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Volumn 110, Issue 48, 2013, Pages 19384-19389

Prefusion structure of syntaxin-1A suggests pathway for folding into neuronal trans-SNARE complex fusion intermediate

Author keywords

FLIC microscopy; Membrane protein structure; Nuclear magnetic resonance

Indexed keywords

SNARE PROTEIN; SYNAPTOBREVIN 2; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNTAXIN 1A;

EID: 84888310908     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1314699110     Document Type: Article
Times cited : (55)

References (43)
  • 1
    • 33644770187 scopus 로고    scopus 로고
    • Structure and function of SNARE and SNARE-interacting proteins
    • Brunger AT (2005) Structure and function of SNARE and SNARE-interacting proteins. Q Rev Biophys 38(1): 1-47.
    • (2005) Q Rev Biophys , vol.38 , Issue.1 , pp. 1-47
    • Brunger, A.T.1
  • 2
    • 84867295592 scopus 로고    scopus 로고
    • Molecular machines governing exocytosis of synaptic vesicles
    • Jahn R, Fasshauer D (2012) Molecular machines governing exocytosis of synaptic vesicles. Nature 490(7419): 201-207.
    • (2012) Nature , vol.490 , Issue.7419 , pp. 201-207
    • Jahn, R.1    Fasshauer, D.2
  • 3
    • 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
  • 4
    • 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
  • 5
    • 33747622293 scopus 로고    scopus 로고
    • SNAREs - Engines for membrane fusion
    • Jahn R, Scheller RH (2006) SNAREs - engines for membrane fusion. Nat Rev Mol Cell Biol 7(9): 631-643.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , Issue.9 , pp. 631-643
    • Jahn, R.1    Scheller, R.H.2
  • 6
    • 0032544441 scopus 로고    scopus 로고
    • Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A
    • Fernandez I, et al. (1998) Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A. Cell 94(6): 841-849.
    • (1998) Cell , vol.94 , Issue.6 , pp. 841-849
    • Fernandez, I.1
  • 7
    • 0034713847 scopus 로고    scopus 로고
    • Structural analysis of the neuronal SNARE protein syntaxin-1A
    • Lerman JC, Robblee J, Fairman R, Hughson FM (2000) Structural analysis of the neuronal SNARE protein syntaxin-1A. Biochemistry 39(29): 8470-8479.
    • (2000) Biochemistry , vol.39 , Issue.29 , pp. 8470-8479
    • Lerman, J.C.1    Robblee, J.2    Fairman, R.3    Hughson, F.M.4
  • 8
    • 41949130893 scopus 로고    scopus 로고
    • Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide
    • Burkhardt P, Hattendorf DA, Weis WI, Fasshauer D (2008) Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide. EMBO J 27(7): 923-933.
    • (2008) EMBO J , vol.27 , Issue.7 , pp. 923-933
    • Burkhardt, P.1    Hattendorf, D.A.2    Weis, W.I.3    Fasshauer, D.4
  • 9
    • 70450235266 scopus 로고    scopus 로고
    • Single vesicle millisecond fusion kinetics reveals number of SNARE complexes optimal for fast SNAREmediated membrane fusion
    • Domanska MK, Kiessling V, Stein A, Fasshauer D, Tamm LK (2009) Single vesicle millisecond fusion kinetics reveals number of SNARE complexes optimal for fast SNAREmediated membrane fusion. J Biol Chem 284(46): 32158-32166.
    • (2009) J Biol Chem , vol.284 , Issue.46 , pp. 32158-32166
    • Domanska, M.K.1    Kiessling, V.2    Stein, A.3    Fasshauer, D.4    Tamm, L.K.5
  • 10
    • 33746915109 scopus 로고    scopus 로고
    • N- to C-terminal SNARE complex assembly promotes rapid membrane fusion
    • Pobbati AV, Stein A, Fasshauer D (2006) N- to C-terminal SNARE complex assembly promotes rapid membrane fusion. Science 313(5787): 673-676.
    • (2006) Science , vol.313 , Issue.5787 , pp. 673-676
    • Pobbati, A.V.1    Stein, A.2    Fasshauer, D.3
  • 11
    • 51749100843 scopus 로고    scopus 로고
    • Conformational switch of syntaxin-1 controls synaptic vesicle fusion
    • Gerber SH, et al. (2008) Conformational switch of syntaxin-1 controls synaptic vesicle fusion. Science 321(5895): 1507-1510.
    • (2008) Science , vol.321 , Issue.5895 , pp. 1507-1510
    • Gerber, S.H.1
  • 12
