ArticleProceedings of the National Academy of Sciences of the United States of America2014
Family of prokaryote cyclic nucleotide-modulated ion channels.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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45 citing papers in PubMed, 72 citations in OpenAlex.
- Structural determinants of voltage sensitivity in hyperpolarization-activated ion channels and their persistence in the evolutionary scale.Pflugers Archiv : European journal of physiology · 2026Article
- Membrane-forming phospholipids allosterically modulate native-state prolyl isomerization in a CNG channel.Protein science : a publication of the Protein Society · 2025Article
- Optogenetic silencing by combining a rhodopsin cyclase with an engineered cGMP-gated potassium channel.Science advances · 2025Article
- Domain coupling in allosteric regulation of SthK measured using time-resolved transition metal ion FRET.eLife · 2025Article
- Ctenophores and parahoxozoans independently evolved functionally diverse voltage-gated K+ channels.The Journal of general physiology · 2025Article
- Article
- Ligand-Coupled Conformational Changes in a Cyclic Nucleotide-Gated Ion Channel Revealed by Time-Resolved Transition Metal Ion FRET.bioRxiv : the preprint server for biology · 2024Article
- PIP2 inhibits pore opening of the cyclic nucleotide-gated channel SthK.Nature communications · 2024Article
- Exploring Flexibility and Folding Patterns Throughout Time in Voltage Sensors.Journal of molecular evolution · 2023Article
- Structural basis of properties, mechanisms, and channelopathy of cyclic nucleotide-gated channels.Channels (Austin, Tex.) · 2023Review
- Native Function of the Bacterial Ion Channel SthK in a Sparsely Tethered Lipid Bilayer Membrane Architecture.The journal of physical chemistry. B · 2023Article
- Genome-Scale Analysis Reveals Extensive Diversification of Voltage-Gated K+ Channels in Stem Cnidarians.Genome biology and evolution · 2023Article
- A Light-Triggered Synthetic Nanopore for Controlling Molecular Transport Across Biological Membranes.Angewandte Chemie (International ed. in English) · 2022Article
- Gating intermediates reveal inhibitory role of the voltage sensor in a cyclic nucleotide-modulated ion channel.Nature communications · 2022Article
- Anionic lipids unlock the gates of select ion channels in the pacemaker family.Nature structural & molecular biology · 2022Article
- Long-term in vivo application of a potassium channel-based optogenetic silencer in the healthy and epileptic mouse hippocampus.BMC biology · 2022Article
- When Is a Potassium Channel Not a Potassium Channel?Function (Oxford, England) · 2022Article
- Article
- CNG channel structure, function, and gating: a tale of conformational flexibility.Pflugers Archiv : European journal of physiology · 2021Review
- External Cd2+ and protons activate the hyperpolarization-gated K+ channel KAT1 at the voltage sensor.The Journal of general physiology · 2021Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cyclic nucleotide-modulated ion channels are molecular pores that mediate the passage of ions across the cell membrane in response to cAMP or GMP. Structural insight into this class of ion channels currently comes from a related homolog, MloK1, that contains six transmembrane domains and a cytoplasmic cyclic nucleotide binding domain. However, unlike eukaryote hyperpolarization-activated cyclic nucleotide-modulated (HCN) and cyclic nucleotide-gated (CNG) channels, MloK1 lacks a C-linker region, which critically contributes to the molecular coupling between ligand binding and channel opening. In this study, we report the identification and characterization of five previously unidentified prokaryote homologs with high sequence similarity (24-32%) to eukaryote HCN and CNG channels and that contain a C-linker region. Biochemical characterization shows that two homologs, termed AmaK and SthK, can be expressed and purified as detergent-solubilized protein from Escherichia coli membranes. Expression of SthK channels in Xenopus laevis oocytes and functional characterization using the patch-clamp technique revealed that the channels are gated by cAMP, but not cGMP, are highly selective for K(+) ions over Na(+) ions, generate a large unitary conductance, and are only weakly voltage dependent. These properties resemble essential properties of various eukaryote HCN or CNG channels. Our results contribute to an understanding of the evolutionary origin of cyclic nucleotide-modulated ion channels and pave the way for future structural and functional studies.
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