ArticleCommunications biology2021
Mechanosensitive channel YnaI has lipid-bound extended sensor paddles.
Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- A brief guideline for the studies of structure-function relationship of ion channels using AlphaFold3.Fundamental research · 2026Review
- Mechanosensitive channel engineering: A study on the mixing and matching of YnaI and MscS sensor paddles and pores.Nature communications · 2025Article
- Lipid interactions and gating hysteresis suggest a physiological role for mechanosensitive channel YnaI.Nature communications · 2025Article
- Nanodiscs remain indispensable for Cryo-EM studies of membrane proteins.Current opinion in structural biology · 2025Review
- "Force-From-Lipids" Dependence of the MscCG Mechanosensitive Channel Gating on Anionic Membranes.Microorganisms · 2023Article
- How Functional Lipids Affect the Structure and Gating of Mechanosensitive MscS-like Channels.International journal of molecular sciences · 2022Review
- Molecular Paradigms for Biological Mechanosensing.The journal of physical chemistry. B · 2021Article
- Cryo-EM Structure of Mechanosensitive Channel YnaI Using SMA2000: Challenges and Opportunities.Membranes · 2021Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The general mechanism of bacterial mechanosensitive channels (MS) has been characterized by extensive studies on a small conductance channel MscS from Escherichia coli (E. coli). However, recent structural studies on the same channel have revealed controversial roles of various channel-bound lipids in channel gating. To better understand bacterial MscS-like channels, it is necessary to characterize homologs other than MscS. Here, we describe the structure of YnaI, one of the closest MscS homologs in E. coli, in its non-conducting state at 3.3 Å resolution determined by cryo electron microscopy. Our structure revealed the intact membrane sensor paddle domain in YnaI, which was stabilized by functionally important residues H43, Q46, Y50 and K93. In the pockets between sensor paddles, there were clear lipid densities that interact strongly with residues Q100 and R120. These lipids were a mixture of natural lipids but may be enriched in cardiolipin and phosphatidylserine. In addition, residues along the ion-conducting pathway and responsible for the heptameric assembly were discussed. Together with biochemical experiments and mutagenesis studies, our results provide strong support for the idea that the pocket lipids are functionally important for mechanosensitive channels.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.