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Structure and mechanogating of the mammalian tactile channel PIEZO2

Author

Listed:
  • Li Wang

    (Tsinghua University)

  • Heng Zhou

    (Tsinghua University)

  • Mingmin Zhang

    (Tsinghua University
    Tsinghua University)

  • Wenhao Liu

    (Tsinghua University
    Tsinghua University)

  • Tuan Deng

    (Tsinghua University)

  • Qiancheng Zhao

    (Tsinghua University)

  • Yiran Li

    (Tsinghua University)

  • Jianlin Lei

    (Tsinghua University)

  • Xueming Li

    (Tsinghua University)

  • Bailong Xiao

    (Tsinghua University
    Tsinghua University)

Abstract

PIEZO2 is a mechanosensitive cation channel that has a key role in sensing touch, tactile pain, breathing and blood pressure. Here we describe the cryo-electron microscopy structure of mouse PIEZO2, which is a three-bladed, propeller-like trimer that comprises 114 transmembrane helices (38 per protomer). Transmembrane helices 1–36 (TM1–36) are folded into nine tandem units of four transmembrane helices each to form the unusual non-planar blades. The three blades are collectively curved into a nano-dome of 28-nm diameter and 10-nm depth, with an extracellular cap-like structure embedded in the centre and a 9-nm-long intracellular beam connecting to the central pore. TM38 and the C-terminal domain are surrounded by the anchor domain and TM37, and enclose the central pore with both transmembrane and cytoplasmic constriction sites. Structural comparison between PIEZO2 and its homologue PIEZO1 reveals that the transmembrane constriction site might act as a transmembrane gate that is controlled by the cap domain. Together, our studies provide insights into the structure and mechanogating mechanism of Piezo channels.

Suggested Citation

  • Li Wang & Heng Zhou & Mingmin Zhang & Wenhao Liu & Tuan Deng & Qiancheng Zhao & Yiran Li & Jianlin Lei & Xueming Li & Bailong Xiao, 2019. "Structure and mechanogating of the mammalian tactile channel PIEZO2," Nature, Nature, vol. 573(7773), pages 225-229, September.
    • Handle: RePEc:nat:nature:v:573:y:2019:i:7773:d:10.1038_s41586-019-1505-8
    DOI: 10.1038/s41586-019-1505-8
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    Cited by:

    1. Sijia Xu & Jie-Xiang Yu & Hongshuang Guo & Shu Tian & You Long & Jing Yang & Lei Zhang, 2023. "Force-induced ion generation in zwitterionic hydrogels for a sensitive silent-speech sensor," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    2. Luis O. Romero & Rebeca Caires & A. Kaitlyn Victor & Juanma Ramirez & Francisco J. Sierra-Valdez & Patrick Walsh & Vincent Truong & Jungsoo Lee & Ugo Mayor & Lawrence T. Reiter & Valeria Vásquez & Jul, 2023. "Linoleic acid improves PIEZO2 dysfunction in a mouse model of Angelman Syndrome," Nature Communications, Nature, vol. 14(1), pages 1-20, December.
    3. Francisco Andrés Peralta & Mélaine Balcon & Adeline Martz & Deniza Biljali & Federico Cevoli & Benoit Arnould & Antoine Taly & Thierry Chataigneau & Thomas Grutter, 2023. "Optical control of PIEZO1 channels," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    4. 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.
    5. 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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