ArticleThe Journal of general physiology2012
Charge movement in gating-locked HCN channels reveals weak coupling of voltage sensors and gate.
Article in The Journal of general physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed.
- Article
- Loose Coupling between the Voltage Sensor and the Activation Gate in Mammalian HCN Channels Suggests a Gating Mechanism.International journal of molecular sciences · 2024Article
- Photo-crosslinking hERG channels causes a U.V.-driven, state-dependent disruption of kinetics and voltage dependence of activation.bioRxiv : the preprint server for biology · 2024Article
- Interplay between VSD, pore, and membrane lipids in electromechanical coupling in HCN channels.eLife · 2023Article
- Charge-voltage curves of Shaker potassium channel are not hysteretic at steady state.The Journal of general physiology · 2023Article
- Activation and closed-state inactivation mechanisms of the human voltage-gated KMolecular cell · 2022Article
- A second S4 movement opens hyperpolarization-activated HCN channels.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Mapping Electromechanical Coupling Pathways in Voltage-Gated Ion Channels: Challenges and the Way Forward.Journal of molecular biology · 2021Review
- Regulation of Ion Channel Function by Gas Molecules.Advances in experimental medicine and biology · 2021Review
- Helix breaking transition in the S4 of HCN channel is critical for hyperpolarization-dependent gating.eLife · 2019Article
- The HCN channel voltage sensor undergoes a large downward motion during hyperpolarization.Nature structural & molecular biology · 2019Article
- cAMP binds to closed, inactivated, and open sea urchin HCN channels in a state-dependent manner.The Journal of general physiology · 2019Article
- Singlet oxygen modification abolishes voltage-dependent inactivation of the sea urchin spHCN channel.The Journal of general physiology · 2018Article
- All four subunits of HCN2 channels contribute to the activation gating in an additive but intricate manner.The Journal of general physiology · 2018Article
- 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
- Spatial positioning of CFTR's pore-lining residues affirms an asymmetrical contribution of transmembrane segments to the anion permeation pathway.The Journal of general physiology · 2016Article
- Interfacial gating triad is crucial for electromechanical transduction in voltage-activated potassium channels.The Journal of general physiology · 2014Article
- Modeling ion channels: past, present, and future.The Journal of general physiology · 2014Review
- State-dependent and site-directed photodynamic transformation of HCN2 channel by singlet oxygen.The Journal of general physiology · 2014Article
- Biochemical and structural analysis of the hyperpolarization-activated K(+) channel MVP.Biochemistry · 2014Article
Corrections and comments
- Commented on by
Authors and funding
2 authors.
Funding
Abstract
HCN (hyperpolarization-activated cyclic nucleotide gated) pacemaker channels have an architecture similar to that of voltage-gated K(+) channels, but they open with the opposite voltage dependence. HCN channels use essentially the same positively charged voltage sensors and intracellular activation gates as K(+) channels, but apparently these two components are coupled differently. In this study, we examine the energetics of coupling between the voltage sensor and the pore by using cysteine mutant channels for which low concentrations of Cd(2+) ions freeze the open-closed gating machinery but still allow the sensors to move. We were able to lock mutant channels either into open or into closed states by the application of Cd(2+) and measure the effect on voltage sensor movement. Cd(2+) did not immobilize the gating charge, as expected for strict coupling, but rather it produced shifts in the voltage dependence of voltage sensor charge movement, consistent with its effect of confining transitions to either closed or open states. From the magnitude of the Cd(2+)-induced shifts, we estimate that each voltage sensor produces a roughly three- to sevenfold effect on the open-closed equilibrium, corresponding to a coupling energy of ∼1.3-2 kT per sensor. Such coupling is not only opposite in sign to the coupling in K(+) channels, but also much weaker.
Indexed as
Identifiers
What OpenQuestion holds
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.