ArticleStructure (London, England : 1993)2015
Role of the Fourth Transmembrane α Helix in the Allosteric Modulation of Pentameric Ligand-Gated Ion Channels.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Structure-Function Studies of Pentameric Ligand-Gated Ion Channels: Combining Experimental and Computational Approaches.Advances in experimental medicine and biology · 2026Review
- Structural mechanism of lipid modulation of pentameric ligand-gated ion channel activity.bioRxiv : the preprint server for biology · 2025Article
- State-dependent binding of cholesterol and an anionic lipid to the muscle-type Torpedo nicotinic acetylcholine receptor.Communications biology · 2024Article
- Mitochondrial gene expression in different organs of Hoplobatrachus rugulosus from China and Thailand under low-temperature stress.BMC zoology · 2022Article
- Structural mechanism of muscle nicotinic receptor desensitization and block by curare.Nature structural & molecular biology · 2022Article
- Mutations of the nACh Receptor M4 Helix Reveal Different Phenotypes in Different Expression Systems: Could Lipids be Responsible?Frontiers in physiology · 2022Article
- Novel Functional Properties of Missense Mutations in the Glycine Receptor β Subunit in Startle Disease.Frontiers in molecular neuroscience · 2021Article
- The functional role of the αM4 transmembrane helix in the muscle nicotinic acetylcholine receptor probed through mutagenesis and coevolutionary analyses.The Journal of biological chemistry · 2020Article
- A lipid site shapes the agonist response of a pentameric ligand-gated ion channel.Nature chemical biology · 2019Article
- Article
- Untangling Direct and Domain-Mediated Interactions Between Nicotinic Acetylcholine Receptors in DHA-Rich Membranes.The Journal of membrane biology · 2019Article
- Boundary lipids of the nicotinic acetylcholine receptor: Spontaneous partitioning via coarse-grained molecular dynamics simulation.Biochimica et biophysica acta. Biomembranes · 2019Article
- An allosteric link connecting the lipid-protein interface to the gating of the nicotinic acetylcholine receptor.Scientific reports · 2018Article
- Pentameric ligand-gated ion channels exhibit distinct transmembrane domain archetypes for folding/expression and function.Scientific reports · 2017Article
- Article
- Article
- Role of the Cys Loop and Transmembrane Domain in the Allosteric Modulation of α4β2 Nicotinic Acetylcholine Receptors.The Journal of biological chemistry · 2017Article
- Perturbation of Critical Prolines in Gloeobacter violaceus Ligand-gated Ion Channel (GLIC) Supports Conserved Gating Motions among Cys-loop Receptors.The Journal of biological chemistry · 2016Article
- Common Internal Allosteric Network Links Anesthetic Binding Sites in a Pentameric Ligand-Gated Ion Channel.PloS one · 2016Article
- The M4 Transmembrane α-Helix Contributes Differently to Both the Maturation and Function of Two Prokaryotic Pentameric Ligand-gated Ion Channels.The Journal of biological chemistry · 2015Article
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Authors and funding
8 authors.
Funding
Abstract
The gating of pentameric ligand-gated ion channels is sensitive to a variety of allosteric modulators that act on structures peripheral to those involved in the allosteric pathway leading from the agonist site to the channel gate. One such structure, the lipid-exposed transmembrane α helix, M4, is the target of lipids, neurosteroids, and disease-causing mutations. Here we show that M4 interactions with the adjacent transmembrane α helices, M1 and M3, modulate pLGIC function. Enhanced M4 interactions promote channel function while ineffective interactions reduce channel function. The interface chemistry governs the intrinsic strength of M4-M1/M3 inter-helical interactions, both influencing channel gating and imparting distinct susceptibilities to the potentiating effects of a lipid-facing M4 congenital myasthenic syndrome mutation. Through aromatic substitutions, functional studies, and molecular dynamics simulations, we elucidate a mechanism by which M4 modulates channel function.
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