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<p>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 (GABA<sub>A</sub>R) 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 GABA<sub>A</sub>R clustering through interactions with postsynaptic scaffolding proteins, such as gephyrin and Ankyrin. GABARAP plays roles in regulating synaptic functions besides autophagy.</p>

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Autophagic Pathway on GABARAP Involved in GABAA Receptor Trafficking

  • 期刊论文

  • 发表日期：

    2026年6月1日

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  • Mengqi Zhou,
  • Wenjing Shi,
  • Haoran Li,
  • Jie Bai

摘要

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.