Architecture of the mammalian mechanosensitive Piezo1 channel

• Autores: Jingpeng Ge, Wanqiu Li, Qiancheng Zhao, Ningning Li, Maofei Chen, Peng Zhi, Ruochong Li, Ning Gao, Bailong Xiao, Maojun Yang
• Localización: Nature: International weekly journal of science, ISSN 0028-0836, Vol. 527, Nº 7576, 2015, págs. 64-69
• Idioma: inglés
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• Resumen

  • Piezo proteins are evolutionarily conserved and functionally diverse mechanosensitive cation channels. However, the overall structural architecture and gating mechanisms of Piezo channels have remained unknown. Here we determine the cryo-electron microscopy structure of the full-length (2,547 amino acids) mouse Piezo1 (Piezo1) at a resolution of 4.8 Å. Piezo1 forms a trimeric propeller-like structure (about 900 kilodalton), with the extracellular domains resembling three distal blades and a central cap. The transmembrane region has 14 apparently resolved segments per subunit. These segments form three peripheral wings and a central pore module that encloses a potential ion-conducting pore. The rather flexible extracellular blade domains are connected to the central intracellular domain by three long beam-like structures. This trimeric architecture suggests that Piezo1 may use its peripheral regions as force sensors to gate the central ion-conducting pore.