메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages

Direct quantitative detection of Doc2b-induced hemifusion in optically trapped membranes

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM BINDING PROTEIN; CALCIUM ION; DOC2B PROTEIN; PHOSPHATIDYLSERINE; PHOSPHOLIPID; SNARE PROTEIN; UNCLASSIFIED DRUG; ARTIFICIAL MEMBRANE; CALCIUM; DOC2B PROTEIN, RAT; NERVE PROTEIN;

EID: 84942163114     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms9387     Document Type: Article
Times cited : (32)

References (40)
  • 2
    • 0028179011 scopus 로고
    • Lipid-Anchored influenza hemagglutinin promotes hemifusion, not complete fusion
    • Kemble, G. W., Danieli, T. &White, J. M. Lipid-Anchored influenza hemagglutinin promotes hemifusion, not complete fusion. Cell 76, 383-391 (1994)
    • (1994) Cell , vol.76 , pp. 383-391
    • Kemble, G.W.1    Danieli, T.2    White, J.M.3
  • 3
    • 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. &Weisshaar, J. C. Lipid mixing and content release in single-vesicle, SNARE-driven fusion assay with 1-5 ms resolution. Biophys. J. 96, 4122-4131 (2009)
    • (2009) Biophys. J , vol.96 , pp. 4122-4131
    • Wang, T.1    Smith, E.A.2    Chapman, E.R.3    Weisshaar, J.C.4
  • 4
    • 79961082568 scopus 로고    scopus 로고
    • In vitro system capable of differentiating fast Ca2-triggered content mixing from lipid exchange for mechanistic studies of neurotransmitter release
    • Kyoung, M. et al. In vitro system capable of differentiating fast Ca2-triggered content mixing from lipid exchange for mechanistic studies of neurotransmitter release. Proc. Natl Acad. Sci. USA 108, E304-E313 (2011)
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. E304-E313
    • Kyoung, M.1
  • 5
    • 33646489221 scopus 로고    scopus 로고
    • Synaptotagmin i and Ca2 promote half fusion more than full fusion in SNARE-mediated bilayer fusion
    • Lu, X., Xu, Y., Zhang, F. &Shin, Y. K. Synaptotagmin I and Ca2 promote half fusion more than full fusion in SNARE-mediated bilayer fusion. FEBS Lett. 580, 2238-2246 (2006)
    • (2006) FEBS Lett , vol.580 , pp. 2238-2246
    • Lu, X.1    Xu, Y.2    Zhang, F.3    Shin, Y.K.4
  • 6
    • 38949185790 scopus 로고    scopus 로고
    • Productive hemifusion intermediates in fast vesicle fusion driven by neuronal SNAREs
    • Liu, T., Wang, T., Chapman, E. R. &Weisshaar, J. C. Productive hemifusion intermediates in fast vesicle fusion driven by neuronal SNAREs. Biophys. J. 94, 1303-1314 (2008)
    • (2008) Biophys. J , vol.94 , pp. 1303-1314
    • Liu, T.1    Wang, T.2    Chapman, E.R.3    Weisshaar, J.C.4
  • 8
    • 0037072603 scopus 로고    scopus 로고
    • Observation of a membrane fusion intermediate structure
    • Yang, L. &Huang, H. W. Observation of a membrane fusion intermediate structure. Science 297, 1877-1879 (2002)
    • (2002) Science , vol.297 , pp. 1877-1879
    • Yang, L.1    Huang, H.W.2
  • 9
    • 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
  • 10
    • 67749120188 scopus 로고    scopus 로고
    • Helical extension of the neuronal SNARE complex into the membrane
    • Stein, A., Weber, G., Wahl, M. C. &Jahn, R. Helical extension of the neuronal SNARE complex into the membrane. Nature 460, 525-528 (2009)
    • (2009) Nature , vol.460 , pp. 525-528
    • Stein, A.1    Weber, G.2    Wahl, M.C.3    Jahn, R.4
  • 11
    • 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
  • 12
    • 80051933736 scopus 로고    scopus 로고
    • Multiple Ca2 sensors in secretion: Teammates, competitors or autocrats?
