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

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.

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Hernandez, J. M.1, Author           
Stein, A.2, Author           
Behrmann, E., Author
Riedel, D.3, Author           
Cypionka, A.4, Author           
Farsi, Z.1, Author           
Walla, P. J.4, Author           
Raunser, S., Author
Jahn, R.1, Author           
Affiliations:
1Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              
2Research Group of Membrane Protein Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_2149675              
3Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578615              
4Research Group of Biomolecular Spectroscopy and Single-Molecule Detection, MPI for biophysical chemistry, Max Planck Society, ou_578565              

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 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.

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Language(s): eng - English
 Dates: 2012-05-312012-06-22
 Publication Status: Issued
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 Rev. Type: Peer
 Identifiers: DOI: 10.1126/science.1221976
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Title: Science
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Pages: - Volume / Issue: 336 (6088) Sequence Number: - Start / End Page: 1581 - 1584 Identifier: -