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The role of MscL amphipathic N terminus indicates a blueprint for bilayer-mediated gating of mechanosensitive channels

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Listed:
  • Navid Bavi

    (Victor Chang Cardiac Research Institute
    St Vincent’s Clinical School, Faculty of Medicine, University of New South Wales)

  • D. Marien Cortes

    (Institute for Biophysical Dynamics, University of Chicago
    Present address: Department of Cell Physiology, Texas Tech University Health Sciences Center, Lubbock, Texas 79430, USA)

  • Charles D. Cox

    (Victor Chang Cardiac Research Institute
    St Vincent’s Clinical School, Faculty of Medicine, University of New South Wales)

  • Paul R. Rohde

    (Victor Chang Cardiac Research Institute)

  • Weihong Liu

    (University of Western Australia
    Present address: Marion Domain Medical and Dental Centre, Oaklands Park, South Australia 5046, Australia)

  • Joachim W. Deitmer

    (FB Biologie, University of Kaiserslautern)

  • Omid Bavi

    (Victor Chang Cardiac Research Institute
    Institute for Nanoscience and Nanotechnology, Sharif University of Technology)

  • Pavel Strop

    (Howard Hughes Medical Institute, California Institute of Technology
    Present address: Pfizer Inc., New York, New York 10017, USA)

  • Adam P. Hill

    (Victor Chang Cardiac Research Institute
    St Vincent’s Clinical School, Faculty of Medicine, University of New South Wales)

  • Douglas Rees

    (Howard Hughes Medical Institute, California Institute of Technology)

  • Ben Corry

    (Research School of Biology, The Australian National University)

  • Eduardo Perozo

    (Institute for Biophysical Dynamics, University of Chicago)

  • Boris Martinac

    (Victor Chang Cardiac Research Institute
    St Vincent’s Clinical School, Faculty of Medicine, University of New South Wales)

Abstract

The bacterial mechanosensitive channel MscL gates in response to membrane tension as a result of mechanical force transmitted directly to the channel from the lipid bilayer. MscL represents an excellent model system to study the basic biophysical principles of mechanosensory transduction. However, understanding of the essential structural components that transduce bilayer tension into channel gating remains incomplete. Here using multiple experimental and computational approaches, we demonstrate that the amphipathic N-terminal helix of MscL acts as a crucial structural element during tension-induced gating, both stabilizing the closed state and coupling the channel to the membrane. We propose that this may also represent a common principle in the gating cycle of unrelated mechanosensitive ion channels, allowing the coupling of channel conformation to membrane dynamics.

Suggested Citation

  • Navid Bavi & D. Marien Cortes & Charles D. Cox & Paul R. Rohde & Weihong Liu & Joachim W. Deitmer & Omid Bavi & Pavel Strop & Adam P. Hill & Douglas Rees & Ben Corry & Eduardo Perozo & Boris Martinac, 2016. "The role of MscL amphipathic N terminus indicates a blueprint for bilayer-mediated gating of mechanosensitive channels," Nature Communications, Nature, vol. 7(1), pages 1-13, September.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11984
    DOI: 10.1038/ncomms11984
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    Cited by:

    1. Jonathan Mount & Grigory Maksaev & Brock T. Summers & James A. J. Fitzpatrick & Peng Yuan, 2022. "Structural basis for mechanotransduction in a potassium-dependent mechanosensitive ion channel," Nature Communications, Nature, vol. 13(1), pages 1-11, December.

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