메뉴 건너뛰기




Volumn 31, Issue 6, 2011, Pages 457-463

Single-molecule FRET study of SNARE-mediated membrane fusion

Author keywords

Fluorescence resonance energy transfer (FRET); Membrane fusion; Single molecule; Soluble N ethylmaleimide sensitive factor attachment protein receptor (SNARE)

Indexed keywords

FLUORESCENT DYE; SNARE PROTEIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNAPTOTAGMIN I; SYNTAXIN 1A;

EID: 84155176609     PISSN: 01448463     EISSN: None     Source Type: Journal    
DOI: 10.1042/BSR20110011     Document Type: Review
Times cited : (23)

References (52)
  • 1
    • 0026492542 scopus 로고
    • Membrane fusion
    • White, J. M. (1992) Membrane fusion. Science 258, 917-924
    • (1992) Science , vol.258 , pp. 917-924
    • White, J.M.1
  • 2
    • 0037459076 scopus 로고    scopus 로고
    • Membrane fusion
    • DOI 10.1016/S0092-8674(03)00112-0
    • Jahn, R., Lang, T. and Sudhof, T. C. (2003) Membrane fusion. Cell 112, 519-533 (Pubitemid 36263084)
    • (2003) Cell , vol.112 , Issue.4 , pp. 519-533
    • Jahn, R.1    Lang, T.2    Sudhof, T.C.3
  • 4
    • 59349117350 scopus 로고    scopus 로고
    • Progress in understanding the neuronal SNARE function and its regulation
    • Yoon, T. -Y. and Shin, Y. -K. (2009) Progress in understanding the neuronal SNARE function and its regulation. Cell. Mol. Life Sci. 66, 460-469
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 460-469
    • Yoon, T.-Y.1    Shin, Y.-K.2
  • 5
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • Stryer, L. (1978) Fluorescence energy transfer as a spectroscopic ruler. Annu. Rev. Biochem. 47, 819-846
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 819-846
    • Stryer, L.1
  • 7
    • 23144455040 scopus 로고    scopus 로고
    • Single-molecule studies of synaptotagmin and complexin binding to the SNARE complex
    • DOI 10.1529/biophysj.104.054064
    • Bowen, M. E., Weninger, K., Ernst, J., Chu, S. and Brunger, A. T. (2005) Single-molecule studies of synaptotagmin and complexin binding to the SNARE complex. Biophys. J. 89, 690-702 (Pubitemid 41098319)
    • (2005) Biophysical Journal , vol.89 , Issue.1 , pp. 690-702
    • Bowen, M.E.1    Weninger, K.2    Ernst, J.3    Chu, S.4    Brunger, A.T.5
  • 8
    • 38949211822 scopus 로고    scopus 로고
    • Accessory Proteins Stabilize the Acceptor Complex for Synaptobrevin, the 1:1 Syntaxin/SNAP-25 Complex
    • DOI 10.1016/j.str.2007.12.010, PII S096921260800004X
    • Weninger, K., Bowen, M. E., Choi, U. B., Chu, S. and Brunger, A. T. (2008) Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin/SNAP-25 complex. Structure 16, 308-320 (Pubitemid 351222650)
    • (2008) Structure , vol.16 , Issue.2 , pp. 308-320
    • Weninger, K.1    Bowen, M.E.2    Choi, U.B.3    Chu, S.4    Brunger, A.T.5
  • 9
    • 34548792937 scopus 로고    scopus 로고
    • Kinetics of complexin binding to the SNARE complex: Correcting single molecule FRET measurements for hidden events
    • DOI 10.1529/biophysj.106.101220
    • Li, Y., Augustine, G. J. and Weninger, K. (2007) Kinetics of complexin binding to the SNARE complex: correcting single molecule FRET measurements for hidden events. Biophys. J. 93, 2178-2187 (Pubitemid 47437601)
    • (2007) Biophysical Journal , vol.93 , Issue.6 , pp. 2178-2187
    • Li, Y.1    Augustine, G.J.2    Weninger, K.3
  • 12
    • 46049088692 scopus 로고    scopus 로고
    • The SNARE Complex from Yeast Is Partially Unstructured on the Membrane
    • DOI 10.1016/j.str.2008.03.018, PII S0969212608001834
    • Su, Z., Ishitsuka, Y., Ha, T. and Shin, Y. -K. (2008) The SNARE complex from yeast is partially unstructured on the membrane. Structure 16, 1138-1146 (Pubitemid 351899286)
