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Structural and functional investigations identify a structural unit for ephaptic coupling in the heart, and provide the mechanistic basis for a novel strategy for the treatment of arrhythmias.

Variants in FGF13, associated with developmental and epileptic encephalopathies, alter neuronal excitability by affecting inhibitory neurons and by a sodium channel-independent mechanism.

Because nociceptors can achieve similar excitability using different sodium channel subtypes, it is difficult to know which channels are being used yet this information is critical for predicting if subtype-selective drugs will reduce pain.

High-speed calcium imaging from the axon initial segment shows that sodium channels are in part permeable to calcium ions.

External calcium regulates neuronal excitability via its actions on voltage-gated sodium channels but not by regulating NALCN via the calcium-sensing receptor.

Sodium ions but not protons induce defined helix movements in a sodium/proton antiporter and suggest a mechanism for Na + binding and transport.

The mRNA that encodes a Drosophila sodium channel enables neurons to adapt to acute temperature changes, via a mechanism independent of its protein-coding role.

The N-terminus of the FGF14b isoform promotes the inactivation of voltage-gated Na⁺ channels to regulate the resurgent Na⁺ channel current needed for high frequency action potentials.

The in-depth structural and functional work provide a deeper understanding as to how the epithelial sodium channel is a heteromeric ion channel that is regulated by Na⁺ and proteolysis.

Skin-associated bacteria underlie the production of a potent defensive neurotoxin in newts, impacting host physiology, molecular evolution, and predator-prey interactions in a coevolutionary arms race.