilayer structure for progression to fusion
    • Zick M, Stroupe C, Orr A, Douville D, Wickner WT (2014) Membranes linked by trans-SNARE complexes require lipids prone to non-bilayer structure for progression to fusion. eLife 3:e01879.
    • (2014) eLife , vol.3 , pp. e01879
    • Zick, M.1    Stroupe, C.2    Orr, A.3    Douville, D.4    Wickner, W.T.5
  • 26
    • 0032549708 scopus 로고    scopus 로고
    • SNAREpins:Minimal machinery for membrane fusion
    • Weber T, et al. (1998) SNAREpins:Minimal machinery for membrane fusion. Cell 92(6):759-772.
    • (1998) Cell , vol.92 , Issue.6 , pp. 759-772
    • Weber, T.1
  • 27
    • 4143122322 scopus 로고    scopus 로고
    • Resolution of organelle docking and fusion kinetics in a cell-free assay
    • Merz AJ, Wickner WT (2004) Resolution of organelle docking and fusion kinetics in a cell-free assay. Proc Natl Acad Sci USA 101(32):11548-11553.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.32 , pp. 11548-11553
    • Merz, A.J.1    Wickner, W.T.2
  • 28
    • 70450230360 scopus 로고    scopus 로고
    • A conserved membrane attachment site in alpha-SNAP facilitates N-ethylmaleimide-sensitive factor (NSF)-driven SNARE complex disassembly
    • Winter U, Chen X, Fasshauer D (2009) A conserved membrane attachment site in alpha-SNAP facilitates N-ethylmaleimide-sensitive factor (NSF)-driven SNARE complex disassembly. J Biol Chem 284(46):31817-31826.
    • (2009) J Biol Chem , vol.284 , Issue.46 , pp. 31817-31826
    • Winter, U.1    Chen, X.2    Fasshauer, D.3
  • 29
    • 84923096947 scopus 로고    scopus 로고
    • Mechanistic insights into the recycling machine of the SNARE complex
    • Zhao M, et al. (2015) Mechanistic insights into the recycling machine of the SNARE complex. Nature 518(7537):61-67.
    • (2015) Nature , vol.518 , Issue.7537 , pp. 61-67
    • Zhao, M.1
  • 30
    • 0037697285 scopus 로고    scopus 로고
    • Defining the SNARE complex binding surface of alpha-SNAP: Implications for SNARE complex disassembly
    • Marz KE, Lauer JM, Hanson PI (2003) Defining the SNARE complex binding surface of alpha-SNAP: Implications for SNARE complex disassembly. J Biol Chem 278(29):27000-27008.
    • (2003) J Biol Chem , vol.278 , Issue.29 , pp. 27000-27008
    • Marz, K.E.1    Lauer, J.M.2    Hanson, P.I.3
  • 31
    • 0035800765 scopus 로고    scopus 로고
    • Molecular mass, stoichiometry, and assembly of 20 S particles
    • Wimmer C, et al. (2001) Molecular mass, stoichiometry, and assembly of 20 S particles. J Biol Chem 276(31):29091-29097.
    • (2001) J Biol Chem , vol.276 , Issue.31 , pp. 29091-29097
    • Wimmer, C.1
  • 32
    • 52249085200 scopus 로고    scopus 로고
    • Efficient termination of vacuolar Rab GTPase signaling requires coordinated action by a GAP and a protein kinase
    • Brett CL, et al. (2008) Efficient termination of vacuolar Rab GTPase signaling requires coordinated action by a GAP and a protein kinase. J Cell Biol 182(6):1141-1151.
    • (2008) J Cell Biol , vol.182 , Issue.6 , pp. 1141-1151
    • Brett, C.L.1
  • 33
    • 0037415612 scopus 로고    scopus 로고
    • Hierarchy of protein assembly at the vertex ring domain for yeast vacuole docking and fusion
    • Wang L, Merz AJ, Collins KM, Wickner W (2003) Hierarchy of protein assembly at the vertex ring domain for yeast vacuole docking and fusion. J Cell Biol 160(3):365-374.
    • (2003) J Cell Biol , vol.160 , Issue.3 , pp. 365-374
    • Wang, L.1    Merz, A.J.2    Collins, K.M.3    Wickner, W.4
  • 34
    • 11244258475 scopus 로고    scopus 로고
    • Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles
    • Fratti RA, Jun Y, Merz AJ, Margolis N, Wickner W (2004) Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles. J Cell Biol 167(6):1087-1098.
