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.
Phosphorylation of a highly conserved serine residue is a physiological response of Escerichia coli to environmental potassium levels that inhibits transport by KdpFABC to maintain cellular homeostasis.
Oligodendrocytes in white matter use Kir4.1 inwardly rectifying potassium channels to prevent extracellular potassium accumulation, enabling neurons to sustain repetitive firing and limiting the initiation of seizures.
The structure of the potassium-chloride cotransporter KCC4 provides insight into the basis of ion specificity, transport stoichiometry, and activity regulation for a broadly physiologically and clinically important transporter family.
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.
Expression of the isolated voltage sensing domain significantly alters its structural conformation as well as its gating kinetics, indicating the importance of studying the biological assembly in its entirety.