GABARAPL1: is a ubiquitin-like protein that is a constituent of the ATG8-conjugation system, one of two evolutionarily conserved phosphatidylethanolamine conjugation systems necessary for the formation of the autophagosome. The human ATG8 system includes seven ubiquitin-like light chain proteins (LCPs) that are homologs of yeast LC3: MAP1LC3A, -B, -C, GABARAP, GABARAPL1, -2, and -3. Pro-LCPs are cleaved by ATG4B to expose a C-terminal glycine residue, the cytosolic LCP-I form. The exposed C-terminus is conjugated to the head group amine of phosphatidylethanolamine (PE) through an amide bond by a sequence of ubiquitination-like reactions that involves an E1 (ATG7), an E2 (ATG3), and an E3 (a complex including ATG5, ATG12, and ATG16L). The PE-congugated form (LCP-II) is tightly associated with the autophagosomal membrane. The LCP-II forms can also be delipidated by the ATG4 proteases: most of the LCPs are delipidated and liberated from the membrane before autophagosomes fuse with lysosomes. Increases cell-surface expression of kappa-type opioid receptor through facilitating anterograde intracellular trafficking of the receptor. Belongs to the MAP1 LC3 family. Interacts with GABRG2 and beta-tubulin. Interacts with KOR-1.
Protein type: Autophagy; Adaptor/scaffold; Ubiquitin-like modifier; Vesicle; Microtubule-binding
Chromosomal Location of Human Ortholog: 12p13.2
Cellular Component: autophagic vacuole; cytoplasmic vesicle membrane; cytosol; dendrite cytoplasm; endoplasmic reticulum; Golgi apparatus; intracellular; microtubule; mitochondrion
Molecular Function: beta-tubulin binding; GABA receptor binding; protein binding; Tat protein binding; ubiquitin protein ligase binding
Biological Process: autophagic vacuole formation; cellular response to nitrogen starvation; macroautophagy; mitochondrion degradation
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