    • (2004) J Cell Biol , vol.167 , Issue.6 , pp. 1087-1098
    • Fratti, R.A.1    Jun, Y.2    Merz, A.J.3    Margolis, N.4    Wickner, W.5
  • 35
    • 84901236309 scopus 로고    scopus 로고
    • SM proteins Sly1 and Vps33 co-assemble with Sec17 and SNARE complexes to oppose SNARE disassembly by Sec18
    • Lobingier BT, Nickerson DP, Lo SY, Merz AJ (2014) SM proteins Sly1 and Vps33 co-assemble with Sec17 and SNARE complexes to oppose SNARE disassembly by Sec18. eLife 3:e02272.
    • (2014) eLife , vol.3 , pp. e02272
    • Lobingier, B.T.1    Nickerson, D.P.2    Lo, S.Y.3    Merz, A.J.4
  • 36
    • 55249096894 scopus 로고    scopus 로고
    • Comprehensive mass-spectrometry-based proteome quantification of haploid versus diploid yeast
    • de Godoy LM, et al. (2008) Comprehensive mass-spectrometry-based proteome quantification of haploid versus diploid yeast. Nature 455(7217):1251-1254.
    • (2008) Nature , vol.455 , Issue.7217 , pp. 1251-1254
    • De Godoy, L.M.1
  • 37
    • 84864817904 scopus 로고    scopus 로고
    • PaxDb, a database of protein abundance averages across all three domains of life
    • Wang M, et al. (2012) PaxDb, a database of protein abundance averages across all three domains of life. Mol Cell Proteomics 11(8):492-500.
    • (2012) Mol Cell Proteomics , vol.11 , Issue.8 , pp. 492-500
    • Wang, M.1
  • 38
    • 0025276048 scopus 로고
    • Cellular concentrations of enzymes and their substrates
    • Albe KR, Butler MH, Wright BE (1990) Cellular concentrations of enzymes and their substrates. J Theor Biol 143(2):163-195.
    • (1990) J Theor Biol , vol.143 , Issue.2 , pp. 163-195
    • Albe, K.R.1    Butler, M.H.2    Wright, B.E.3
  • 39
    • 20044377804 scopus 로고    scopus 로고
    • Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion
    • Collins KM, Thorngren NL, Fratti RA, Wickner WT (2005) Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion. EMBO J 24(10):1775-1786.
    • (2005) EMBO J , vol.24 , Issue.10 , pp. 1775-1786
    • Collins, K.M.1    Thorngren, N.L.2    Fratti, R.A.3    Wickner, W.T.4
  • 40
    • 0345363228 scopus 로고    scopus 로고
    • Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane
    • Schneiter R, et al. (1999) Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane. J Cell Biol 146(4):741-754.
    • (1999) J Cell Biol , vol.146 , Issue.4 , pp. 741-754
    • Schneiter, R.1
  • 41
    • 0029009125 scopus 로고
    • Isolation and biochemical characterization of organelles from the yeast, Saccharomyces cerevisiae
    • Zinser E, Daum G (1995) Isolation and biochemical characterization of organelles from the yeast, Saccharomyces cerevisiae. Yeast 11(6):493-536.
    • (1995) Yeast , vol.11 , Issue.6 , pp. 493-536
    • Zinser, E.1    Daum, G.2
  • 42
    • 0033197735 scopus 로고    scopus 로고
    • The length of the flexible SNAREpin juxtamembrane region is a critical determinant of SNARE-dependent fusion
    • McNew JA, Weber T, Engelman DM, Söllner TH, Rothman JE (1999) The length of the flexible SNAREpin juxtamembrane region is a critical determinant of SNARE-dependent fusion. Mol Cell 4(3):415-421.
    • (1999) Mol Cell , vol.4 , Issue.3 , pp. 415-421
    • McNew, J.A.1    Weber, T.2    Engelman, D.M.3    Söllner, T.H.4    Rothman, J.E.5
  • 43
    • 37149039641 scopus 로고    scopus 로고
    • Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion
    • Jun Y, Xu H, Thorngren N, Wickner W (2007) Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion. EMBO J 26(24):4935-4945.
    • (2007) EMBO J , vol.26 , Issue.24 , pp. 4935-4945
    • Jun, Y.1    Xu, H.2    Thorngren, N.3    Wickner, W.4
  • 44
    • 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 ZP, Südhof TC (2013) Lipid-anchored SNAREs lacking transmembrane regions fully support membrane fusion during neurotransmitter release. Neuron 80(2):470-483.
