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.

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

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.

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.

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

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

Detection of unbinding transitional states in the charybdotoxin first-order dissociation from a Kv-channel reveals that the bound neurotoxin wobbles, suggesting diverse intermediates and dissociation pathways in this protein–protein interaction.

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

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