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  Tight docking of membranes before fusion represents a novel, metastable state with unique properties

Witkowska, A., Heinz, L. P., Grubmüller, H., & Jahn, R. (2021). Tight docking of membranes before fusion represents a novel, metastable state with unique properties. Nature Communications, 12: 3606. doi:10.1038/s41467-021-23722-8.

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 Creators:
Witkowska, A.1, Author              
Heinz, L. P.2, Author              
Grubmüller, H.3, Author              
Jahn, R.4, Author              
Affiliations:
1Laboratory of Neurobiology, MPI for Biophysical Chemistry, Max Planck Society, ou_3049887              
2Department of Theoretical and Computational Biophysics, MPI for Biophysical Chemistry, Max Planck Society, ou_578631              
3Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society, ou_578631              
4Laboratory of Neurobiology, Max Planck Institute for Biophysical Chemistry, Max Planck Society, ou_3049887              

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Free keywords: Membrane biophysics; Membrane structure and assembly
 Abstract: Membrane fusion is fundamental to biological processes as diverse as membrane trafficking or viral infection. Proteins catalyzing membrane fusion need to overcome energy barriers to induce intermediate steps in which the integrity of bilayers is lost. Here, we investigate the structural features of tightly docked intermediates preceding hemifusion. Using lipid vesicles in which progression to hemifusion is arrested, we show that the metastable intermediate does not require but is enhanced by divalent cations and is characterized by the absence of proteins and local membrane thickening. Molecular dynamics simulations reveal that thickening is due to profound lipid rearrangements induced by dehydration of the membrane surface.

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Language(s): eng - English
 Dates: 2021-062021-06-14
 Publication Status: Published online
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 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41467-021-23722-8
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Title: Nature Communications
Source Genre: Journal
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Pages: 7 Volume / Issue: 12 Sequence Number: 3606 Start / End Page: - Identifier: -