Structure and mechanogating of the mammalian tactile channel PIEZO2

Li Wang, Heng Zhou, Mingmin Zhang, Wenhao Liu, Tuan Deng, Qiancheng Zhao, Yiran Li, Jianlin Lei, Xueming Li () and Bailong Xiao ()
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Li Wang: Tsinghua University
Heng Zhou: Tsinghua University
Mingmin Zhang: Tsinghua University
Wenhao Liu: 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

Nature, 2019, vol. 573, issue 7773, 225-229

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41586-019-1505-8

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