Journal
FEBS JOURNAL
Volume 286, Issue 13, Pages 2461-2470Publisher
WILEY
DOI: 10.1111/febs.14711
Keywords
cryo-EM structure; ion permeation; lever; mechanogating; mechanotransduction; Piezo channel; pore
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Funding
- National Key R&D Program of China [2016YFA0500402, 31630090, 31825014, 2015CB910102, 31422027, 31371118]
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The evolutionarily conserved Piezo proteins, including Piezo1 and Piezo2, constitute a bona fide class of mechanosensitive (MS) cation channels, which play critical roles in various mammalian physiologies, including sensation of touch, proprioception and regulation of vascular development, and blood pressure. Furthermore, mutations in Piezos have been linked to various human genetic diseases, validating their potential as therapeutic targets. Thus, it is pivotal to understand how Piezo channels effectively convert mechanical force into selective cation permeation, and therefore precisely control the various mechanotransduction processes. On the basis of our recently determined cryoelectron microscopy structures of the full-length 2547-residue mouse Piezo1, structure-guided mutagenesis, and electrophysiological and pharmacological characterizations, here we focus on reviewing the key structural features and functional components that enable Piezo1 to employ a lever-like mechanogating mechanism to function as a sophisticated mechanotransduction channel.
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