ArticleBiophysical journal2012
Unraveling subunit cooperativity in homotetrameric HCN2 channels.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- An inter-subunit path is required for entropically-driven and negatively cooperative binding of cyclic nucleotides in the HCN2 channel.Communications biology · 2026Article
- PIP2-driven cytoplasmic domain motions are coupled to Kir2 channel gating.The Journal of general physiology · 2025Article
- cAMP binding to closed pacemaker ion channels is cooperative.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The allosteric gating mechanism of the MthK channel.National science review · 2022Article
- Thermodynamic profile of mutual subunit control in a heteromeric receptor.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- 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
- Structure and dynamics underlying elementary ligand binding events in human pacemaking channels.eLife · 2016Article
- Patch-clamp fluorometry-based channel counting to determine HCN channel conductance.The Journal of general physiology · 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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3 authors.
Funding
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Abstract
In a multimeric receptor protein, the binding of a ligand can modulate the binding of a succeeding ligand. This phenomenon, called cooperativity, is caused by the interaction of the receptor subunits. By using a complex Markovian model and a set of parameters determined previously, we analyzed how the successive binding of four ligands leads to a complex cooperative interaction of the subunits in homotetrameric HCN2 pacemaker channels. The individual steps in the model were characterized by Gibbs free energies for the equilibria and activation energies, specifying the affinity of the binding sites and the transition rates, respectively. Moreover, cooperative free energies were calculated for each binding step in both the closed and the open channel. We show that the cooperativity sequence positive-negative-positive determined for the binding affinity is generated by the combined effect of very different cooperativity sequences determined for the binding and unbinding rates, which are negative-negative-positive and no-negative-no, respectively. It is concluded that in the ligand-induced activation of HCN2 channels, the sequence of cooperativity based on the binding affinity is caused by two even qualitatively different sequences of cooperativity that are based on the rates of ligand binding and unbinding.
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