ArticleThe Journal of general physiology2010
Position and motions of the S4 helix during opening of the Shaker potassium channel.
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 13 papers.
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Who cites it
13 citing papers in PubMed, 17 citations in OpenAlex.
- State-dependent motion of a genetically encoded fluorescent biosensor.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Deglycosylation of Shaker KThe Journal of general physiology · 2018Article
- Article
- Erythromelalgia mutation Q875E Stabilizes the activated state of sodium channel Nav1.7.The Journal of biological chemistry · 2015Article
- Shaker IR T449 mutants separate C- from U-type inactivation.The Journal of membrane biology · 2014Article
- Opening the shaker K+ channel with hanatoxin.The Journal of general physiology · 2013Article
- Article
- Structural interactions between lipids, water and S1-S4 voltage-sensing domains.Journal of molecular biology · 2012Article
- Neutralisation of a single voltage sensor affects gating determinants in all four pore-forming S6 segments of Ca(V)1.2: a cooperative gating model.Pflugers Archiv : European journal of physiology · 2012Article
- Article
- Functional interactions between residues in the S1, S4, and S5 domains of Kv2.1.European biophysics journal : EBJ · 2011Article
- An electrostatic potassium channel opener targeting the final voltage sensor transition.The Journal of general physiology · 2011Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The four voltage sensors in voltage-gated potassium (Kv) channels activate upon membrane depolarization and open the pore. The location and motion of the voltage-sensing S4 helix during the early activation steps and the final opening transition are unresolved. We studied Zn(2+) bridges between two introduced His residues in Shaker Kv channels: one in the R1 position at the outer end of the S4 helix (R362H), and another in the S5 helix of the pore domain (A419H or F416H). Zn(2+) bridges readily form between R362H and A419H in open channels after the S4 helix has undergone its final motion. In contrast, a distinct bridge forms between R362H and F416H after early S4 activation, but before the final S4 motion. Both bridges form rapidly, providing constraints on the average position of S4 relative to the pore. These results demonstrate that the outer ends of S4 and S5 remain in close proximity during the final opening transition, with the S4 helix translating a significant distance normal to the membrane plane.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.