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

Witkowska, A.; Heinz, L. P.; Grubmüller, H.; Jahn, R.

doi:10.1038/s41467-021-23722-8

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

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

MPS-Authors

/persons/resource/persons205206

Witkowska, A.
Laboratory of Neurobiology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons220629

Heinz, L. P.
Department of Theoretical and Computational Biophysics, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons15155

Grubmüller, H.
Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15266

Jahn, R.
Laboratory of Neurobiology, Max Planck Institute for Biophysical Chemistry, Max Planck Society;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

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.

Cite as: https://hdl.handle.net/21.11116/0000-0008-AB5D-0

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.