Single-particle cryo-electron microscopy reveals the first subnanometer structure of ATP-sensitive potassium (K_ATP) channels, which provides insight into the structural mechanisms of channel assembly and gating.

Structure-based approach identifies a K_ATP-binding compound that has the potential of normalizing insulin secretion in congenital hyperinsulinism by correcting defective K_ATP channel trafficking to the cell surface.

Diverse K_ATP channel inhibitors occupy a common binding pocket and stabilize an interaction between Kir6.2 and SUR1 to allosterically control gating and promote the assembly and trafficking of nascent channels.

Lactate is preferred to glucose as an energy substrate and exacerbates spiking activity in most neuron types of juvenile somatosensory cortex by closing ATP-sensitive potassium channels.

MgADP binding to the high-affinity 'consensus' ATPase active site of SUR1 and remodeling of the L0-loop (lasso region) overrides tonic ATP inhibition of KATP channels.

Altered activity of ATP-sensitive K⁺ channels underlies the metabolic seizure resistance produced by genetic manipulation of the BAD protein in mice.

A structure of a pancreatic ATP-sensitive potassium channel complex at 3.63Å resolution obtained by cryo-electron microscopy reveals how a commonly used anti-diabetic drug interacts with and inhibits the channel to stimulate insulin secretion.

Depletion of LRRC8A provides genetic evidence for the importance of Cl^- channels in NLRP3 activation.

Local ATP production by the plasma membrane-associated glycolytic enzyme pyruvate kinase is essential for the nutrient-dependent closure of the ATP-sensitive potassium channels that initiate insulin release from pancreatic β-cells.

Supporting cells in the cochlea change their shape in response to purinergic receptor activation, which influences hair cell excitability by altering potassium redistribution in the extracellular space.