    • Walter, A. M., Groffen, A. J., Sorensen, J. B. &Verhage, M. Multiple Ca2 sensors in secretion: teammates, competitors or autocrats? Trends Neurosci. 34, 487-497 (2011)
    • (2011) Trends Neurosci , vol.34 , pp. 487-497
    • Walter, A.M.1    Groffen, A.J.2    Sorensen, J.B.3    Verhage, M.4
  • 13
    • 49449095255 scopus 로고    scopus 로고
    • Synaptotagmin arrests the SNARE complex before triggering fast, efficient membrane fusion in response to Ca2
    • Chicka, M. C., Hui, E., Liu, H. &Chapman, E. R. Synaptotagmin arrests the SNARE complex before triggering fast, efficient membrane fusion in response to Ca2. Nature Struct. Mol. Biol. 15, 827-835 (2008)
    • (2008) Nature Struct. Mol. Biol , vol.15 , pp. 827-835
    • Chicka, M.C.1    Hui, E.2    Liu, H.3    Chapman, E.R.4
  • 14
    • 0027438591 scopus 로고
    • Mutational analysis of Drosophila synaptotagmin demonstrates its essential role in Ca(2)-Activated neurotransmitter release
    • Littleton, J. T., Stern, M., Schulze, K., Perin, M. &Bellen, H. J. Mutational analysis of Drosophila synaptotagmin demonstrates its essential role in Ca(2)-Activated neurotransmitter release. Cell 74, 1125-1134 (1993)
    • (1993) Cell , vol.74 , pp. 1125-1134
    • Littleton, J.T.1    Stern, M.2    Schulze, K.3    Perin, M.4    Bellen, H.J.5
  • 15
    • 0028061861 scopus 로고
    • Synaptotagmin I: A major Ca2 sensor for transmitter release at a central synapse
    • Geppert, M. et al. Synaptotagmin I: a major Ca2 sensor for transmitter release at a central synapse. Cell 79, 717-727 (1994)
    • (1994) Cell , vol.79 , pp. 717-727
    • Geppert, M.1
  • 16
    • 0026631563 scopus 로고
    • Synaptotagmin: A calcium sensor on the synaptic vesicle surface
    • Brose, N., Petrenko, A. G., Sudhof, T. C. &Jahn, R. Synaptotagmin: a calcium sensor on the synaptic vesicle surface. Science 256, 1021-1025 (1992)
    • (1992) Science , vol.256 , pp. 1021-1025
    • Brose, N.1    Petrenko, A.G.2    Sudhof, T.C.3    Jahn, R.4
  • 17
    • 34249933061 scopus 로고    scopus 로고
    • How synaptotagmin promotes membrane fusion
    • Martens, S., Kozlov, M. M. &McMahon, H. T. How synaptotagmin promotes membrane fusion. Science 316, 1205-1208 (2007)
    • (2007) Science , vol.316 , pp. 1205-1208
    • Martens, S.1    Kozlov, M.M.2    McMahon, H.T.3
  • 18
    • 68749083522 scopus 로고    scopus 로고
    • Synaptotagmin-mediated bending of the target membrane is a critical step in Ca(2)-regulated fusion
    • Hui, E., Johnson, C. P., Yao, J., Dunning, F. M. &Chapman, E. R. Synaptotagmin-mediated bending of the target membrane is a critical step in Ca(2)-regulated fusion. Cell 138, 709-721 (2009)
    • (2009) Cell , vol.138 , pp. 709-721
    • Hui, E.1    Johnson, C.P.2    Yao, J.3    Dunning, F.M.4    Chapman, E.R.5
  • 19
    • 0027197065 scopus 로고
    • Synaptotagmin: A calcium-sensitive inhibitor of exocytosis?
    • Popov, S. V. &Poo, M. M. Synaptotagmin: a calcium-sensitive inhibitor of exocytosis? Cell 73, 1247-1249 (1993)
    • (1993) Cell , vol.73 , pp. 1247-1249
    • Popov, S.V.1    Poo, M.M.2
  • 20
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Sollner, T., Bennett, M. K., Whiteheart, S. W., Scheller, R. H. &Rothman, J. E. A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 75, 409-418 (1993)
    • (1993) Cell , vol.75 , pp. 409-418
    • Sollner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 21
    • 0027974130 scopus 로고
    • Calcium dependence of neurotransmitter release and rate of spontaneous vesicle fusions are altered in Drosophila synaptotagmin mutants
    • Littleton, J. T., Stern, M., Perin, M. &Bellen, H. J. Calcium dependence of neurotransmitter release and rate of spontaneous vesicle fusions are altered in Drosophila synaptotagmin mutants. Proc. Natl Acad. Sci. USA 91, 10888-10892 (1994)
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10888-10892
    • Littleton, J.T.1    Stern, M.2    Perin, M.3    Bellen, H.J.4
