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

Mobile and immobile GABA_A receptors in the C. elegans neuromuscular synapse are stabilized by two distinct protein scaffolds.

Extrasynaptic GABA_A receptors that emerge at puberty trigger adolescent synaptic pruning; pruning is prevented and cognition is impaired if the receptors are absent.

Presynaptic GABAB receptors are highly expressed and strongly suppress synaptic transmission at the input and output of hippocampal somatostatin interneurons.

Differential, state-dependent occupancy of three discrete binding sites on α₁β₃ GABA_A receptors determines whether a specific neurosteroid analogue potentiates or inhibits GABA-elicited currents or competitively antagonizes neurosteroid action.

The role of an important gating domain in linkage between the benzodiazepine drug-binding site and the pore gate in GABA_A receptors.

A novel GABAAR assembly pathway that promotes synaptic inhibition is established and provides a molecular explanation for how GABAARs with distinct subunit compositions display distinct subcellular distributions.

All perisomatic GABAergic synpases on hippocampal pyramidal cells have a similar GABA_A receptor subunit composition.

GABA-A receptors on dopamine neuron axons not only depolarize the membrane but also limit action potential propagation, an effect potentiated by positive allosteric modulators of GABA-A receptors like diazepam (Valium).

The sodium leak NALCN channel functions as a core effector of GABA-B and D2 receptors that is used along with GIRK channels to regulate action potential firing in dopamine neurons.