    • 84872802734 scopus 로고    scopus 로고
    • Reconstitution of the vital functions of Munc18 and Munc13 in neurotransmitter release
    • Ma C, Su L, Seven AB, Xu Y, Rizo J (2013) Reconstitution of the vital functions of Munc18 and Munc13 in neurotransmitter release. Science 339(6118): 421-425.
    • (2013) Science , vol.339 , Issue.6118 , pp. 421-425
    • Ma, C.1    Su, L.2    Seven, A.B.3    Xu, Y.4    Rizo, J.5
  • 13
    • 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 MP, et al. (2012) 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(25): 9816-9821.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.25 , pp. 9816-9821
    • Christie, M.P.1
  • 14
    • 84872866275 scopus 로고    scopus 로고
    • Syntaxin-1 N-peptide and Habc-domain perform distinct essential functions in synaptic vesicle fusion
    • Zhou P, et al. (2013) Syntaxin-1 N-peptide and Habc-domain perform distinct essential functions in synaptic vesicle fusion. EMBO J 32(1): 159-171.
    • (2013) EMBO J , vol.32 , Issue.1 , pp. 159-171
    • Zhou, P.1
  • 15
    • 43649085762 scopus 로고    scopus 로고
    • NMR analysis of the closed conformation of syntaxin-1
    • Chen X, Lu J, Dulubova I, Rizo J (2008) NMR analysis of the closed conformation of syntaxin-1. J Biomol NMR 41(1): 43-54.
    • (2008) J Biomol NMR , vol.41 , Issue.1 , pp. 43-54
    • Chen, X.1    Lu, J.2    Dulubova, I.3    Rizo, J.4
  • 16
    • 0034704771 scopus 로고    scopus 로고
    • Three-dimensional structure of the neuronal- Sec1-syntaxin 1a complex
    • Misura KMS, Scheller RH, Weis WI (2000) Three-dimensional structure of the neuronal- Sec1-syntaxin 1a complex. Nature 404(6776): 355-362.
    • (2000) Nature , vol.404 , Issue.6776 , pp. 355-362
    • Misura, K.M.S.1    Scheller, R.H.2    Weis, W.I.3
  • 17
    • 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 SH, Latham CF, Gee CL, James DE, Martin JL (2007) 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(21): 8773-8778.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.21 , pp. 8773-8778
    • Hu, S.H.1    Latham, C.F.2    Gee, C.L.3    James, D.E.4    Martin, J.L.5
  • 18
    • 84875883726 scopus 로고    scopus 로고
    • Allosteric control of syntaxin 1a by Munc18-1: Characterization of the open and closed conformations of syntaxin
    • Dawidowski D, Cafiso DS (2013) Allosteric control of syntaxin 1a by Munc18-1: characterization of the open and closed conformations of syntaxin. Biophys J 104(7): 1585-1594.
    • (2013) Biophys J , vol.104 , Issue.7 , pp. 1585-1594
    • Dawidowski, D.1    Cafiso, D.S.2
  • 19
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
    • Sutton RB, Fasshauer D, Jahn R, Brunger AT (1998) Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature 395(6700): 347-353.
    • (1998) Nature , vol.395 , Issue.6700 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 20
    • 67749120188 scopus 로고    scopus 로고
    • Helical extension of the neuronal SNARE complex into the membrane
    • Stein A, Weber G, Wahl MC, Jahn R (2009) Helical extension of the neuronal SNARE complex into the membrane. Nature 460(7254): 525-528.
    • (2009) Nature , vol.460 , Issue.7254 , pp. 525-528
    • Stein, A.1    Weber, G.2    Wahl, M.C.3    Jahn, R.4
  • 21
    • 18144392619 scopus 로고    scopus 로고
    • A partially zipped SNARE complex stabilized by the membrane
    • Zhang YH, Su ZL, Zhang F, Chen Y, Shin YK (2005) A partially zipped SNARE complex stabilized by the membrane. J Biol Chem 280(16): 15595-15600.
    • (2005) J Biol Chem , vol.280 , Issue.16 , pp. 15595-15600
    • Zhang, Y.H.1    Su, Z.L.2    Zhang, F.3    Chen, Y.4    Shin, Y.K.5
  • 22
    • 28844480494 scopus 로고    scopus 로고
    • Effective rotational correlation times of proteins from NMR relaxation interference
    • Lee D, Hilty C, Wider G, Wüthrich K (2006) Effective rotational correlation times of proteins from NMR relaxation interference. J Magn Reson 178(1): 72-76.
    • (2006) J Magn Reson , vol.178 , Issue.1 , pp. 72-76