  • 22
    • 79951717108 scopus 로고    scopus 로고
    • Synaptotagmin increases the dynamic range of synapses by driving Ca2-evoked release and by clamping a nearlinear remaining Ca2 sensor
    • Kochubey, O. &Schneggenburger, R. Synaptotagmin increases the dynamic range of synapses by driving Ca2-evoked release and by clamping a nearlinear remaining Ca2 sensor. Neuron 69, 736-748 (2011)
    • (2011) Neuron , vol.69 , pp. 736-748
    • Kochubey, O.1    Schneggenburger, R.2
  • 23
    • 1842477457 scopus 로고    scopus 로고
    • Synaptotagmin interaction with the syntaxin/SNAP-25 dimer is mediated by an evolutionarily conserved motif and is sensitive to inositol hexakisphosphate
    • Rickman, C. et al. Synaptotagmin interaction with the syntaxin/SNAP-25 dimer is mediated by an evolutionarily conserved motif and is sensitive to inositol hexakisphosphate. J. Biol. Chem. 279, 12574-12579 (2004)
    • (2004) J. Biol. Chem , vol.279 , pp. 12574-12579
    • Rickman, C.1
  • 24
    • 0842291506 scopus 로고    scopus 로고
    • PIP2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane
    • Bai, J., Tucker, W. C. &Chapman, E. R. PIP2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane. Nature Struct. Mol. Biol. 11, 36-44 (2004)
    • (2004) Nature Struct. Mol. Biol , vol.11 , pp. 36-44
    • Bai, J.1    Tucker, W.C.2    Chapman, E.R.3
  • 25
    • 77950286800 scopus 로고    scopus 로고
    • Doc2b is a high-Affinity Ca2 sensor for spontaneous neurotransmitter release
    • Groffen, A. J. et al. Doc2b is a high-Affinity Ca2 sensor for spontaneous neurotransmitter release. Science 327, 1614-1618 (2010)
    • (2010) Science , vol.327 , pp. 1614-1618
    • Groffen, A.J.1
  • 26
    • 33645861074 scopus 로고    scopus 로고
    • DOC2A and DOC2B are sensors for neuronal activity with unique calcium-dependent and kinetic properties
    • Groffen, A. J. A., Friedrich, R., Brian, E. C., Ashery, U. &Verhage, M. DOC2A and DOC2B are sensors for neuronal activity with unique calcium-dependent and kinetic properties. J. Neurochem. 97, 818-833 (2006)
    • (2006) J. Neurochem , vol.97 , pp. 818-833
    • Groffen, A.J.A.1    Friedrich, R.2    Brian, E.C.3    Ashery, U.4    Verhage, M.5
  • 27
    • 0018199103 scopus 로고
    • Does Ca2 cause fusion or lysis of unilamellar lipid vesicles?
    • Ginsberg, L. Does Ca2 cause fusion or lysis of unilamellar lipid vesicles? Nature 275, 758-760 (1978)
    • (1978) Nature , vol.275 , pp. 758-760
    • Ginsberg, L.1
  • 28
    • 80052442505 scopus 로고    scopus 로고
    • Quantifying how DNA stretches, melts and changes twist under tension
    • Gross, P. et al. Quantifying how DNA stretches, melts and changes twist under tension. Nat. Phys 7, 731-736 (2011)
    • (2011) Nat. Phys , vol.7 , pp. 731-736
    • Gross, P.1
  • 29
    • 16644362025 scopus 로고    scopus 로고
    • Using the atomic force microscope to study the interaction between two solid supported lipid bilayers and the influence of synapsin i
    • Pera, I., Stark, R., Kappl, M., Butt, H.-J. &Benfenati, F. Using the atomic force microscope to study the interaction between two solid supported lipid bilayers and the influence of synapsin I. Biophys. J. 87, 2446-2455 (2004)
    • (2004) Biophys. J , vol.87 , pp. 2446-2455
    • Pera, I.1    Stark, R.2    Kappl, M.3    Butt, H.-J.4    Benfenati, F.5
  • 30
    • 78049345303 scopus 로고    scopus 로고
    • Interaction of synaptotagmin with lipid bilayers, analyzed by single-molecule force spectroscopy
    • Takahashi, H., Shahin, V., Henderson, R. M., Takeyasu, K. &Edwardson, J. M. Interaction of synaptotagmin with lipid bilayers, analyzed by single-molecule force spectroscopy. Biophys. J. 99, 2550-2558 (2010)
    • (2010) Biophys. J. , vol.99 , pp. 2550-2558
    • Takahashi, H.1    Shahin, V.2    Henderson, R.M.3    Takeyasu, K.4    Edwardson, J.M.5
  • 31
    • 0032568662 scopus 로고    scopus 로고
