ArticleThe Journal of general physiology1998
A mutation in S6 of Shaker potassium channels decreases the K+ affinity of an ion binding site revealing ion-ion interactions in the pore.
Article in The Journal of general physiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
- Electric field-induced pore constriction in the human KProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Dilation of ion selectivity filters in cation channels.Trends in biochemical sciences · 2024Review
- Eukaryotic Kv channel Shaker inactivates through selectivity filter dilation rather than collapse.Science advances · 2023Article
- Mutations within the selectivity filter reveal that Kv1 channels have distinct propensities to slow inactivate.The Journal of general physiology · 2022Article
- Structure of the Shaker Kv channel and mechanism of slow C-type inactivation.Science advances · 2022Article
- Conductance stability and Na+ interaction with Shab K+ channels under low K+ conditions.Channels (Austin, Tex.) · 2021Article
- Selectivity filter ion binding affinity determines inactivation in a potassium channel.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Allosteric coupling of the inner activation gate to the outer pore of a potassium channel.Scientific reports · 2013Article
- Preferential binding of K+ ions in the selectivity filter at equilibrium explains high selectivity of K+ channels.The Journal of general physiology · 2012Article
- Structural correlates of selectivity and inactivation in potassium channels.Biochimica et biophysica acta · 2012Review
- A synthetic S6 segment derived from KvAP channel self-assembles, permeabilizes lipid vesicles, and exhibits ion channel activity in bilayer lipid membrane.The Journal of biological chemistry · 2011Article
- A novel current pathway parallel to the central pore in a mutant voltage-gated potassium channel.The Journal of biological chemistry · 2011Article
- Origins of ion selectivity in potassium channels from the perspective of channel block.The Journal of general physiology · 2011Review
- Electrostatic influences of charged inner pore residues on the conductance and gating of small conductance Ca2+ activated K+ channels.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Tuning the ion selectivity of tetrameric cation channels by changing the number of ion binding sites.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Quinidine interaction with Shab K+ channels: pore block and irreversible collapse of the K+ conductance.The Journal of physiology · 2010Article
- Novel insights into K+ selectivity from high-resolution structures of an open K+ channel pore.Nature structural & molecular biology · 2010Article
- Four-mode gating model of fast inactivation of sodium channel Nav1.2a.Pflugers Archiv : European journal of physiology · 2008Article
- Stability of the Shab K+ channel conductance in 0 K+ solutions: the role of the membrane potential.Biophysical journal · 2007Article
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2 authors.
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Abstract
Under physiological conditions, potassium channels are extraordinarily selective for potassium over other ions. However, in the absence of potassium, certain potassium channels can conduct sodium. Sodium flux is blocked by the addition of low concentrations of potassium. Potassium affinity, and therefore the ability to block sodium current, varies among potassium channel subtypes (Korn, S.J., and S.R. Ikeda. 1995. Science. 269:410-412; Starkus, J.G., L. Kuschel, M.D. Rayner, and S.H. Heinemann. 1997. J. Gen. Physiol. 110:539-550). The Shaker potassium channel conducts sodium poorly in the presence of very low (micromolar) potassium due to its high potassium affinity (Starkus, J.G., L. Kuschel, M.D. Rayner, and S.H. Heinemann. 1997. J. Gen. Physiol. 110:539-550; Ogielska, E.M., and R. W. Aldrich. 1997. Biophys. J. 72:A233 [Abstr.]). We show that changing a single residue in S6, A463C, decreases the apparent internal potassium affinity of the Shaker channel pore from the micromolar to the millimolar range, as determined from the ability of potassium to block the sodium currents. Independent evidence that A463C decreases the apparent affinity of a binding site in the pore comes from a study of barium block of potassium currents. The A463C mutation decreases the internal barium affinity of the channel, as expected if barium blocks current by binding to a potassium site in the pore. The decrease in the apparent potassium affinity in A463C channels allows further study of possible ion interactions in the pore. Our results indicate that sodium and potassium can occupy the pore simultaneously and that multiple occupancy results in interactions between ions in the channel pore.
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