Mechanosensitive cation channels convert external mechanical stimuli into various biological actions, including touch, hearing, balance and cardiovascular regulation. The eukaryotic Piezo proteins are mechanotransduction channels, although their structure and gating mechanisms are not well elucidated. In related papers in this issue of Nature, two groups report cryo-electron microscopy structures of the full-length mouse Piezo1 and reveal three flexible propeller blades. Each blade is made up of at least 26 helices, forming a series of helical bundles, which adopt a curved transmembrane region. A kinked beam and anchor domain link these Piezo repeats to the pore, giving clues as to how the channel responds to membrane tension and mechanical force.
- Structure of the mechanically activated ion channel Piezo1 (Article p481, doi: 10.1038/nature25453)
- Structure and mechanogating mechanism of the Piezo1 channel (Article p487, doi: 10.1038/nature25743)
- Force-activated ion channels in close-up (News & Views p469, doi: 10.1038/d41586-018-01631-z)
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