ArticleScientific reports2016
Molecular Interactions between Tarantula Toxins and Low-Voltage-Activated Calcium Channels.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- KvThe Journal of physiology · 2025Article
- Article
- µ-Theraphotoxin Pn3a inhibition of CaeLife · 2022Article
- Multitarget nociceptor sensitization by a promiscuous peptide from the venom of the King Baboon spider.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Cyclic Peptides as T-Type Calcium Channel Blockers: Characterization and Molecular Mapping of the Binding Site.ACS pharmacology & translational science · 2021Article
- Gating modifier toxins isolated from spider venom: Modulation of voltage-gated sodium channels and the role of lipid membranes.The Journal of biological chemistry · 2018Article
- Coupling between an electrostatic network and the ZnThe Journal of general physiology · 2018Article
- Using voltage-sensor toxins and their molecular targets to investigate NaThe Journal of physiology · 2018Review
- The Drosophila Gr28bD product is a non-specific cation channel that can be used as a novel thermogenetic tool.Scientific reports · 2018Article
- Lengths of the C-Terminus and Interconnecting Loops Impact Stability of Spider-Derived Gating Modifier Toxins.Toxins · 2017Article
- Insect-Active Toxins with Promiscuous Pharmacology from the African Theraphosid Spider Monocentropus balfouri.Toxins · 2017Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Few gating-modifier toxins have been reported to target low-voltage-activated (LVA) calcium channels, and the structural basis of toxin sensitivity remains incompletely understood. Studies of voltage-gated potassium (Kv) channels have identified the S3b-S4 "paddle motif," which moves at the protein-lipid interface to drive channel opening, as the target for these amphipathic neurotoxins. Voltage-gated calcium (Cav) channels contain four homologous voltage sensor domains, suggesting multiple toxin binding sites. We show here that the S3-S4 segments within Cav3.1 can be transplanted into Kv2.1 to examine their individual contributions to voltage sensing and pharmacology. With these results, we now have a more complete picture of the conserved nature of the paddle motif in all three major voltage-gated ion channel types (Kv, Nav, and Cav). When screened with tarantula toxins, the four paddle sequences display distinct toxin binding properties, demonstrating that gating-modifier toxins can bind to Cav channels in a domain specific fashion. Domain III was the most commonly and strongly targeted, and mutagenesis revealed an acidic residue that is important for toxin binding. We also measured the lipid partitioning strength of all toxins tested and observed a positive correlation with their inhibition of Cav3.1, suggesting a key role for membrane partitioning.
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