Structure and mechanogating mechanism of the Piezo1 channel

Qiancheng Zhao, Heng Zhou, Shaopeng Chi, Yanfeng Wang, Jianhua Wang, Jie Geng, Kun Wu, Wenhao Liu, Tingxin Zhang, Meng-Qiu Dong, Jiawei Wang, Xueming Li () and Bailong Xiao ()
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Qiancheng Zhao: School of Pharmaceutical Sciences or Life Sciences, Tsinghua University
Heng Zhou: School of Pharmaceutical Sciences or Life Sciences, Tsinghua University
Shaopeng Chi: School of Pharmaceutical Sciences or Life Sciences, Tsinghua University
Yanfeng Wang: School of Pharmaceutical Sciences or Life Sciences, Tsinghua University
Jianhua Wang: National Institute of Biological Sciences
Jie Geng: School of Pharmaceutical Sciences or Life Sciences, Tsinghua University
Kun Wu: School of Pharmaceutical Sciences or Life Sciences, Tsinghua University
Wenhao Liu: School of Pharmaceutical Sciences or Life Sciences, Tsinghua University
Tingxin Zhang: School of Pharmaceutical Sciences or Life Sciences, Tsinghua University
Meng-Qiu Dong: National Institute of Biological Sciences
Jiawei Wang: School of Pharmaceutical Sciences or Life Sciences, Tsinghua University
Xueming Li: School of Pharmaceutical Sciences or Life Sciences, Tsinghua University
Bailong Xiao: School of Pharmaceutical Sciences or Life Sciences, Tsinghua University

Nature, 2018, vol. 554, issue 7693, 487-492

Abstract: Abstract The mechanosensitive Piezo channels function as key eukaryotic mechanotransducers. However, their structures and mechanogating mechanisms remain unknown. Here we determine the three-bladed, propeller-like electron cryo-microscopy structure of mouse Piezo1 and functionally reveal its mechanotransduction components. Despite the lack of sequence repetition, we identify nine repetitive units consisting of four transmembrane helices each—which we term transmembrane helical units (THUs)—which assemble into a highly curved blade-like structure. The last transmembrane helix encloses a hydrophobic pore, followed by three intracellular fenestration sites and side portals that contain pore-property-determining residues. The central region forms a 90?Å-long intracellular beam-like structure, which undergoes a lever-like motion to connect THUs to the pore via the interfaces of the C-terminal domain, the anchor-resembling domain and the outer helix. Deleting extracellular loops in the distal THUs or mutating single residues in the beam impairs the mechanical activation of Piezo1. Overall, Piezo1 possesses a unique 38-transmembrane-helix topology and designated mechanotransduction components, which enable a lever-like mechanogating mechanism.

Date: 2018
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DOI: 10.1038/nature25743

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