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

Author

Listed:
  • Agata Witkowska

    (Laboratory of Neurobiology, Max-Planck-Institute for Biophysical Chemistry
    Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP))

  • Leonard P. Heinz

    (Department of Theoretical and Computational Biophysics, Max-Planck-Institute for Biophysical Chemistry)

  • Helmut Grubmüller

    (Department of Theoretical and Computational Biophysics, Max-Planck-Institute for Biophysical Chemistry)

  • Reinhard Jahn

    (Laboratory of Neurobiology, Max-Planck-Institute for Biophysical Chemistry
    University of Göttingen)

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.

Suggested Citation

  • Agata Witkowska & Leonard P. Heinz & Helmut Grubmüller & Reinhard Jahn, 2021. "Tight docking of membranes before fusion represents a metastable state with unique properties," Nature Communications, Nature, vol. 12(1), pages 1-7, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-23722-8
    DOI: 10.1038/s41467-021-23722-8
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    Cited by:

    1. Vidya Mangala Prasad & Jelle S. Blijleven & Jolanda M. Smit & Kelly K. Lee, 2022. "Visualization of conformational changes and membrane remodeling leading to genome delivery by viral class-II fusion machinery," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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