    • (2008) Structure , vol.16 , Issue.7 , pp. 1138-1146
    • Su, Z.1    Ishitsuka, Y.2    Ha, T.3    Shin, Y.-K.4
  • 14
    • 67650021208 scopus 로고    scopus 로고
    • C2AB: A molecular glue for lipid vesicles with negatively charged surface
    • Diao, J., Yoon, T. -Y., Su, Z., Shin, Y. -K. and Ha, T. (2009) C2AB: a molecular glue for lipid vesicles with negatively charged surface. Langmuir 25, 7177-7180
    • (2009) Langmuir , vol.25 , pp. 7177-7180
    • Diao, J.1    Yoon, T.-Y.2    Su, Z.3    Shin, Y.-K.4    Ha, T.5
  • 15
    • 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., Su, Z., Lu, X., Yoon, T. -Y., Shin, Y. -K. and Ha, T. (2010) 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) ACS Chem. Neurosci. , vol.1 , pp. 168-174
    • Diao, J.1    Su, Z.2    Lu, X.3    Yoon, T.-Y.4    Shin, Y.-K.5    Ha, T.6
  • 18
    • 84155194865 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted
  • 19
    • 67650759736 scopus 로고    scopus 로고
    • Single-molecule studies of the neuronal SNARE fusion machinery
    • Brunger, A. T., Weninger, K., Bowen, M. and Chu, S. (2009) Single-molecule studies of the neuronal SNARE fusion machinery. Annu. Rev. Biochem. 78, 903-928
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 903-928
    • Brunger, A.T.1    Weninger, K.2    Bowen, M.3    Chu, S.4
  • 20
    • 0034713847 scopus 로고    scopus 로고
    • Structural analysis of the neuronal SNARE protein syntaxin-1A
    • DOI 10.1021/bi0003994
    • Lerman, J. C., Robblee, J., Fairman, R. and Hughson, F. M. (2000) Structural analysis of the neuronal SNARE protein syntaxin-1A. Biochem. 39, 8470-8479 (Pubitemid 30489943)
    • (2000) Biochemistry , vol.39 , Issue.29 , pp. 8470-8479
    • Lerman, J.C.1    Robblee, J.2    Fairman, R.3    Hughson, F.M.4
  • 22
    • 43649085762 scopus 로고    scopus 로고
    • NMR analysis of the closed conformation of syntaxin-1
    • Chen, X., Lu, J., Dulubova, I. and Rizo, J. (2008) NMR analysis of the closed conformation of syntaxin-1. J. Biomol. NMR 41, 43-54
    • (2008) J. Biomol. NMR , vol.41 , pp. 43-54
    • Chen, X.1    Lu, J.2    Dulubova, I.3    Rizo, J.4
  • 23
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
    • DOI 10.1038/26412
    • Sutton, R., Fasshauer, D., Jahn, R. and Brunger, A. T. (1998) Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution. Nature 395, 347-353 (Pubitemid 28450677)
    • (1998) Nature , vol.395 , Issue.6700 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 24
    • 38149026393 scopus 로고    scopus 로고
    • The Structure of the yeast plasma membrane SNARE complex reveals destabilizing water-filled cavities
    • Strop, P., Kaiser, S. E., Vrljic, M. and Brunger, A. T. (2008) The Structure of the yeast plasma membrane SNARE complex reveals destabilizing water-filled cavities. J. Biol. Chem. 283, 1113-1119
    • (2008) J. Biol. Chem. , vol.283 , pp. 1113-1119
    • Strop, P.1    Kaiser, S.E.2    Vrljic, M.3    Brunger, A.T.4
  • 27
    • 77649270851 scopus 로고    scopus 로고
    • Detecting the conformation of individual proteins in live cells
    • Sakon, J. J. and Weninger, K. R. (2010) Detecting the conformation of individual proteins in live cells. Nat. Methods 7, 203-205
    • (2010) Nat. Methods , vol.7 , pp. 203-205
    • Sakon, J.J.1    Weninger, K.R.2
  • 29
    • 22144492905 scopus 로고    scopus 로고
    • Accurate FRET measurements within single diffusing biomolecules using alternating-laser excitation
    • DOI 10.1529/biophysj.104.054114
    • Lee, N. K., Kapanidis, A. N., Wang, Y., Michalet, X., Mukhopadhyay, J., Ebright, R. H. and Weiss, S. (2005) Accurate FRET measurements within single diffusing biomolecules using alternating-laser excitation. Biophys. J. 88, 2939-2953 (Pubitemid 40976158)
