ArticleProceedings of the National Academy of Sciences of the United States of America2009
Activation of the SK potassium channel-calmodulin complex by nanomolar concentrations of terbium.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Structure, Gating and Basic Functions of the Ca2+-activated K Channel of Intermediate Conductance.Current neuropharmacology · 2018Review
- Crystal structure of a heterotetrameric NMDA receptor ion channel.Science (New York, N.Y.) · 2014Article
- Initial steps of inactivation at the K+ channel selectivity filter.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Sarcoplasmic reticulum Ca²⁺ release is both necessary and sufficient for SK channel activation in ventricular myocytes.American journal of physiology. Heart and circulatory physiology · 2014Article
- Contribution of the KCa3.1 channel-calmodulin interactions to the regulation of the KCa3.1 gating process.The Journal of general physiology · 2013Article
- 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
- Calcium microdomains near R-type calcium channels control the induction of presynaptic long-term potentiation at parallel fiber to purkinje cell synapses.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- Allosteric block of KCa2 channels by apamin.The Journal of biological chemistry · 2010Article
- 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
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Small conductance Ca(2+)-activated K(+) (SK) channels sense intracellular Ca(2+) concentrations via the associated Ca(2+)-binding protein calmodulin. Structural and functional studies have revealed essential properties of the interaction between calmodulin and SK channels. However, it is not fully understood how the binding of Ca(2+) to calmodulin leads to channel opening. Drawing on previous biochemical studies of free calmodulin using lanthanide ions as Ca(2+) substitutes, we have used the lanthanide ion, Tb(3+), as an alternative ligand to study the activation properties of SK channels. We found that SK channels can be fully activated by nanomolar concentrations of Tb(3+), indicating an apparent affinity >100-fold higher than Ca(2+). Competition experiments show that Tb(3+) binds to the same sites as Ca(2+) to activate the channels. Additionally, SK channels activated by Tb(3+) demonstrate a remarkably slow deactivation process. Comparison of our results with previous biochemical studies suggests that in the intact SK channel complex, the N-lobe of calmodulin provides ligand-binding sites for channel gating, and that its ligand-binding properties are comparable to those of the N-lobe in isolated calmodulin.
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