Potassium ions enter and leave human sperm cells via a calcium-dependent ion channel that is also pH-independent.

Highly temperature-sensitive behavior of voltage-gated potassium channels provides a mechanistic model for how heat-activated TRP channels serve as temperature and pain sensors.

ZDHHC14 controls palmitoylation and axon initial segment targeting of PSD93 and Kv1-family potassium channels, events that are essential for normal neuronal excitability.

The mammalian potassium channel KCa3.1, which is important for T- and B-cell activation, is inhibited by cytoplasmic copper, mediated by a histidine residue (His358) that is phosphorylated to activate the channel.

The pseudokinase protein SCYL1 is an evolutionarily conserved enhancer of Slo2 potassium channel activity.

Type 1 potassium channels alter their composition and localisation to suppress hyper-excitability and neuropathic pain of injured sensory neurons.

Loss of potassium channel activity from fast-spiking interneurons increases their excitability leading to unexpectedly increased fast excitatory transmission and seizure susceptibility.

An integrative structural biology approach provides refined models of the KCNQ1-KCNE1 channel complex, which propose a new mechanism to explain how KCNE1 modulates KCNQ1 channel activation.

Tuning the strength of inter- and intra-subunit hydrogen bonds can control potassium flux across biological membranes.

Serotonin neurons in chronically isolated mice become less responsive to excitatory stimulation, but inhibiting a distinctive calcium-activated potassium channel can restore both neuronal activity and behavior.