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Journal Article

Membrane fusion intermediates via directional and full assembly of the SNARE complex.

MPS-Authors
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Hernandez,  J. M.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Stein,  A.
Research Group of Membrane Protein Biochemistry, MPI for Biophysical Chemistry, Max Planck Society;

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Riedel,  D.
Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society;

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Cypionka,  A.
Research Group of Biomolecular Spectroscopy and Single-Molecule Detection, MPI for biophysical chemistry, Max Planck Society;

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Farsi,  Z.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Walla,  P. J.
Research Group of Biomolecular Spectroscopy and Single-Molecule Detection, MPI for biophysical chemistry, Max Planck Society;

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Jahn,  R.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

Fulltext (public)

1479531.pdf
(Publisher version), 4MB

Supplementary Material (public)

1479531_SM.pdf
(Supplementary material), 987KB

Citation

Hernandez, J. M., Stein, A., Behrmann, E., Riedel, D., Cypionka, A., Farsi, Z., et al. (2012). Membrane fusion intermediates via directional and full assembly of the SNARE complex. Science, 336(6088), 1581-1584. doi:10.1126/science.1221976.


Cite as: http://hdl.handle.net/11858/00-001M-0000-000F-A228-9
Abstract
Cellular membrane fusion is thought to proceed through intermediates including docking of apposed lipid bilayers, merging of proximal leaflets to form a hemifusion diaphragm, and fusion pore opening. A membrane-bridging four-helix complex of soluble N-ethylmaleimide–sensitive factor attachment protein receptors (SNAREs) mediates fusion. However, how assembly of the SNARE complex generates docking and other fusion intermediates is unknown. Using a cell-free reaction, we identified intermediates visually and then arrested the SNARE fusion machinery when fusion was about to begin. Partial and directional assembly of SNAREs tightly docked bilayers, but efficient fusion and an extended form of hemifusion required assembly beyond the core complex to the membrane-connecting linkers. We propose that straining of lipids at the edges of an extended docking zone initiates fusion.