    • C2-domains, Structure and Function of a Universal Ca2-binding Domain
    • Rizo, J. &Sudhof, T. C. C2-domains, Structure and Function of a Universal Ca2-binding Domain. J. Biol. Chem. 273, 15879-15882 (1998)
    • (1998) J. Biol. Chem , vol.273 , pp. 15879-15882
    • Rizo, J.1    Sudhof, T.C.2
  • 32
    • 46449135255 scopus 로고    scopus 로고
    • The hydrophobic insertion mechanism of membrane curvature generation by proteins
    • Campelo, F., McMahon, H. T. &Kozlov, M. M. The hydrophobic insertion mechanism of membrane curvature generation by proteins. Biophys. J. 95, 2325-2339 (2008)
    • (2008) Biophys. J , vol.95 , pp. 2325-2339
    • Campelo, F.1    McMahon, H.T.2    Kozlov, M.M.3
  • 33
    • 0036158070 scopus 로고    scopus 로고
    • Membrane fusion: Stalk model revisited
    • Markin, V. S. &Albanesi, J. P. Membrane fusion: stalk model revisited. Biophys. J. 82, 693-712 (2002)
    • (2002) Biophys. J , vol.82 , pp. 693-712
    • Markin, V.S.1    Albanesi, J.P.2
  • 34
    • 79955112041 scopus 로고    scopus 로고
    • Doc2 supports spontaneous synaptic transmission by a Ca(2)-independent mechanism
    • Pang, Z. P. et al. Doc2 supports spontaneous synaptic transmission by a Ca(2)-independent mechanism. Neuron 70, 244-251 (2011)
    • (2011) Neuron , vol.70 , pp. 244-251
    • Pang, Z.P.1
  • 35
    • 0030932857 scopus 로고    scopus 로고
    • DOC2 proteins in rat brain: Complementary distribution and proposed function as vesicular adapter proteins in early stages of secretion
    • Verhage, M. et al. DOC2 proteins in rat brain: complementary distribution and proposed function as vesicular adapter proteins in early stages of secretion. Neuron 18, 453-461 (1997)
    • (1997) Neuron , vol.18 , pp. 453-461
    • Verhage, M.1
  • 36
    • 0030959242 scopus 로고    scopus 로고
    • Physical and functional interactions of Doc2 and Munc13 in Ca2-dependent exocytotic machinery
    • Orita, S. et al. Physical and functional interactions of Doc2 and Munc13 in Ca2-dependent exocytotic machinery. J. Biol. Chem. 272, 16081-16084 (1997)
    • (1997) J. Biol. Chem , vol.272 , pp. 16081-16084
    • Orita, S.1
  • 37
    • 84872008490 scopus 로고    scopus 로고
    • Studying calciumtriggered vesicle fusion in a single vesicle-vesicle content and lipid-mixing system
    • Kyoung, M., Zhang, Y., Diao, J., Chu, S. &Brunger, A. T. Studying calciumtriggered vesicle fusion in a single vesicle-vesicle content and lipid-mixing system. Nat. Protoc. 8, 1-16 (2013)
    • (2013) Nat. Protoc , vol.8 , pp. 1-16
    • Kyoung, M.1    Zhang, Y.2    Diao, J.3    Chu, S.4    Brunger, A.T.5
  • 38
    • 28044460304 scopus 로고    scopus 로고
    • Neuronal activation by GPI-linked neuroligin-1 displayed in synthetic lipid bilayer membranes
    • Baksh, M. M. et al. Neuronal activation by GPI-linked neuroligin-1 displayed in synthetic lipid bilayer membranes. Langmuir 21, 10693-10698 (2005)
    • (2005) Langmuir , vol.21 , pp. 10693-10698
    • Baksh, M.M.1
  • 39
    • 2542453015 scopus 로고    scopus 로고
    • Ca 2-induced recruitment of the secretory vesicle protein DOC2B to the target membrane
    • Groffen, A. J. A. et al. Ca(2)-induced recruitment of the secretory vesicle protein DOC2B to the target membrane. J. Biol. Chem. 279, 23740-23747 (2004)
    • (2004) J. Biol. Chem , vol.279 , pp. 23740-23747
    • Groffen, A.J.A.1
  • 40
    • 77954586689 scopus 로고    scopus 로고
    • Combining optical tweezers, single-molecule fluorescence microscopy, and microfluidics for studies of DNA-protein interactions
    • Gross, P., Farge, G., Peterman, E. J. G. &Wuite, G. J. L. Combining optical tweezers, single-molecule fluorescence microscopy, and microfluidics for studies of DNA-protein interactions. Methods Enzymol. 475, 427-453 (2010)
    • (2010) Methods Enzymol , vol.475 , pp. 427-453
    • Gross, P.1    Farge, G.2    Peterman, E.J.G.3    Wuite, G.J.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.