ArticleThe Journal of general physiology2010
The contribution of individual subunits to the coupling of the voltage sensor to pore opening in Shaker K channels: effect of ILT mutations in heterotetramers.
Article in The Journal of general physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Differential negative dominance by KCNA2 variants associated with global developmental delay suggests KCNA2 haploinsufficiency in humans.The Journal of physiology · 2026Article
- Energy landscape of a Kv channel revealed by temperature steps while perturbing its electromechanical coupling.Nature communications · 2025Article
- An epilepsy-associated KProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Intersubunit Concerted Cooperative and cis-Type Mechanisms Modulate Allosteric Gating in Two-Pore-Domain Potassium Channel TREK-2.Frontiers in cellular neuroscience · 2016Article
- Cellular mechanisms of mutations in Kv7.1: auditory functions in Jervell and Lange-Nielsen syndrome vs. Romano-Ward syndrome.Frontiers in cellular neuroscience · 2015Article
- Mechanosensitive gating of Kv channels.PloS one · 2015Review
- A self-consistent approach for determining pairwise interactions that underlie channel activation.The Journal of general physiology · 2014Article
- Voltage-sensor movements describe slow inactivation of voltage-gated sodium channels I: wild-type skeletal muscle Na(V)1.4.The Journal of general physiology · 2013Article
- The pore of voltage-gated potassium ion channels is strained when closed.Nature communications · 2013Article
- Probing the structural basis for differential KCNQ1 modulation by KCNE1 and KCNE2.The Journal of general physiology · 2012Article
- Tetrameric assembly of KvLm K+ channels with defined numbers of voltage sensors.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- KCNQ1 channels do not undergo concerted but sequential gating transitions in both the absence and the presence of KCNE1 protein.The Journal of biological chemistry · 2012Article
- Voltage-dependent conformational changes in connexin channels.Biochimica et biophysica acta · 2012Review
- Mechanism of electromechanical coupling in voltage-gated potassium channels.Frontiers in pharmacology · 2012Article
- Being flexible: the voltage-controllable activation gate of kv channels.Frontiers in pharmacology · 2012Article
- Estimating the voltage-dependent free energy change of ion channels using the median voltage for activation.The Journal of general physiology · 2012Article
- Double mutant cycle analysis identified a critical leucine residue in the IIS4S5 linker for the activation of the Ca(V)2.3 calcium channel.The Journal of biological chemistry · 2011Article
- Mode shift of the voltage sensors in Shaker K+ channels is caused by energetic coupling to the pore domain.The Journal of general physiology · 2011Article
- Control of a final gating charge transition by a hydrophobic residue in the S2 segment of a K+ channel voltage sensor.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
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2 authors.
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Abstract
Voltage-gated ion channels couple conformational change(s) of the voltage-sensing domain to those of the opening of an intracellular gate to allow ionic conduction. Much larger positive potentials are required to couple these conformational changes to the opening of the gate of Shaker K(+) channels with the concurrent mutations V369I, I372L, and S376T (ILT) at the N-terminal end of the S4 segment. We used cut-open oocyte voltage clamp to study the biophysical and thermodynamical properties of heterotetrameric concatemerized channels with different stoichiometries of ILT mutations. The voltage-sensing domains of ILT mutant channels require smaller depolarization to activate but their intracellular gate does not immediately follow the movement of the voltage-sensing domain, requiring larger depolarization to open. Our results demonstrate that each subunit contributes equally to the rightward shift of the conductance-voltage relationship and that a single ILT-containing subunit is sufficient to induce a large enthalpic and entropic barrier, limiting opening of the intracellular gate.
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