ArticleThe Journal of biological chemistry2008
C-terminal movement during gating in cyclic nucleotide-modulated channels.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed.
- Structure mirroring function: What's the 'matter' with the funny current?The Journal of physiology · 2026Review
- Domain coupling in allosteric regulation of SthK measured using time-resolved transition metal ion FRET.eLife · 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
- Mapping the contribution of the C-linker domain to gating polarity in CNBD channels.Biophysical journal · 2024Article
- Functional and structural characterization of interactions between opposite subunits in HCN pacemaker channels.Communications biology · 2022Article
- Uncoupling of Voltage- and Ligand-Induced Activation in HCN2 Channels by Glycine Inserts.Frontiers in physiology · 2022Article
- Gating movements and ion permeation in HCN4 pacemaker channels.Molecular cell · 2021Article
- Allosteric signaling in C-linker and cyclic nucleotide-binding domain of HCN2 channels.Biophysical journal · 2021Article
- Mechanism of ligand activation of a eukaryotic cyclic nucleotide-gated channel.Nature structural & molecular biology · 2020Article
- Allosteric conformational change of a cyclic nucleotide-gated ion channel revealed by DEER spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- cyclic AMP Regulation and Its Command in the Pacemaker Channel HCN4.Frontiers in physiology · 2020Review
- Two mutations at different positions in the CNBH domain of the hERG channel accelerate deactivation and impair the interaction with the EAG domain.The Journal of physiology · 2018Article
- An iris diaphragm mechanism to gate a cyclic nucleotide-gated ion channel.Nature communications · 2018Article
- HCN Channels: New Therapeutic Targets for Pain Treatment.Molecules (Basel, Switzerland) · 2018Review
- Mechanical transduction of cytoplasmic-to-transmembrane-domain movements in a hyperpolarization-activated cyclic nucleotide-gated cation channel.The Journal of biological chemistry · 2018Article
- Structural insights into the mechanisms of CNBD channel function.The Journal of general physiology · 2018Review
- CryoEM structure of a prokaryotic cyclic nucleotide-gated ion channel.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Investigating cyclic nucleotide and cyclic dinucleotide binding to HCN channels by surface plasmon resonance.PloS one · 2017Article
- The Arabidopsis AtPP2CA Protein Phosphatase Inhibits the GORK K+ Efflux Channel and Exerts a Dominant Suppressive Effect on Phosphomimetic-activating Mutations.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Activation of cyclic nucleotide-modulated channels such as CNG and HCN channels is promoted by ligand-induced conformational changes in their C-terminal regions. The primary intersubunit interface of these C termini includes two salt bridges per subunit, formed between three residues (one positively charged and two negatively charged amino acids) that we term the SB triad. We previously hypothesized that the SB triad is formed in the closed channel and breaks when the channel opens. Here we tested this hypothesis by dynamically manipulating the SB triad in functioning CNGA1 channels. Reversing the charge at positions Arg-431 and Glu-462, two of the SB triad residues, by either mutation or application of charged reagents increased the favorability of channel opening. To determine how a charge reversal mutation in the SB triad structurally affects the channel, we solved the crystal structure of the HCN2 C-terminal region with the equivalent E462R mutation. The backbone structure of this mutant was very similar to that of wild type, but the SB triad was rearranged such that both salt bridges did not always form simultaneously, suggesting a mechanism for the increased ease of opening of the mutant channels. To prevent movement in the SB triad, we tethered two components of the SB triad region together with cysteine-reactive cross-linkers. Preventing normal movement of the SB triad region with short cross-linkers inhibited channel opening, whereas longer cross-linkers did not. These results support our hypothesis that the SB triad forms in the closed channel and indicate that this region expands as the channel opens.
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