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Updated: Jun 3, 2026

Using an α-Bungarotoxin Binding Site Tag to Study GABA A Receptor Membrane Localization and Trafficking
Published on: March 28, 2014
Autophagic Pathway on GABARAP Involved in GABAA Receptor Trafficking
Mengqi Zhou1, Wenjing Shi1, Haoran Li2
1Medical School, Kunming University of Science and Technology, The Affiliated Hospital of Kunming University of Science and Technology, The First People's Hospital of Anning, Kunming University of Science and Technology, 727 Jingming South Road, Chenggong District, Kunming, 650500, Yunnan, China.
Abstract:
The formation of lipidated Gamma-Aminobutyric Acid Receptor-Associated Protein (GABARAP), which is a crucial subfamily in the Autophagy-associated protein 8 (Atg8) group, not only requires the intricate collaboration of other autophagy-related proteins, but acts to necessarily promote the conduction of autophagy and Gamma-Aminobutyric Acid (GABA) A Receptor (GABAAR) trafficking. The molecular pathway on the formation of GABARAP is same as LC3-II, in which GABARAP is activated through Autophagy Activating Kinase 1 (ULK-1), Atg12-Atg5-Atg16L1 and Atg 4, whereas Rapamycin Complex 1 (mTORC1) and AMP-activated protein kinase (AMPK) inhibit Ulk1. The lipidated GABARAP interacts with molecules related to the synapse and regulates GABAAR clustering through interactions with postsynaptic scaffolding proteins, such as gephyrin and Ankyrin. GABARAP plays roles in regulating synaptic functions besides autophagy.
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