title: Architecture of the mammalian mechanosensitive Piezo1 channel.
abstract: 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.
authors.affiliation: Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences or Medicine, Tsinghua University, Beijing 100084, China.|Ministry of Education, Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
authors.forename: Jingpeng
authors.initials: J
authors.lastname: Ge
authors.affiliation: Ministry of Education, Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
authors.forename: Wanqiu
authors.initials: W
authors.lastname: Li
authors.affiliation: Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences or Medicine, Tsinghua University, Beijing 100084, China.|Department of Pharmacology and Pharmaceutical Sciences, School of Medicine, Tsinghua University, Beijing 100084, China.
authors.forename: Qiancheng
authors.initials: Q
authors.lastname: Zhao
authors.affiliation: Ministry of Education, Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
authors.forename: Ningning
authors.initials: N
authors.lastname: Li
authors.affiliation: Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences or Medicine, Tsinghua University, Beijing 100084, China.|Ministry of Education, Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
authors.forename: Maofei
authors.initials: M
authors.lastname: Chen
authors.affiliation: Department of Pharmacology and Pharmaceutical Sciences, School of Medicine, Tsinghua University, Beijing 100084, China.
authors.forename: Peng
authors.initials: P
authors.lastname: Zhi
authors.affiliation: Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences or Medicine, Tsinghua University, Beijing 100084, China.|Ministry of Education, Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
authors.forename: Ruochong
authors.initials: R
authors.lastname: Li
authors.affiliation: Ministry of Education, Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
authors.forename: Ning
authors.initials: N
authors.lastname: Gao
authors.affiliation: Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences or Medicine, Tsinghua University, Beijing 100084, China.|Department of Pharmacology and Pharmaceutical Sciences, School of Medicine, Tsinghua University, Beijing 100084, China.|IDG/McGovern Institute for Brain Research, Tsinghua University, Beijing 100084, China.
authors.forename: Bailong
authors.initials: B
authors.lastname: Xiao
authors.affiliation: Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences or Medicine, Tsinghua University, Beijing 100084, China.|Ministry of Education, Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
authors.forename: Maojun
authors.initials: M
authors.lastname: Yang
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D020285:Cryoelectron Microscopy; D004553:Electric Conductivity; D015640:Ion Channel Gating; D007473:Ion Channels / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure*; D051379:Mice; D008958:Models, Molecular; D018583:Pliability; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism
chemical_list: D007473:Ion Channels; C552920:Piezo1 protein, mouse; D021122:Protein Subunits