ArticleProceedings of the National Academy of Sciences of the United States of America2005
S3b amino acid residues do not shuttle across the bilayer in voltage-dependent Shaker K+ channels.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed.
- Modulation of Kv Channel Gating by Light-Controlled Membrane Thickness.Biomolecules · 2025Article
- Exploring Flexibility and Folding Patterns Throughout Time in Voltage Sensors.Journal of molecular evolution · 2023Article
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- Nano-positioning system for structural analysis of functional homomeric proteins in multiple conformations.Structure (London, England : 1993) · 2012Article
- Voltage sensor of ion channels and enzymes.Biophysical reviews · 2012Review
- Article
- Modification of hERG1 channel gating by Cd2+.The Journal of general physiology · 2010Article
- Down-state model of the voltage-sensing domain of a potassium channel.Biophysical journal · 2010Article
- Strong cooperativity between subunits in voltage-gated proton channels.Nature structural & molecular biology · 2010Article
- From the gating charge response to pore domain movement: initial motions of Kv1.2 dynamics under physiological voltage changes.Molecular membrane biology · 2009Article
- Models of voltage-dependent conformational changes in NaChBac channels.Biophysical journal · 2008Article
- Article
- Mapping the membrane-aqueous border for the voltage-sensing domain of a potassium channel.The Journal of biological chemistry · 2007Article
- Two atomic constraints unambiguously position the S4 segment relative to S1 and S2 segments in the closed state of Shaker K channel.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Constraints on voltage sensor movement in the shaker K+ channel.The Journal of general physiology · 2006Article
- Molecular template for a voltage sensor in a novel K+ channel. II. Conservation of a eukaryotic sensor fold in a prokaryotic K+ channel.The Journal of general physiology · 2006Article
- Molecular template for a voltage sensor in a novel K+ channel. I. Identification and functional characterization of KvLm, a voltage-gated K+ channel from Listeria monocytogenes.The Journal of general physiology · 2006Article
- Interactive domains between pore loops of the yeast K+ channel TOK1 associate with extracellular K+ sensitivity.The Biochemical journal · 2006Article
- How ion channels sense membrane potential.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
In voltage-dependent channels, positive charges contained within the S4 domain are the voltage-sensing elements. The "voltage-sensor paddle" gating mechanism proposed for the KvAP K+ channel has been the subject of intense discussion regarding its general applicability to the family of voltage-gated channels. In this model, the voltage sensor composed of the S3b and the S4 segment shuttles across the lipid bilayer during channel activation. Guided by this mechanism, we assessed here the accessibility of residues in the S3 segment of the Shaker K+ channel by using cysteine-scanning mutagenesis. Mutants expressed robust K+ currents in Xenopus oocytes and reacted with methanethiosulfonate ethyltrimethylammonium in both closed and open conformations of the channel. Because Shaker has a long S3-S4 linker segment, we generated a deletion mutant with only three residues to emulate the KvAP structure. In this short linker mutant, all of the tested residues in the S3b were accessible to methanethiosulfonate ethyltrimethylammonium in both closed and open conformations. Because the S3b moves together with the S4 domain in the paddle model, we tested the effects of deleting two negative charges or adding a positive charge to this region of the channel. We found that altering the S3b net charge does not modify the total gating charge involved in channel activation. We conclude that the S3b segment is always exposed to the external milieu of the Shaker K+ channel. Our results are incompatible with any model involving a large membrane displacement of segment S3b.
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