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Gamma-aminobutyric acid receptor-associated protein-like 1 (GABARAPL1) is a ubiquitin-like protein involved in autophagy and receptor trafficking. Highly conserved across species, it belongs to the GABARAP/Atg8 protein family and is essential for autophagic vacuole formation and regulation of mitochondrial quality. GABARAPL1 interacts with the GABA(A) receptor and kappa opioid receptor, modulating their trafficking to the plasma membrane[1][2][3][4]. Experimentally, decreased GABARAPL1 impairs autophagic flux, increases cell proliferation and invasion (notably in breast cancer models), and disturbs mitochondrial homeostasis[1]. GABARAPL1 also plays a tumor suppressor role, and its reduced expression is linked to more aggressive cellular phenotypes and altered mitochondrial metabolism in certain cancers[1]. Additionally, changes in GABARAPL1 expression are observed in neurodegenerative and muscular diseases, reflecting its role in cellular response to stress and protein/organelle turnover[1][4]. No clinical drugs directly target GABARAPL1 at this time, but the protein represents a key node in autophagy regulation and disease-related cellular processes.
Not drug-targeted at present; biologically, modulates receptor trafficking and autophagic degradation
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