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Piezo1 ion channel pore properties are dictated by C-terminal region

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  • Bertrand Coste

    (Aix Marseille Université, CNRS, CRN2M-UMR7286
    Howard Hughes Medical Institute, Molecular and Cellular Neuroscience, The Scripps Research Institute)

  • Swetha E. Murthy

    (Howard Hughes Medical Institute, Molecular and Cellular Neuroscience, The Scripps Research Institute)

  • Jayanti Mathur

    (Genomics Institute of the Novartis Research Foundation)

  • Manuela Schmidt

    (Howard Hughes Medical Institute, Molecular and Cellular Neuroscience, The Scripps Research Institute
    Present Address: Somatosensory Signaling Group; Max Planck Institute of Experimental Medicine, 37075 Goettingen, Germany.)

  • Yasmine Mechioukhi

    (Aix Marseille Université, CNRS, CRN2M-UMR7286)

  • Patrick Delmas

    (Aix Marseille Université, CNRS, CRN2M-UMR7286)

  • Ardem Patapoutian

    (Howard Hughes Medical Institute, Molecular and Cellular Neuroscience, The Scripps Research Institute
    Genomics Institute of the Novartis Research Foundation)

Abstract

Piezo1 and Piezo2 encode mechanically activated cation channels that function as mechanotransducers involved in vascular system development and touch sensing, respectively. Structural features of Piezos remain unknown. Mouse Piezo1 is bioinformatically predicted to have 30–40 transmembrane (TM) domains. Here, we find that nine of the putative inter-transmembrane regions are accessible from the extracellular side. We use chimeras between mPiezo1 and dPiezo to show that ion-permeation properties are conferred by C-terminal region. We further identify a glutamate residue within a conserved region adjacent to the last two putative TM domains of the protein, that when mutated, affects unitary conductance and ion selectivity, and modulates pore block. We propose that this amino acid is either in the pore or closely associates with the pore. Our results describe important structural motifs of this channel family and lay the groundwork for a mechanistic understanding of how Piezos are mechanically gated and conduct ions.

Suggested Citation

  • Bertrand Coste & Swetha E. Murthy & Jayanti Mathur & Manuela Schmidt & Yasmine Mechioukhi & Patrick Delmas & Ardem Patapoutian, 2015. "Piezo1 ion channel pore properties are dictated by C-terminal region," Nature Communications, Nature, vol. 6(1), pages 1-11, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8223
    DOI: 10.1038/ncomms8223
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    Cited by:

    1. Nathalia G. Amado & Elena D. Nosyreva & David Thompson & Thomas J. Egeland & Osita W. Ogujiofor & Michelle Yang & Alexandria N. Fusco & Niccolo Passoni & Jeremy Mathews & Brandi Cantarel & Linda A. Ba, 2024. "PIEZO1 loss-of-function compound heterozygous mutations in the rare congenital human disorder Prune Belly Syndrome," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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