    • Lee, D.1    Hilty, C.2    Wider, G.3    Wüthrich, K.4
  • 23
    • 36049014994 scopus 로고    scopus 로고
    • Size and shape of detergent micelles determined by small-angle X-ray scattering
    • Lipfert J, Columbus L, Chu VB, Lesley SA, Doniach S (2007) Size and shape of detergent micelles determined by small-angle X-ray scattering. J Phys Chem B 111(43): 12427-12438.
    • (2007) J Phys Chem B , vol.111 , Issue.43 , pp. 12427-12438
    • Lipfert, J.1    Columbus, L.2    Chu, V.B.3    Lesley, S.A.4    Doniach, S.5
  • 24
    • 0030247064 scopus 로고    scopus 로고
    • Fluorescence interference-contrast microscopy on oxidized silicon using a monomolecular dye layer
    • Lambacher A, Fromherz P (1996) Fluorescence interference-contrast microscopy on oxidized silicon using a monomolecular dye layer. Appl Phys Adv Mater 63(3): 207-216.
    • (1996) Appl Phys Adv Mater , vol.63 , Issue.3 , pp. 207-216
    • Lambacher, A.1    Fromherz, P.2
  • 25
    • 0037216786 scopus 로고    scopus 로고
    • Measuring distances in supported bilayers by fluorescence interference-contrast microscopy: Polymer supports and SNARE proteins
    • Kiessling V, Tamm LK (2003) Measuring distances in supported bilayers by fluorescence interference-contrast microscopy: polymer supports and SNARE proteins. Biophys J 84(1): 408-418.
    • (2003) Biophys J , vol.84 , Issue.1 , pp. 408-418
    • Kiessling, V.1    Tamm, L.K.2
  • 26
    • 20444429381 scopus 로고    scopus 로고
    • Probing the structure of supported membranes and tethered oligonucleotides by fluorescence interference contrast microscopy
    • Ajo-Franklin CM, Yoshina-Ishii C, Boxer SG (2005) Probing the structure of supported membranes and tethered oligonucleotides by fluorescence interference contrast microscopy. Langmuir 21(11): 4976-4983.
    • (2005) Langmuir , vol.21 , Issue.11 , pp. 4976-4983
    • Ajo-Franklin, C.M.1    Yoshina-Ishii, C.2    Boxer, S.G.3
  • 27
    • 73949139901 scopus 로고    scopus 로고
    • Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation
    • Ellena JF, et al. (2009) Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. Proc Natl Acad Sci USA 106(48): 20306-20311.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.48 , pp. 20306-20311
    • Ellena, J.F.1
  • 28
    • 48749099702 scopus 로고    scopus 로고
    • HOPS proofreads the trans-SNARE complex for yeast vacuole fusion
    • Starai VJ, Hickey CM, Wickner W (2008) HOPS proofreads the trans-SNARE complex for yeast vacuole fusion. Mol Biol Cell 19(6): 2500-2508.
    • (2008) Mol Biol Cell , vol.19 , Issue.6 , pp. 2500-2508
    • Starai, V.J.1    Hickey, C.M.2    Wickner, W.3
  • 29
    • 34948901461 scopus 로고    scopus 로고
    • Distinct domains of complexin i differentially regulate neurotransmitter release
    • Xue M, et al. (2007) Distinct domains of complexin I differentially regulate neurotransmitter release. Nat Struct Mol Biol 14(10): 949-958.
    • (2007) Nat Struct Mol Biol , vol.14 , Issue.10 , pp. 949-958
    • Xue, M.1
  • 30
    • 58849105859 scopus 로고    scopus 로고
    • Alternative zippering as an on-off switch for SNARE-mediated fusion
    • Giraudo CG, et al. (2009) Alternative zippering as an on-off switch for SNARE-mediated fusion. Science 323(5913): 512-516.
    • (2009) Science , vol.323 , Issue.5913 , pp. 512-516
    • Giraudo, C.G.1
  • 31
    • 27844499290 scopus 로고    scopus 로고
    • Autonomous function of synaptotagmin 1 in triggering synchronous release independent of asynchronous release
    • Maximov A, Südhof TC (2005) Autonomous function of synaptotagmin 1 in triggering synchronous release independent of asynchronous release. Neuron 48(4): 547-554.
    • (2005) Neuron , vol.48 , Issue.4 , pp. 547-554
    • Maximov, A.1    Südhof, T.C.2
  • 32
    • 0037157825 scopus 로고    scopus 로고
    • Calcium-independent stimulation of membrane fusion and SNAREpin formation by synaptotagmin i
    • Mahal LK, Sequeira SM, Gureasko JM, Söllner TH (2002) Calcium-independent stimulation of membrane fusion and SNAREpin formation by synaptotagmin I. J Cell Biol 158(2): 273-282.