    • (2005) Biophysical Journal , vol.88 , Issue.4 , pp. 2939-2953
    • Lee, N.K.1    Kapanidis, A.N.2    Wang, Y.3    Michalet, X.4    Mukhopadhyay, J.5    Ebright, R.H.6    Weiss, S.7
  • 30
    • 33746408759 scopus 로고    scopus 로고
    • Accurate single-pair Förster resonant energy transfer through combination of pulsed interleaved excitation, time correlated single-photon counting, and fluorescence correlation spectroscopy
    • Ruttinger, S., Macdonald, R., Kramer, B., Koberling, F., Roos, M. and Hildt, E. (2006) Accurate single-pair Förster resonant energy transfer through combination of pulsed interleaved excitation, time correlated single-photon counting, and fluorescence correlation spectroscopy. J. Biomed. Opt. 11, 024012
    • (2006) J. Biomed. Opt. , vol.11 , pp. 024012
    • Ruttinger, S.1    Macdonald, R.2    Kramer, B.3    Koberling, F.4    Roos, M.5    Hildt, E.6
  • 31
    • 79851509342 scopus 로고    scopus 로고
    • Three-dimensional molecular modeling with single molecule FRET
    • Brunger, A. T., Strop, P., Vrljic, M., Chu, S. and Weninger, K. R. (2011) Three-dimensional molecular modeling with single molecule FRET. J. Struct. Biol. 173, 497-505
    • (2011) J. Struct. Biol. , vol.173 , pp. 497-505
    • Brunger, A.T.1    Strop, P.2    Vrljic, M.3    Chu, S.4    Weninger, K.R.5
  • 32
    • 0019874707 scopus 로고
    • Use of resonance energy transfer to monitor membrane fusion
    • Struck, D. K., Hoekstra, D. and Pagano, R. E. (1981) Use of resonance energy transfer to monitor membrane fusion. Biochemistry 20, 4093-4099
    • (1981) Biochemistry , vol.20 , pp. 4093-4099
    • Struck, D.K.1    Hoekstra, D.2    Pagano, R.E.3
  • 33
    • 0017365231 scopus 로고
    • Lateral diffusion of surface immunoglobulin, Thy-1 antigen, and a lipid probe in lymphocyte plasma membranes
    • Schlessinger, J., Axelrod, D., Koppel, D. E., Webb, W. W. and Elson, E. L. (1977) Lateral diffusion of surface immunoglobulin, Thy-1 antigen, and a lipid probe in lymphocyte plasma membranes. Science 195, 307-309
    • (1977) Science , vol.195 , pp. 307-309
    • Schlessinger, J.1    Axelrod, D.2    Koppel, D.E.3    Webb, W.W.4    Elson, E.L.5
  • 36
    • 16344389389 scopus 로고    scopus 로고
    • Single molecule observation of liposome-bilayer fusion thermally induced by SNAREs
    • Bowen, M. E., Weninger, K., Brunger, A. T. and Chu, S. (2004) Single molecule observation of liposome-bilayer fusion thermally induced by SNAREs. Biophys. J. 87, 3569-3584
    • (2004) Biophys. J. , vol.87 , pp. 3569-3584
    • Bowen, M.E.1    Weninger, K.2    Brunger, A.T.3    Chu, S.4
  • 37
    • 25844484158 scopus 로고    scopus 로고
    • SNARE-driven, 25-millisecond vesicle fusion in vitro
    • DOI 10.1529/biophysj.105.062539
    • Liu, T., Tucker, W. C., Bhalla, A., Chapman, E. R. and Weisshaar, J. C. (2005) SNARE-driven, 25-millisecond vesicle fusion in vitro. Biophys. J. 89, 2458-2472 (Pubitemid 41401035)
    • (2005) Biophysical Journal , vol.89 , Issue.4 , pp. 2458-2472
    • Liu, T.1    Tucker, W.C.2    Bhalla, A.3    Chapman, E.R.4    Weisshaar, J.C.5
  • 38
    • 70450235266 scopus 로고    scopus 로고
    • Single Vesicle millisecond fusion kinetics reveals number of SNARE complexes optimal for fast SNARE-mediated membrane fusion
    • Domanska, M. K., Kiessling, V., Stein, A., Fasshauer, D. and Tamm, L. K. (2009) Single Vesicle millisecond fusion kinetics reveals number of SNARE complexes optimal for fast SNARE-mediated membrane fusion. J. Biol. Chem. 284, 32158-32166
    • (2009) J. Biol. Chem. , vol.284 , pp. 32158-32166
    • Domanska, M.K.1    Kiessling, V.2    Stein, A.3    Fasshauer, D.4    Tamm, L.K.5
  • 40
