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Removal of the mechanoprotective influence of the cytoskeleton reveals PIEZO1 is gated by bilayer tension

Author

Listed:
  • Charles D. Cox

    (Victor Chang Cardiac Research Institute)

  • Chilman Bae

    (State University of New York at Buffalo)

  • Lynn Ziegler

    (State University of New York at Buffalo)

  • Silas Hartley

    (State University of New York at Buffalo)

  • Vesna Nikolova-Krstevski

    (Victor Chang Cardiac Research Institute)

  • Paul R. Rohde

    (Victor Chang Cardiac Research Institute)

  • Chai-Ann Ng

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

  • Frederick Sachs

    (State University of New York at Buffalo
    The Centre for Single Molecule Biophysics, State University of New York at Buffalo)

  • Philip A. Gottlieb

    (State University of New York at Buffalo
    The Centre for Single Molecule Biophysics, State University of New York at Buffalo)

  • Boris Martinac

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

Abstract

Mechanosensitive ion channels are force-transducing enzymes that couple mechanical stimuli to ion flux. Understanding the gating mechanism of mechanosensitive channels is challenging because the stimulus seen by the channel reflects forces shared between the membrane, cytoskeleton and extracellular matrix. Here we examine whether the mechanosensitive channel PIEZO1 is activated by force-transmission through the bilayer. To achieve this, we generate HEK293 cell membrane blebs largely free of cytoskeleton. Using the bacterial channel MscL, we calibrate the bilayer tension demonstrating that activation of MscL in blebs is identical to that in reconstituted bilayers. Utilizing a novel PIEZO1–GFP fusion, we then show PIEZO1 is activated by bilayer tension in bleb membranes, gating at lower pressures indicative of removal of the cortical cytoskeleton and the mechanoprotection it provides. Thus, PIEZO1 channels must sense force directly transmitted through the bilayer.

Suggested Citation

  • Charles D. Cox & Chilman Bae & Lynn Ziegler & Silas Hartley & Vesna Nikolova-Krstevski & Paul R. Rohde & Chai-Ann Ng & Frederick Sachs & Philip A. Gottlieb & Boris Martinac, 2016. "Removal of the mechanoprotective influence of the cytoskeleton reveals PIEZO1 is gated by bilayer tension," Nature Communications, Nature, vol. 7(1), pages 1-13, April.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms10366
    DOI: 10.1038/ncomms10366
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    Cited by:

    1. Shilong Yang & Xinwen Miao & Steven Arnold & Boxuan Li & Alan T. Ly & Huan Wang & Matthew Wang & Xiangfu Guo & Medha M. Pathak & Wenting Zhao & Charles D. Cox & Zheng Shi, 2022. "Membrane curvature governs the distribution of Piezo1 in live cells," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    2. Martina Nicoletti & Letizia Chiodo & Alessandro Loppini, 2021. "Biophysics and Modeling of Mechanotransduction in Neurons: A Review," Mathematics, MDPI, vol. 9(4), pages 1-32, February.
    3. Mingfeng Zhang & Yuanyue Shan & Charles D. Cox & Duanqing Pei, 2023. "A mechanical-coupling mechanism in OSCA/TMEM63 channel mechanosensitivity," Nature Communications, Nature, vol. 14(1), pages 1-9, December.
    4. Clement Verkest & Irina Schaefer & Timo A. Nees & Na Wang & Juri M. Jegelka & Francisco J. Taberner & Stefan G. Lechner, 2022. "Intrinsically disordered intracellular domains control key features of the mechanically-gated ion channel PIEZO2," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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