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- W4221109990 abstract "Flycatcher1 (FLYC1), a MscS homolog, has recently been identified as a candidate mechanosensitive (MS) ion channel involved in Venus flytrap prey recognition. FLYC1 is a larger protein and its sequence diverges from previously studied MscS homologs, suggesting it has unique structural features that contribute to its function. Here, we characterize FLYC1 by cryo-electron microscopy, molecular dynamics simulations, and electrophysiology. Akin to bacterial MscS and plant MSL1 channels, we find that FLYC1 central core includes side portals in the cytoplasmic cage that regulate ion preference and conduction, by identifying critical residues that modulate channel conductance. Topologically unique cytoplasmic flanking regions can adopt 'up' or 'down' conformations, making the channel asymmetric. Disruption of an up conformation-specific interaction severely delays channel deactivation by 40-fold likely due to stabilization of the channel open state. Our results illustrate novel structural features and likely conformational transitions that regulate mechano-gating of FLYC1." @default.
- W4221109990 created "2022-04-03" @default.
- W4221109990 creator A5007007378 @default.
- W4221109990 creator A5020755193 @default.
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- W4221109990 creator A5066449841 @default.
- W4221109990 creator A5067790213 @default.
- W4221109990 creator A5073726872 @default.
- W4221109990 creator A5077248191 @default.
- W4221109990 creator A5079371611 @default.
- W4221109990 date "2022-02-14" @default.
- W4221109990 modified "2023-10-13" @default.
- W4221109990 title "Structural insights into the Venus flytrap mechanosensitive ion channel Flycatcher1" @default.
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