    • 59049093107 scopus 로고    scopus 로고
    • Effects of linker sequences on vesicle fusion mediated by lipid-anchored DNA oligonucleotides
    • Chan, Y. H., van Lengerich, B. and Boxer, S. G. (2009) Effects of linker sequences on vesicle fusion mediated by lipid-anchored DNA oligonucleotides. Proc. Natl. Acad. Sci. U.S.A 106, 979-984
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 979-984
    • Chan, Y.H.1    Van Lengerich, B.2    Boxer, S.G.3
  • 42
    • 33646151867 scopus 로고    scopus 로고
    • Neuronal SNAREs do not trigger fusion between synthetic membranes but do promote PEG-mediated membrane fusion
    • Dennison, S. M., Bowen, M. E., Brunger, A. T. and Lentz, B. (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, S.M.1    Bowen, M.E.2    Brunger, A.T.3    Lentz, B.4
  • 44
    • 68049123308 scopus 로고    scopus 로고
    • Lipid mixing and content release in single-vesicle, SNARE-driven fusion assay with 1-5 ms resolution
    • Wang, T., Smith, E. A., Chapman, E. R. and Weisshaar, J. C. (2009) Lipid mixing and content release in single-vesicle, SNARE-driven fusion assay with 1-5 ms resolution. Biophys. J. 96, 4122-4131
    • (2009) Biophys. J. , vol.96 , pp. 4122-4131
    • Wang, T.1    Smith, E.A.2    Chapman, E.R.3    Weisshaar, J.C.4
  • 45
    • 33846028172 scopus 로고    scopus 로고
    • Three-color alternating-laser excitation of single molecules: Monitoring multiple interactions and distances
    • DOI 10.1529/biophysj.106.093211
    • Lee, N. K., Kapanidis, A. N., Koh, H. R., Korlann, Y., Ho, S. O., Kim, Y., Gassman, N., Kim, S. K. and Weiss, S. (2007) Three-color alternating-laser excitation of single molecules: monitoring multiple interactions and distances. Biophys. J. 92, 303-312 (Pubitemid 46048438)
    • (2007) Biophysical Journal , vol.92 , Issue.1 , pp. 303-312
    • Nam, K.L.1    Kapanidis, A.N.2    Hye, R.K.3    Korlann, Y.4    Sam, O.H.5    Kim, Y.6    Gassman, N.7    Seong, K.K.8    Weiss, S.9
  • 46
    • 78349288412 scopus 로고    scopus 로고
    • Four-color single-molecule fluorescence with noncovalent dye labeling to monitor dynamic multimolecular complexes
    • DeRocco, V. C., Anderson, T., Piehler, J., Erie, D. A. and Weninger, K. (2010) Four-color single-molecule fluorescence with noncovalent dye labeling to monitor dynamic multimolecular complexes. Biotech. 49, 807-816
    • (2010) Biotech. , vol.49 , pp. 807-816
    • DeRocco, V.C.1    Anderson, T.2    Piehler, J.3    Erie, D.A.4    Weninger, K.5
  • 49
    • 33645325418 scopus 로고    scopus 로고
    • Efficient incorporation of unnatural amino acids into proteins in Escherichia coli
    • Ryu, Y. and Schultz, R G. (2006) Efficient incorporation of unnatural amino acids into proteins in Escherichia coli. Nat. Methods 3, 263-265
    • (2006) Nat. Methods , vol.3 , pp. 263-265
    • Ryu, Y.1    Schultz, R.G.2
  • 50
    • 77951107295 scopus 로고    scopus 로고
    • Real-time tRNA transit on single translating ribosomes at codon resolution
    • Uemura, S., Aitken, C. E., Korlach, J., Flusberg, B. A., Turner, S. W. and Puglisi, J. D. (2010) Real-time tRNA transit on single translating ribosomes at codon resolution. Nature 464, 1012-1017
    • (2010) Nature , vol.464 , pp. 1012-1017
    • Uemura, S.1    Aitken, C.E.2    Korlach, J.3    Flusberg, B.A.4    Turner, S.W.5    Puglisi, J.D.6
  • 52
    • 33749026335 scopus 로고    scopus 로고
    • Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
    • Rust, M. J., Bates, M. and Zhuang, X. (2006) Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM). Nat. Methods 3, 793-796
    • (2006) Nat. Methods , vol.3 , pp. 793-796
    • Rust, M.J.1    Bates, M.2    Zhuang, X.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.