A potassium channel, as a nonconducting function, organizes compartmentalized neuronal calcium signaling microdomains via structural and functional coupling of plasma membrane and endoplasmic reticulum calcium channels.
Cryo-EM structures of the gating cycle of bestrophin reveal the molecular underpinnings of activation and inactivation gating in this calcium-activated chloride channel and reveal a surprisingly wide pore.
The small glycine residue in the Cav selectivity filter is an overlooked feature that determines Ca2+ selectivity and provides new insight into the Ca2+ selectivity mechanism conserved from prokaryotes to eukaryotes.
Ion conduction in the calcium-activated chloride channel TMEM16A is directly regulated by calcium, which binds to a site close to the pore thereby shaping the electrostatics at its intracellular entrance.
A cationic molecule derived from an uncharged Cav2.2 calcium channel inhibitor powerfully inhibits both sodium and calcium channels with extracellular application and inhibits both pain and neurogenic inflammation.
The activation of small-conductance calcium-activated potassium channels in spines by action potentials regulates the induction of spike-timing dependent synaptic plasticity during low-frequency single action potential–EPSP pairing.