ArticleThe Journal of biological chemistry2016
Structure and Energetics of Allosteric Regulation of HCN2 Ion Channels by Cyclic Nucleotides.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 61 citations in OpenAlex.
- An inter-subunit path is required for entropically-driven and negatively cooperative binding of cyclic nucleotides in the HCN2 channel.Communications biology · 2026Article
- Domain coupling in allosteric regulation of SthK measured using time-resolved transition metal ion FRET.eLife · 2025Article
- An Allosteric Model for Electromechanical Coupling in Cardiac CNBD Channels.bioRxiv : the preprint server for biology · 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
- Measuring conformational equilibria in allosteric proteins with time-resolved tmFRET.Biophysical journal · 2024Article
- Measuring conformational equilibria in allosteric proteins with time-resolved tmFRET.bioRxiv : the preprint server for biology · 2024Article
- Direct regulation of the voltage sensor of HCN channels by membrane lipid compartmentalization.Nature communications · 2023Article
- HCN2 Ion Channels Drive Pain in Rodent Models of Migraine.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022Article
- Single-molecule imaging with cell-derived nanovesicles reveals early binding dynamics at a cyclic nucleotide-gated ion channel.Nature communications · 2021Article
- Electromechanical coupling mechanism for activation and inactivation of an HCN channel.Nature communications · 2021Article
- Allosteric signaling in C-linker and cyclic nucleotide-binding domain of HCN2 channels.Biophysical journal · 2021Article
- Binding and structural asymmetry governs ligand sensitivity in a cyclic nucleotide-gated ion channel.The Journal of general physiology · 2019Article
- Functional characterization and optimization of a bacterial cyclic nucleotide-gated channel.The Journal of biological chemistry · 2019Article
- Article
- Insights into the molecular mechanism for hyperpolarization-dependent activation of HCN channels.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Insights on the Structure, Molecular Weight and Activity of an Antibacterial Protein-Polymer Hybrid.Chemphyschem : a European journal of chemical physics and physical chemistry · 2018Article
- Structural insights into the mechanisms of CNBD channel function.The Journal of general physiology · 2018Review
- Mechanism for the inhibition of the cAMP dependence of HCN ion channels by the auxiliary subunit TRIP8b.The Journal of biological chemistry · 2017Article
- Rates and equilibrium constants of the ligand-induced conformational transition of an HCN ion channel protein domain determined by DEER spectroscopy.Physical chemistry chemical physics : PCCP · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Hyperpolarization-activated cyclic nucleotide-gated (HCN) ion channels play an important role in regulating electrical activity in the heart and brain. They are gated by the binding of cyclic nucleotides to a conserved, intracellular cyclic nucleotide-binding domain (CNBD), which is connected to the channel pore by a C-linker region. Binding of cyclic nucleotides increases the rate and extent of channel activation and shifts it to less hyperpolarized voltages. We probed the allosteric mechanism of different cyclic nucleotides on the CNBD and on channel gating. Electrophysiology experiments showed that cAMP, cGMP, and cCMP were effective agonists of the channel and produced similar increases in the extent of channel activation. In contrast, electron paramagnetic resonance (EPR) and nuclear magnetic resonance (NMR) on the isolated CNBD indicated that the induced conformational changes and the degrees of stabilization of the active conformation differed for the three cyclic nucleotides. We explain these results with a model where different allosteric mechanisms in the CNBD all converge to have the same effect on the C-linker and render all three cyclic nucleotides similarly potent activators of the channel.
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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.