Gamma-aminobutyric acid type A receptor alpha-3 beta-2 gamma-2S subtype (GABA_A receptor α3β2γ2S)

The Gamma-aminobutyric acid type A (GABA_A) receptor α3β2γ2S subtype is a heteropentameric ligand-gated ion channel that serves as a primary mediator of fast inhibitory neurotransmission in the mammalian central nervous system (Olsen & Sieghart, 2008). It is typically composed of two α3 subunits, two β2 subunits, and one γ2S (short) subunit, which together form a pore selective for chloride ions (Sigel & Steinmann, 2012). Upon the binding of the neurotransmitter GABA, the receptor undergoes a conformational change that opens the channel, leading to chloride influx and subsequent hyperpolarization of the postsynaptic neuron (Rudolph & Knoflach, 2011). This specific subtype is highly expressed in the reticular nucleus of the thalamus and various brainstem nuclei, playing a crucial role in regulating sensorimotor gating and rhythmic neuronal activity (Atack, 2011). Pharmacologically, the α3β2γ2S subtype contains a benzodiazepine binding site at the α3/γ2 interface, making it a target for various anxiolytic and sedative-hypnotic drugs (Sigel & Ernst, 2018). Research into α3-selective modulators aims to develop treatments for anxiety and chronic pain that lack the profound sedative side effects typically associated with α1-containing GABA_A receptors (Engin et al., 2012).

Other names

GABRA3-GABRB2-GABRG2S receptorα3β2γ2S GABA-A receptorGABA(A) receptor subunit alpha-3/beta-2/gamma-2S complex

Positive allosteric modulation of the GABA-A receptor chloride channel, specifically at the benzodiazepine binding site located at the interface of the alpha-3 and gamma-2 subunits (Sigel & Ernst, 2018).