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

Charles D. Cox, Chilman Bae, Lynn Ziegler, Silas Hartley, Vesna Nikolova-Krstevski, Paul R. Rohde, Chai-Ann Ng, Frederick Sachs, Philip A. Gottlieb () and Boris Martinac ()
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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
Frederick Sachs: State University of New York at Buffalo
Philip A. Gottlieb: State University of New York at Buffalo
Boris Martinac: Victor Chang Cardiac Research Institute

Nature Communications, 2016, vol. 7, issue 1, 1-13

Abstract: 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.

Date: 2016
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DOI: 10.1038/ncomms10366

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