    • (2002) J Cell Biol , vol.158 , Issue.2 , pp. 273-282
    • Mahal, L.K.1    Sequeira, S.M.2    Gureasko, J.M.3    Söllner, T.H.4
  • 33
    • 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
  • 34
    • 84862630110 scopus 로고    scopus 로고
    • Membrane fusion intermediates via directional and full assembly of the SNARE complex
    • Hernandez JM, et al. (2012) Membrane fusion intermediates via directional and full assembly of the SNARE complex. Science 336(6088): 1581-1584.
    • (2012) Science , vol.336 , Issue.6088 , pp. 1581-1584
    • Hernandez, J.M.1
  • 35
    • 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 (2011) Munc13 mediates the transition from the closed syntaxin-Munc18 complex to the SNARE complex. Nat Struct Mol Biol 18(5): 542-549.
    • (2011) Nat Struct Mol Biol , vol.18 , Issue.5 , pp. 542-549
    • Ma, C.1    Li, W.2    Xu, Y.3    Rizo, J.4
  • 36
    • 80655149438 scopus 로고    scopus 로고
    • Munc18-1 domain-1 controls vesicle docking and secretion by interacting with syntaxin-1 and chaperoning it to the plasma membrane
    • Han GA, et al. (2011) Munc18-1 domain-1 controls vesicle docking and secretion by interacting with syntaxin-1 and chaperoning it to the plasma membrane. Mol Biol Cell 22(21): 4134-4149.
    • (2011) Mol Biol Cell , vol.22 , Issue.21 , pp. 4134-4149
    • Han, G.A.1
  • 37
    • 0037204063 scopus 로고    scopus 로고
    • Differential control of vesicle priming and short-term plasticity by Munc13 isoforms
    • Rosenmund C, et al. (2002) Differential control of vesicle priming and short-term plasticity by Munc13 isoforms. Neuron 33(3): 411-424.
    • (2002) Neuron , vol.33 , Issue.3 , pp. 411-424
    • Rosenmund, C.1
  • 38
    • 1542297734 scopus 로고    scopus 로고
    • Determinants of liposome fusion mediated by synaptic SNARE proteins
    • Schuette CG, et al. (2004) Determinants of liposome fusion mediated by synaptic SNARE proteins. Proc Natl Acad Sci USA 101(9): 2858-2863.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.9 , pp. 2858-2863
    • Schuette, C.G.1
  • 39
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Shen Y, Delaglio F, Cornilescu G, Bax A (2009) TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44(4): 213-223.
    • (2009) J Biomol NMR , vol.44 , Issue.4 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 40
    • 50449105226 scopus 로고    scopus 로고
    • Automated errortolerant macromolecular structure determination from multidimensional nuclear Overhauser enhancement spectra and chemical shift assignments: Improved robustness and performance of the PASD algorithm
    • Kuszewski JJ, Thottungal RA, Clore GM, Schwieters CD (2008) Automated errortolerant macromolecular structure determination from multidimensional nuclear Overhauser enhancement spectra and chemical shift assignments: improved robustness and performance of the PASD algorithm. J Biomol NMR 41(4): 221-239.
    • (2008) J Biomol NMR , vol.41 , Issue.4 , pp. 221-239
    • Kuszewski, J.J.1    Thottungal, R.A.2    Clore, G.M.3    Schwieters, C.D.4
  • 42
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski RA, Rullmannn JA, MacArthur MW, Kaptein R, Thornton JM (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8(4): 477-486.
    • (1996) J Biomol NMR , vol.8 , Issue.4 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    Macarthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 43
    • 0033543577 scopus 로고    scopus 로고
    • Altered flexibility in the substratebinding site of related native and engineered high-alkaline Bacillus subtilisins
    • Mulder FAA, Schipper D, Bott R, Boelens R (1999) Altered flexibility in the substratebinding site of related native and engineered high-alkaline Bacillus subtilisins. J Mol Biol 292(1): 111-123.
    • (1999) J Mol Biol , vol.292 , Issue.1 , pp. 111-123
    • Mulder, F.A.A.1    Schipper, D.2    Bott, R.3    Boelens, R.4


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