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Updated: Jan 28, 2026

Using an α-Bungarotoxin Binding Site Tag to Study GABA A Receptor Membrane Localization and Trafficking
Published on: March 28, 2014
Molecular constituents and localization of the ionotropic GABA receptor complex in vivo
1Department of Cellular and Molecular Physiology, Department of Neuroscience, Yale University School of Medicine, New Haven, CT 06510, United States.
Abstract:
The ionotropic GABA receptor (GABAAR) mediates fast inhibition in the brain. The GABAAR 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 GABAARs, 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 GABAARs remain unsolved. A reinvestigation of native GABAAR 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.
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