| First Author | Ge J | Year | 2015 |
| Journal | Nature | Volume | 527 |
| Issue | 7576 | Pages | 64-9 |
| PubMed ID | 26390154 | Mgi Jnum | J:247395 |
| Mgi Id | MGI:5925849 | Doi | 10.1038/nature15247 |
| Citation | Ge J, et al. (2015) Architecture of the mammalian mechanosensitive Piezo1 channel. Nature 527(7576):64-9 |
| abstractText | 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 A. 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. |
