ArticleNature communications2019
Mutation of a single residue promotes gating of vertebrate and invertebrate two-pore domain potassium channels.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Mechanisms of intracellular pH gating and local anesthetic inhibition of the two-pore domain KProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Gating crosstalk in potassium channels.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Equivalent gain-of-function variants in KCNK3 and KCNK9 and their contribution to distinct TASK K2P channelopathies.The Journal of general physiology · 2026Article
- Gating shift to an ohmic mode of TREK-1 channel induced by docosahexaenoic acid.Biophysical journal · 2026Article
- Structural basis for proton inhibition of the two-pore domain KStructure (London, England : 1993) · 2026Article
- The TWK-26/KCNK3 potassium channel and FLR-4 protein kinase coordinate nutrient absorption in the C. elegans intestine.Genetics · 2026Article
- Insights into the structure and modulation of human TWIK-2.Nature communications · 2026Article
- Light-induced analgesia provides a drug-free optical method for pain relief via activation of TRAAK kNature communications · 2026Article
- Structure of the human KNature structural & molecular biology · 2025Article
- Effective polarization in potassium channel simulations: Ion conductance, occupancy, voltage response, and selectivity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- BiallelicBrain communications · 2025Article
- Functional validation of human SK channels variants causing NEDMAB and Zimmermann-Laband syndrome-3 inBrain communications · 2025Article
- Two K2P Channels, TWK-46 and TWK-26 do not affectmicroPublication biology · 2025Article
- Cannabinoid inhibition of mechanosensitive KbioRxiv : the preprint server for biology · 2024Article
- Constitutive sodium permeability in aProceedings of the National Academy of Sciences of the United States of America · 2024Article
- A leak KPNAS nexus · 2024Article
- Structure of the human KbioRxiv : the preprint server for biology · 2024Article
- Wnt-Ror-Dvl signalling and the dystrophin complex organize planar-polarized membrane compartments in C. elegans muscles.Nature communications · 2024Article
- A tonically active master neuron modulates mutually exclusive motor states at two timescales.Science advances · 2024Article
- Natural variation in theeLife · 2024Article
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Authors and funding
13 authors.
Funding
Abstract
Mutations that modulate the activity of ion channels are essential tools to understand the biophysical determinants that control their gating. Here, we reveal the conserved role played by a single amino acid position (TM2.6) located in the second transmembrane domain of two-pore domain potassium (K2P) channels. Mutations of TM2.6 to aspartate or asparagine increase channel activity for all vertebrate K2P channels. Using two-electrode voltage-clamp and single-channel recording techniques, we find that mutation of TM2.6 promotes channel gating via the selectivity filter gate and increases single channel open probability. Furthermore, channel gating can be progressively tuned by using different amino acid substitutions. Finally, we show that the role of TM2.6 was conserved during evolution by rationally designing gain-of-function mutations in four Caenorhabditis elegans K2P channels using CRISPR/Cas9 gene editing. This study thus describes a simple and powerful strategy to systematically manipulate the activity of an entire family of potassium channels.
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