ArticlePLoS computational biology2012
Probability fluxes and transition paths in a Markovian model describing complex subunit cooperativity in HCN2 channels.
Article in PLoS computational biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Enlightening activation gating in P2X receptors.Purinergic signalling · 2022Review
- Allosteric signaling in C-linker and cyclic nucleotide-binding domain of HCN2 channels.Biophysical journal · 2021Article
- Unravelling the intricate cooperativity of subunit gating in P2X2 ion channels.Scientific reports · 2020Article
- Article
- All four subunits of HCN2 channels contribute to the activation gating in an additive but intricate manner.The Journal of general physiology · 2018Article
- Activation gating in HCN2 channels.PLoS computational biology · 2018Article
- Retigabine holds KV7 channels open and stabilizes the resting potential.The Journal of general physiology · 2016Article
- Structure and Energetics of Allosteric Regulation of HCN2 Ion Channels by Cyclic Nucleotides.The Journal of biological chemistry · 2016Article
- Conformational Flip of Nonactivated HCN2 Channel Subunits Evoked by Cyclic Nucleotides.Biophysical journal · 2015Article
- Patch-clamp fluorometry: electrophysiology meets fluorescence.Biophysical journal · 2014Review
- Hysteresis of ligand binding in CNGA2 ion channels.Nature communications · 2013Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hyperpolarization-activated cyclic nucleotide-modulated (HCN) channels are voltage-gated tetrameric cation channels that generate electrical rhythmicity in neurons and cardiomyocytes. Activation can be enhanced by the binding of adenosine-3',5'-cyclic monophosphate (cAMP) to an intracellular cyclic nucleotide binding domain. Based on previously determined rate constants for a complex Markovian model describing the gating of homotetrameric HCN2 channels, we analyzed probability fluxes within this model, including unidirectional probability fluxes and the probability flux along transition paths. The time-dependent probability fluxes quantify the contributions of all 13 transitions of the model to channel activation. The binding of the first, third and fourth ligand evoked robust channel opening whereas the binding of the second ligand obstructed channel opening similar to the empty channel. Analysis of the net probability fluxes in terms of the transition path theory revealed pronounced hysteresis for channel activation and deactivation. These results provide quantitative insight into the complex interaction of the four structurally equal subunits, leading to non-equality in their function.
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