ArticleNature communications2020
Prolyl isomerization controls activation kinetics of a cyclic nucleotide-gated ion channel.
Article in Nature communications, 2020. 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, 18 citations in OpenAlex.
- Modeling Peptides in Aqueous Ionic Liquid Mixtures: A Quantum Mechanics/Molecular Dynamics Study of Structural and NMR Properties.Journal of chemical theory and computation · 2026Article
- Biophysical characterization of Cyclophilin B reveals membrane localization as its primary functional determinant as a prolyl isomerase.Protein science : a publication of the Protein Society · 2026Article
- Membrane-forming phospholipids allosterically modulate native-state prolyl isomerization in a CNG channel.Protein science : a publication of the Protein Society · 2025Article
- Computational study of terahertz-driven controllable molecular isomerization.Nature communications · 2025Article
- Single-molecule nanopore sensing of prolineChemical science · 2025Article
- Phi-Value and NMR Structural Analysis of a Coupled Native-State Prolyl Isomerization and Conformational Protein Folding Process.Biomolecules · 2025Article
- Proline substitutions in the ASIC1 β11-12 linker slow desensitization.Biophysical journal · 2024Article
- Discrimination between cyclic nucleotides in a cyclic nucleotide-gated ion channel.Nature structural & molecular biology · 2023Article
- 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
- Protein folding and unfolding: proline cis-trans isomerization at the c subunits of FProteins · 2022Article
- Photopharmacology of Ion Channels through the Light of the Computational Microscope.International journal of molecular sciences · 2021Review
- Electromechanical coupling mechanism for activation and inactivation of an HCN channel.Nature communications · 2021Article
- Druggable Lipid Binding Sites in Pentameric Ligand-Gated Ion Channels and Transient Receptor Potential Channels.Frontiers in physiology · 2021Review
- Correlating ion channel structure and function.Methods in enzymology · 2021Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
SthK, a cyclic nucleotide-modulated ion channel from Spirochaeta thermophila, activates slowly upon cAMP increase. This is reminiscent of the slow, cAMP-induced activation reported for the hyperpolarization-activated and cyclic nucleotide-gated channel HCN2 in the family of so-called pacemaker channels. Here, we investigate slow cAMP-induced activation in purified SthK channels using stopped-flow assays, mutagenesis, enzymatic catalysis and inhibition assays revealing that the cis/trans conformation of a conserved proline in the cyclic nucleotide-binding domain determines the activation kinetics of SthK. We propose that SthK exists in two forms: trans Pro300 SthK with high ligand binding affinity and fast activation, and cis Pro300 SthK with low affinity and slow activation. Following channel activation, the cis/trans equilibrium, catalyzed by prolyl isomerases, is shifted towards trans, while steady-state channel activity is unaffected. Our results reveal prolyl isomerization as a regulatory mechanism for SthK, and potentially eukaryotic HCN channels. This mechanism could contribute to electrical rhythmicity in cells.
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