Structure of the triheteromeric α1β1γ2S GABAA receptor in complex with GABA illuminates the principles of receptor assembly and agonist binding.

The in-depth structural and functional work provide a deeper understanding as to how the epithelial sodium channel is a heteromeric ion channel that is regulated by Na⁺ and proteolysis.

Structures of the GluK2/K5 kainate receptor reveal the heteromer architecture and how the receptor organizes in apo, antagonist-bound, and desensitized states.

Reconstructed ancestral muscle-type acetylcholine receptor β-subunits readily form homopentameric ion channels that open spontaneously, and display functional hallmarks of the modern-day heteropentameric receptor despite being devoid of canonical agonist-binding sites.

Shank promotes functional coupling between CaV1 calcium channels and BK potassium channels.

Soluble fragments cleaved from the N-terminus of PC-1 activate the PC-1/PC-2 heteromeric polycystin channel, describing for the first time that the N-terminus itself is an endogenous ligand.

Synthetic polycystin proteins self-assemble as function channels when reconstituted in lipid vesicles.

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 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.

Two acid-sensing members of the degenerin/epithelial sodium channel family play distinct roles in controlling different aspects of rhythmic proton and calcium oscillations in the nematode intestine.