ArticleChemistry & biology2014
Structural requirements in the transmembrane domain of GLIC revealed by incorporation of noncanonical histidine analogs.
Article in Chemistry & biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- A single main-chain hydrogen bond required to keep GABANature communications · 2025Article
- Cryo-EM structures of prokaryotic ligand-gated ion channel GLIC provide insights into gating in a lipid environment.Nature communications · 2024Article
- Unveiling the Chemical Diversity of the Deep-Sea SpongeMarine drugs · 2022Article
- Article
- Allosteric potentiation of a ligand-gated ion channel is mediated by access to a deep membrane-facing cavity.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- A chimeric prokaryotic-eukaryotic pentameric ligand gated ion channel reveals interactions between the extracellular and transmembrane domains shape neurosteroid modulation.Neuropharmacology · 2017Article
- Pentameric ligand-gated ion channels exhibit distinct transmembrane domain archetypes for folding/expression and function.Scientific reports · 2017Article
- Article
- 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
- Signal Transduction at the Domain Interface of Prokaryotic Pentameric Ligand-Gated Ion Channels.PLoS biology · 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
- A chimeric prokaryotic pentameric ligand-gated channel reveals distinct pathways of activation.The Journal of general physiology · 2015Article
- Role of the Fourth Transmembrane α Helix in the Allosteric Modulation of Pentameric Ligand-Gated Ion Channels.Structure (London, England : 1993) · 2015Article
- Ethanol Modulation is Quantitatively Determined by the Transmembrane Domain of Human α1 Glycine Receptors.Alcoholism, clinical and experimental research · 2015Article
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Authors and funding
3 authors.
Funding
Abstract
The cyanobacterial pentameric ligand-gated ion channel GLIC, a homolog of the Cys-loop receptor superfamily, has provided useful structural and functional information about its eukaryotic counterparts. X-ray diffraction data and site-directed mutagenesis have previously implicated a transmembrane histidine residue (His234) as essential for channel function. Here, we investigated the role of His234 via synthesis and incorporation of histidine analogs and α-hydroxy acids using in vivo nonsense suppression. Receptors were expressed heterologously in Xenopus laevis oocytes, and whole-cell voltage-clamp electrophysiology was used to monitor channel activity. We show that an interhelix hydrogen bond involving His234 is important for stabilization of the open state, and that the shape and basicity of its side chain are highly sensitive to perturbations. In contrast, our data show that two other His residues are not involved in the acid-sensing mechanism.
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