ArticleeLife2025
Twist is the key to the gating of mechanosensitive ion channel NOMPC.
Article in eLife, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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Who cites it
3 citing papers in PubMed.
- Structural Remodeling of TCR-HLA-DQ8 Recognition by a β-Cell Stress-Associated C19S Insulin Neoepitope in Type 1 Diabetes.International journal of molecular sciences · 2026Article
- Lipid Regulation of Mechanosensitive Ion Channels.International journal of molecular sciences · 2026Review
- Article
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Authors and funding
2 authors.
Funding
Abstract
NOMPC, a tethered mechanosensitive ion channel belonging to the transient receptor potential (TRP) family, converts mechanical stimuli into ionic electric signals that excite neuronal cells (Yan et al., 2013). Previous investigations have demonstrated that a pushing force applied to the linker helix domain or the compression of NOMPC's ankyrin repeat (AR) domain can trigger channel opening (Wang et al., 2021). In this study, we explored the direct mechanical causes of NOMPC channel opening as well as the torsional properties of the AR domain, using all-atom molecular dynamics simulations. Our results indicate that a torque directed toward the extracellular side, exerted on the amphipathic TRP domain, is the primary factor driving channel opening. The coupling between compression and twisting of the AR domain ensures that both types of deformation can induce channel opening. Therefore, we propose a twist-to-open model, facilitated by the compression-twist coupling property of the AR domain, to provide further insight into the gating mechanism of the NOMPC channel.
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Registered trials
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