The cryo-electron microscopy structures of an LRRC8C chimera with native channel properties reveal the diverse oligomeric assembly and suggest that lipids may play a role in gating in volume-regulated anion channels.

The basis for small-molecule block, insights into gating, and an unexpected architectural role for the lipid membrane are revealed in structures of the volume regulated anion channel LRRC8A.

The homomeric structure of human SWELL1 (LRRC8A) provides insights into properties of a novel chloride channel family.

SWELL1 is required for basal, stretch, and flow-mediated endothelial AKT-eNOS signaling in vitro and protects against angiotensin-induced hypertension and diabetes-associated vascular dysfunction in vivo.

VRAC activation, observed with a FRET sensor of intracellular LRRC8-domains movement during gating and by fluorometry, requires plasma membrane localization and diacylglycerol signaling, but is independent of intracellular ionic strength.

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

LRRC8A is an essential component of a mechanoresponsive ion channel signaling complex that tunes skeletal muscle differentiation, muscle cell size, function and metabolic pathways to regulate adiposity and systemic glycemia.

LRRC23 is a radial spoke 3 head component essential for normal sperm motility and fertility in mammals.

The structure of a pannexin 1 uncovers the extracellular loops of pannexin 1 as important structural motifs for ion selectivity and channel inhibition.

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