ArticleBiophysical journal2002
Localization of divalent cation-binding site in the pore of a small conductance Ca(2+)-activated K(+) channel and its role in determining current-voltage relationship.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Restoration of mitochondrial CaJournal of molecular and cellular cardiology · 2026Article
- Magnesium Ions as Modulators of Voltage-Gated and Ligand-Gated Ion Channels in Central Neurons.International journal of molecular sciences · 2025Review
- Functional validation of human SK channels variants causing NEDMAB and Zimmermann-Laband syndrome-3 inBrain communications · 2025Article
- Dual effects of the small-conductance CaAmerican journal of physiology. Heart and circulatory physiology · 2023Article
- Small-conductance CaHeart rhythm · 2020Article
- Impact of IBiophysical journal · 2020Article
- PKA phosphorylation underlies functional recruitment of sarcolemmal SK2 channels in ventricular myocytes from hypertrophic hearts.The Journal of physiology · 2020Article
- Ion Channels in Pulmonary Hypertension: A Therapeutic Interest?International journal of molecular sciences · 2018Review
- A biophysically detailed computational model of urinary bladder small DRG neuron soma.PLoS computational biology · 2018Article
- Functional expression of SK channels in murine detrusor PDGFR+ cells.The Journal of physiology · 2013Article
- Natural and synthetic modulators of SK (K(ca)2) potassium channels inhibit magnesium-dependent activity of the kinase-coupled cation channel TRPM7.British journal of pharmacology · 2012Article
- Crucial role of a shared extracellular loop in apamin sensitivity and maintenance of pore shape of small-conductance calcium-activated potassium (SK) channels.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Modulation of hair cell efferents.Hearing research · 2011Review
- Negative gating modulation by (R)-N-(benzimidazol-2-yl)-1,2,3,4-tetrahydro-1-naphthylamine (NS8593) depends on residues in the inner pore vestibule: pharmacological evidence of deep-pore gating of K(Ca)2 channels.Molecular pharmacology · 2011Article
- 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
- Article
- EF hands at the N-lobe of calmodulin are required for both SK channel gating and stable SK-calmodulin interaction.The Journal of general physiology · 2009Article
- Inhibition of K(Ca)2.2 and K(Ca)2.3 channel currents by protonation of outer pore histidine residues.The Journal of general physiology · 2009Article
- Intracellular Mg2+ is a voltage-dependent pore blocker of HCN channels.American journal of physiology. Cell physiology · 2008Article
- Ca2+-activated K+ channels in murine endothelial cells: block by intracellular calcium and magnesium.The Journal of general physiology · 2008Article
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Authors and funding
2 authors.
Funding
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Abstract
In our previous study, we proposed that the inwardly rectifying current-voltage (I-V) relationship of small-conductance Ca(2+)-activated K(+) channels (SK(Ca) channels) is the result of voltage-dependent blockade of K(+) currents by intracellular divalent cations. We expressed a cloned SK(Ca) channel, rSK2, in Xenopus oocytes and further characterized the nature of the divalent cation-binding site by electrophysiological means. Using site-directed substitution of hydrophilic residues in K(+)-conducting pathway and subsequent functional analysis of mutations, we identified an amino acid residue, Ser-359, in the pore-forming region of rSK2 critical for the strong rectification of the I-V relationship. This residue interacts directly with intracellular divalent cations and determines the ionic selectivity. Therefore, we confirmed our proposition by localizing the divalent cation-binding site within the conduction pathway of the SK(Ca) channel. Because the Ser residue unique for the subfamily of SK(Ca) channels is likely to locate closely to the selectivity filter of the channels, it may also contribute to other permeation characteristics of SK(Ca) channels.
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