ArticleThe Journal of general physiology2013
Opening the shaker K+ channel with hanatoxin.
Article in The Journal of general physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- A Kv2 inhibitor combination reveals native neuronal conductances consistent with Kv2/KvS heteromers.eLife · 2025Article
- Article
- Neuronomodulation of Excitable Neurons.Neuroscience bulletin · 2024Review
- Peptide Toxins Targeting KV Channels.Handbook of experimental pharmacology · 2021Review
- KFrontiers in cellular neuroscience · 2020Review
- Article
- Spider Venom: Components, Modes of Action, and Novel Strategies in Transcriptomic and Proteomic Analyses.Toxins · 2019Review
- The tarantula toxin GxTx detains KThe Journal of general physiology · 2019Article
- Unlocking the gating mechanism of Kv2.1 using guangxitoxin.The Journal of general physiology · 2019Article
- Deglycosylation of Shaker KThe Journal of general physiology · 2018Article
- Heat activation is intrinsic to the pore domain of TRPV1.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The envenomation of general physiology throughout the last century.The Journal of general physiology · 2017Review
- Article
- Molecular Interactions between Tarantula Toxins and Low-Voltage-Activated Calcium Channels.Scientific reports · 2016Article
- Article
- Structural basis for the inhibition of voltage-dependent K+ channel by gating modifier toxin.Scientific reports · 2015Article
- Resin-acid derivatives as potent electrostatic openers of voltage-gated K channels and suppressors of neuronal excitability.Scientific reports · 2015Article
- Article
- Structural interactions of a voltage sensor toxin with lipid membranes.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Chemoselective tarantula toxins report voltage activation of wild-type ion channels in live cells.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Voltage-activated ion channels open and close in response to changes in membrane voltage, a property that is fundamental to the roles of these channels in electrical signaling. Protein toxins from venomous organisms commonly target the S1-S4 voltage-sensing domains in these channels and modify their gating properties. Studies on the interaction of hanatoxin with the Kv2.1 channel show that this tarantula toxin interacts with the S1-S4 domain and inhibits opening by stabilizing a closed state. Here we investigated the interaction of hanatoxin with the Shaker Kv channel, a voltage-activated channel that has been extensively studied with biophysical approaches. In contrast to what is observed in the Kv2.1 channel, we find that hanatoxin shifts the conductance-voltage relation to negative voltages, making it easier to open the channel with membrane depolarization. Although these actions of the toxin are subtle in the wild-type channel, strengthening the toxin-channel interaction with mutations in the S3b helix of the S1-S4 domain enhances toxin affinity and causes large shifts in the conductance-voltage relationship. Using a range of previously characterized mutants of the Shaker Kv channel, we find that hanatoxin stabilizes an activated conformation of the voltage sensors, in addition to promoting opening through an effect on the final opening transition. Chimeras in which S3b-S4 paddle motifs are transferred between Kv2.1 and Shaker Kv channels, as well as experiments with the related tarantula toxin GxTx-1E, lead us to conclude that the actions of tarantula toxins are not simply a product of where they bind to the channel, but that fine structural details of the toxin-channel interface determine whether a toxin is an inhibitor or opener.
Indexed as
Identifiers
What OpenQuestion holds
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.