ArticleNature chemical biology2026
A two-step clockwork mechanism opens a proteo-lipidic pore in PIEZO2.
Article in Nature chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Docking-score landscapes shape active-learning performance across Vina, Glide, and SILCS.Journal of computer-aided molecular design · 2026Article
- Piezo2 tension sensitivity and its modulation by alternative splicing.Cell reports · 2026Article
- Challenges of conventional iterative all-atom and coarse-grained multiscale molecular dynamics.Scientific reports · 2026Article
- CholBindNet as an interpretable neural network for cholesterol-binding site classification.Communications chemistry · 2026Article
- Yoda molecules agonize PIEZO2.bioRxiv : the preprint server for biology · 2026Article
- Piezo2-Initiated Ultrafast Signaling and Its Acquired Channelopathy in Light of Quantum Gravity Theory.International journal of molecular sciences · 2026Review
- Piezo2 tension sensitivity and its modulation by alternative splicing.bioRxiv : the preprint server for biology · 2026Article
- CholBindNet: Interpretable Neural Networks for Cholesterol Binding Site Prediction.bioRxiv : the preprint server for biology · 2026Article
- Optimizing a coarse-grained model for large-scale membrane protein simulation.Biophysical reports · 2025Article
- Delayed-Onset Muscle Soreness Begins with a Transient Neural Switch.International journal of molecular sciences · 2025Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Mechanosensitive PIEZO channels are thought to open via tension-induced flattening of peripheral transmembrane arm domains, yet the structural basis of this activation remains unclear. Here, by leveraging hybrid-resolution molecular dynamics simulations, we uncover how large-scale PIEZO2 arm movements funnel into subtle gating motions in the central pore under physiological tension. Arm flattening correlates with anticlockwise rotation of the pore relative to the arms and with clockwise twisting of inner pore helices. These clockwork motions open the pore in a two-step fashion, yielding a fully conducting state and a stable subconducting state populated at a low tension, which was detected electrophysiologically. The fully open PIEZO2 pore is walled by both lipids and amino acids and recapitulates minimal pore size, conductance, ion selectivity and outward rectification of chloride currents measured electrophysiologically. These findings provide structural insights into PIEZO2 gating and demonstrate hybrid-resolution molecular dynamics as a powerful approach to study large-scale membrane protein dynamics and guide drug discovery.
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