Structural insights into the Venus flytrap mechanosensitive ion channel Flycatcher1

Sebastian Jojoa-Cruz, Kei Saotome, Che Chun Alex Tsui, Wen-Hsin Lee, Mark S. P. Sansom, Swetha E. Murthy (), Ardem Patapoutian () and Andrew B. Ward ()
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Sebastian Jojoa-Cruz: Department of Integrative Structural and Computational Biology, Scripps Research
Kei Saotome: Department of Integrative Structural and Computational Biology, Scripps Research
Che Chun Alex Tsui: Department of Integrative Structural and Computational Biology, Scripps Research
Wen-Hsin Lee: Department of Integrative Structural and Computational Biology, Scripps Research
Mark S. P. Sansom: University of Oxford
Swetha E. Murthy: Howard Hughes Medical Institute, Department of Neuroscience, Dorris Neuroscience Center, Scripps Research
Ardem Patapoutian: Howard Hughes Medical Institute, Department of Neuroscience, Dorris Neuroscience Center, Scripps Research
Andrew B. Ward: Department of Integrative Structural and Computational Biology, Scripps Research

Nature Communications, 2022, vol. 13, issue 1, 1-11

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-022-28511-5

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