Molecular constituents and localization of the ionotropic GABA receptor complex in vivo

Abstract

The ionotropic GABA receptor (GABA A R) mediates fast inhibition in the brain. The GABA A R pore-forming (α, β, and non-α/β) subunits were isolated approximately 30 years ago and have since been the focus of extensive studies. As a result, many properties of GABA A Rs, including subunit assembly and channel and pharmacological properties, have been discovered. However, several of the underlying mechanisms such as the process for the synaptic localization of GABA A Rs remain unsolved. A reinvestigation of native GABA A R complexes in the brain and primary neurons identified two major molecular constituents, namely, the transmembrane GARLH/LHFPL protein family and the inhibitory synaptic protein neuroligin 2. This identification of the principal components of native receptor complexes may provide new mechanistic insight on receptor regulation.