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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), 1581-4. doi:10.1126/science.1221976.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0028-63CE-A Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0028-63CF-8
Genre: Journal Article

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Hernandez, J. M., Author
Stein, A., Author
Behrmann, E.1, Author
Riedel, D., Author
Cypionka, A., Author
Farsi, Z., Author
Walla, P. J., Author
Raunser, S., Author
Jahn, R., Author
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1External Organizations, ou_persistent22              

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Free keywords: Animals Lipid Bilayers/chemistry/*metabolism *Liposomes/chemistry/metabolism *Membrane Fusion Protein Binding Protein Conformation Rats SNARE Proteins/chemistry/*metabolism Vesicle-Associated Membrane Protein 2/metabolism
 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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 Dates: 2012
 Publication Status: Issued
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 Identifiers: Other: 22653732
DOI: 10.1126/science.1221976
ISSN: 1095-9203 (Electronic)
ISSN: 0036-8075 (Linking)
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Title: Science
  Alternative Title : Science
Source Genre: Journal
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Pages: - Volume / Issue: 336 (6088) Sequence Number: - Start / End Page: 1581 - 4 Identifier: -