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  Arrest of trans-SNARE zippering uncovers loosely and tightly docked intermediates in membrane fusion.

Yavuz, H., Kattan, I., Hernandez, J. M., Hofnagel, O., Witkowska, A., Raunser, S., et al. (2018). Arrest of trans-SNARE zippering uncovers loosely and tightly docked intermediates in membrane fusion. Journal of Biological Chemistry, 293(22), 8645-8655. doi:10.1074/jbc.RA118.003313.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0001-2E86-5 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-C243-6
Genre: Journal Article

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 Creators:
Yavuz, H.1, Author              
Kattan, I.1, Author              
Hernandez, J. M., Author
Hofnagel, O., Author
Witkowska, A.1, Author              
Raunser, S., Author
Walla, P. J., Author
Jahn, R.1, Author              
Affiliations:
1Department of Neurobiology, MPI for Biophysical Chemistry, Max Planck Society, ou_578595              

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Free keywords: SNARE proteins; docking; exocytosis; membrane fusion; membrane reconstitution; soluble NSF attachment protein receptor (SNARE)
 Abstract: Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins mediate intracellular membrane fusion in the secretory pathway. They contain conserved regions, termed SNARE motifs, that assemble between opposing membranes directionally from their N-termini to their membrane-proximal C-termini in a highly exergonic reaction. However, how this energy is utilized to overcome the energy barriers along the fusion pathway is still under debate. Here we have used mutants of the SNARE synaptobrevin to arrest trans-SNARE zippering at defined stages. We have uncovered two distinct vesicle docking intermediates, where the membranes are loosely and tightly connected, respectively. The tightly connected state is irreversible and independent of maintaining assembled SNARE complexes. Together, our results shed new light on the intermediate stages along the pathway of membrane fusion.

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Language(s): eng - English
 Dates: 2018-04-172018-06-01
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1074/jbc.RA118.003313
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 293 (22) Sequence Number: - Start / End Page: 8645 - 8655 Identifier: -