ArticleThe Journal of general physiology2014
Calcium-dependent stoichiometries of the KCa2.2 (SK) intracellular domain/calmodulin complex in solution.
Article in The Journal of general physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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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.
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Who cites it
18 citing papers in PubMed.
- Pharmacological Enhancement of Small Conductance CaCirculation research · 2025Article
- 6,7-Dichloro-1H-indole-2,3-dione-3-oxime functions as a superagonist for the intermediate-conductance CaMolecular pharmacology · 2025Article
- Multivalent Protein-Nucleic Acid Interactions Probed by Composition-Gradient Multiangle Light Scattering.ACS omega · 2024Article
- Investigating the Impact of Electrostatic Interactions on Calmodulin Binding and CaInternational journal of molecular sciences · 2024Article
- Challenges in the Therapeutic Targeting of KCa Channels: From Basic Physiology to Clinical Applications.International journal of molecular sciences · 2024Review
- Article
- Protein intrinsic viscosity determination with the Viscosizer TD instrument: reaching beyond the initially expected applications.European biophysics journal : EBJ · 2021Article
- Atomistic Insights of Calmodulin Gating of Complete Ion Channels.International journal of molecular sciences · 2020Review
- Pharmacology of Small- and Intermediate-Conductance Calcium-Activated Potassium Channels.Annual review of pharmacology and toxicology · 2020Review
- Activation mechanism of a human SK-calmodulin channel complex elucidated by cryo-EM structures.Science (New York, N.Y.) · 2018Article
- Coordination to lanthanide ions distorts binding site conformation in calmodulin.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structural basis and energy landscape for the CaProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Are there superagonists for calcium-activated potassium channels?Channels (Austin, Tex.) · 2017Article
- Recent applications of light scattering measurement in the biological and biopharmaceutical sciences.Analytical biochemistry · 2016Review
- Conserved properties of individual Ca2+-binding sites in calmodulin.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Knockdown of the small conductance Ca(2+) -activated K(+) channels is potently cytotoxic in breast cancer cell lines.British journal of pharmacology · 2016Article
- The VieB auxiliary protein negatively regulates the VieSA signal transduction system in Vibrio cholerae.BMC microbiology · 2015Article
- Towards a Unified Theory of Calmodulin Regulation (Calmodulation) of Voltage-Gated Calcium and Sodium Channels.Current molecular pharmacology · 2015Review
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4 authors.
Funding
Abstract
Ca(2+) activates SK Ca(2+)-activated K(+) channels through the protein Ca(2+) sensor, calmodulin (CaM). To understand how SK channels operate, it is necessary to determine how Ca(2+) regulates CaM binding to its target on SK. Tagless, recombinant SK peptide (SKp), was purified for binding studies with CaM at low and high Ca(2+) concentrations. Composition gradient multi-angle light scattering accurately measures the molar mass, stoichiometry, and affinity of protein complexes. In 2 mM Ca(2+), SKp and CaM bind with three different stoichiometries that depend on the molar ratio of SKp:CaM in solution. These complexes include 28 kD 1SKp/1CaM, 39 kD 2SKp/1CaM, and 44 kD 1SKp/2CaM. A 2SKp/2CaM complex, observed in prior crystallographic studies, is absent. At <5 nM Ca(2+), 1SKp/1CaM and 2SKp/1CaM were observed; however, 1SKp/2CaM was absent. Analytical ultracentrifugation was used to characterize the physical properties of the three SKp/CaM stoichiometries. In high Ca(2+), the sedimentation coefficient is smaller for a 1SKp:1CaM solution than it is for either 2SKp:1CaM or 1SKp:2CaM. At low Ca(2+) and at >100 µM protein concentrations, a molar excess of SKp over CaM causes aggregation. Aggregation is not observed in Ca(2+) or with CaM in molar excess. In low Ca(2+) both 1SKp:1CaM and 1SKp:2CaM solutions have similar sedimentation coefficients, which is consistent with the absence of a 1SKp/2CaM complex in low Ca(2+). These results suggest that complexes with stoichiometries other than 2SKp/2CaM are important in gating.
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