ArticleScience advances2025
The conductance of KCNQ2 and its pathogenic variants is determined by individual subunit gating.
Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Novel proteolytic post-translational modification in voltage-gated potassium channel KCNQ2.Scientific reports · 2026Article
- Two-step voltage-sensor activation of the human KNature communications · 2026Article
- Targeting ion channel dysregulation in tumors: emerging therapeutic opportunities.Trends in pharmacological sciences · 2026Review
- Voltage-sensing domains: structural and functional diversity.European biophysics journal : EBJ · 2025Review
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11 authors.
Funding
Abstract
KCNQ2 channel subunits form part of the M-current and underlie one of the major potassium currents throughout the human nervous system, regulating resting membrane potentials, shaping action potentials, and impeding repetitive neuronal firing. However, how individual subunits within tetramers control channel functionality remains unresolved. Here, we investigate (i) whether opening of KCNQ2 channels requires a concerted step or can result from independent subunit activation and (ii) how individual subunits regulate gate opening and conductance. The E140R mutation in the S2 segment prevents activated voltage sensor conformations, but concatemeric constructs containing up to three E140R subunits retain KCNQ2-like currents. The underlying single-channel currents show subconductance levels resulting from limitations in inner gate dimensions, determined by the number of activated subunits and their spatial arrangement. Channel opening is allosteric and requires activation of only a single subunit, which can accentuate the influence of clinically relevant heterozygous mutations at threshold voltages.
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