ArticleThe Journal of general physiology2008
Alpha-scorpion toxin impairs a conformational change that leads to fast inactivation of muscle sodium channels.
Article in The Journal of general physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 92 citations in OpenAlex.
- Article
- ω-Grammotoxin-SIA inhibits voltage-gated Na+ channel currents.The Journal of general physiology · 2024Article
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- Analysis of the sensitization activity ofFrontiers in nutrition · 2024Article
- Eugenol and lidocaine inhibit voltage-gated NaFrontiers in pharmacology · 2024Article
- Differential regulation of cardiac sodium channels by intracellular fibroblast growth factors.The Journal of general physiology · 2023Article
- Historical Perspective of the Characterization of Conotoxins Targeting Voltage-Gated Sodium Channels.Marine drugs · 2023Review
- Structural and Functional Characterization of a Novel Scorpion Toxin that Inhibits NaFrontiers in pharmacology · 2022Article
- Allosteric interactions among voltage-sensor modules of sodium channels probed by scorpion toxin modifiers.Journal of neurobiology and physiology · 2022Article
- A Novel Spider Toxin Inhibits Fast Inactivation of the NaFrontiers in pharmacology · 2021Article
- Spider venom-derived peptide induces hyperalgesia in NaNature communications · 2020Article
- Effects of FGF14 and NaThe Journal of general physiology · 2019Article
- Molecular game theory for a toxin-dominant food chain model.National science review · 2019Article
- The tarantula toxin GxTx detains KThe Journal of general physiology · 2019Article
- Review
- Role of human Hv1 channels in sperm capacitation and white blood cell respiratory burst established by a designed peptide inhibitor.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Using voltage-sensor toxins and their molecular targets to investigate NaThe Journal of physiology · 2018Review
- Peptide ion channel toxins from the bootlace worm, the longest animal on Earth.Scientific reports · 2018Article
- Proteomic endorsed transcriptomic profiles of venom glands from Tityus obscurus and T. serrulatus scorpions.PloS one · 2018Article
- Three-dimensional Modelling of the Voltage-gated Sodium Ion Channel from Anopheles gambiae Reveals Spatial Clustering of Evolutionarily Conserved Acidic Residues at the Extracellular Sites.Current neuropharmacology · 2017Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Alpha-scorpion toxins bind in a voltage-dependent way to site 3 of the sodium channels, which is partially formed by the loop connecting S3 and S4 segments of domain IV, slowing down fast inactivation. We have used Ts3, an alpha-scorpion toxin from the Brazilian scorpion Tityus serrulatus, to analyze the effects of this family of toxins on the muscle sodium channels expressed in Xenopus oocytes. In the presence of Ts3 the total gating charge was reduced by 30% compared with control conditions. Ts3 accelerated the gating current kinetics, decreasing the contribution of the slow component to the ON gating current decay, indicating that S4-DIV was specifically inhibited by the toxin. In addition, Ts3 accelerated and decreased the fraction of charge in the slow component of the OFF gating current decay, which reflects an acceleration in the recovery from the fast inactivation. Site-specific fluorescence measurements indicate that Ts3 binding to the voltage-gated sodium channel eliminates one of the components of the fluorescent signal from S4-DIV. We also measured the fluorescent signals produced by the movement of the first three voltage sensors to test whether the bound Ts3 affects the movement of the other voltage sensors. While the fluorescence-voltage (F-V) relationship of domain II was only slightly affected and the F-V of domain III remained unaffected in the presence of Ts3, the toxin significantly shifted the F-V of domain I to more positive potentials, which agrees with previous studies showing a strong coupling between domains I and IV. These results are consistent with the proposed model, in which Ts3 specifically impairs the fraction of the movement of the S4-DIV that allows fast inactivation to occur at normal rates.
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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.