    • (2013) Neuron , vol.80 , Issue.2 , pp. 470-483
    • Zhou, P.1    Bacaj, T.2    Yang, X.3    Pang, Z.P.4    Südhof, T.C.5
  • 45
    • 59049093107 scopus 로고    scopus 로고
    • Effects of linker sequences on vesicle fusion mediated by lipid-anchored DNA oligonucleotides
    • Chan YH, van Lengerich B, Boxer SG (2009) Effects of linker sequences on vesicle fusion mediated by lipid-anchored DNA oligonucleotides. Proc Natl Acad Sci USA 106(4):979-984.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.4 , pp. 979-984
    • Chan, Y.H.1    Van Lengerich, B.2    Boxer, S.G.3
  • 46
    • 84880386623 scopus 로고    scopus 로고
    • Individual vesicle fusion events mediated by lipid-anchored DNA
    • van Lengerich B, Rawle RJ, Bendix PM, Boxer SG (2013) Individual vesicle fusion events mediated by lipid-anchored DNA. Biophys J 105(2):409-419.
    • (2013) Biophys J , vol.105 , Issue.2 , pp. 409-419
    • Van Lengerich, B.1    Rawle, R.J.2    Bendix, P.M.3    Boxer, S.G.4
  • 47
    • 0036180245 scopus 로고    scopus 로고
    • Vacuole fusion at a ring of vertex docking sites leaves membrane fragments within the organelle
    • Wang L, Seeley ES, Wickner W, Merz AJ (2002) Vacuole fusion at a ring of vertex docking sites leaves membrane fragments within the organelle. Cell 108(3):357-369.
    • (2002) Cell , vol.108 , Issue.3 , pp. 357-369
    • Wang, L.1    Seeley, E.S.2    Wickner, W.3    Merz, A.J.4
  • 48
    • 33745938170 scopus 로고    scopus 로고
    • Unraveling the mechanisms of synaptotagmin and SNARE function in neurotransmitter release
    • Rizo J, Chen X, Araç D (2006) Unraveling the mechanisms of synaptotagmin and SNARE function in neurotransmitter release. Trends Cell Biol 16(7):339-350.
    • (2006) Trends Cell Biol , vol.16 , Issue.7 , pp. 339-350
    • Rizo, J.1    Chen, X.2    Araç, D.3
  • 49
    • 84868581277 scopus 로고    scopus 로고
    • Phosphatidylserine inhibits and calcium promotes model membrane fusion
    • Tarafdar PK, Chakraborty H, Dennison SM, Lentz BR (2012) Phosphatidylserine inhibits and calcium promotes model membrane fusion. Biophys J 103(9):1880-1889.
    • (2012) Biophys J , vol.103 , Issue.9 , pp. 1880-1889
    • Tarafdar, P.K.1    Chakraborty, H.2    Dennison, S.M.3    Lentz, B.R.4
  • 50
    • 84866132236 scopus 로고    scopus 로고
    • Single reconstituted neuronal SNARE complexes zipper in three distinct stages
    • Gao Y, et al. (2012) Single reconstituted neuronal SNARE complexes zipper in three distinct stages. Science 337(6100):1340-1343.
    • (2012) Science , vol.337 , Issue.6100 , pp. 1340-1343
    • Gao, Y.1
  • 51
    • 84874769362 scopus 로고    scopus 로고
    • Calcium control of neurotransmitter release
    • Südhof TC (2012) Calcium control of neurotransmitter release. Cold Spring Harb Perspect Biol 4(1):a011353.
    • (2012) Cold Spring Harb Perspect Biol , vol.4 , Issue.1 , pp. a011353
    • Südhof, T.C.1
  • 52
    • 0034648771 scopus 로고    scopus 로고
    • Functional architecture of an intracellular membrane t-SNARE
    • Fukuda R, et al. (2000) Functional architecture of an intracellular membrane t-SNARE. Nature 407(6801):198-202.
    • (2000) Nature , vol.407 , Issue.6801 , pp. 198-202
    • Fukuda, R.1
  • 53
    • 0030015868 scopus 로고    scopus 로고
    • Homotypic vacuole fusion requires Sec17p (yeast alpha-SNAP) and Sec18p (yeast NSF)
    • Haas A, Wickner W (1996) Homotypic vacuole fusion requires Sec17p (yeast alpha-SNAP) and Sec18p (yeast NSF). EMBO J 15(13):3296-3305.
    • (1996) EMBO J , vol.15 , Issue.13 , pp. 3296-3305
    • Haas, A.1    Wickner, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.