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Structure and mechanogating mechanism of the Piezo1 channel.

Zhao, Qiancheng; Zhou, Heng; Chi, Shaopeng; Wang, Yanfeng; Wang, Jianhua; Geng, Jie; Wu, Kun; Liu, Wenhao; Zhang, Tingxin; Dong, Meng-Qiu; Wang, Jiawei; Li, Xueming; Xiao, Bailong.
Nature; 554(7693): 487-492, 2018 02 22.
Artigo em Inglês | MEDLINE | ID: mdl-29469092
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.
Selo DaSilva