GABARAP (GABA type A receptor-associated protein) is a ubiquitin-like modifier with dual roles in receptor trafficking and cellular degradation pathways. It mediates intracellular transport of GABA(A) receptors and coordinates their interaction with the cytoskeleton. Beyond its classical function, GABARAP is essential for autophagosomal maturation, particularly in later stages after LC3-family proteins initiate phagophore membrane elongation. It participates in selective autophagy of the endoplasmic reticulum through interaction with reticulophagy receptors, including TEX264, allowing ER remodeling and turnover under nutrient stress 1. GABARAP also regulates cytoskeletal organization and cell migration by promoting localization of the CUL3(KBTBD6/7) E3 ubiquitin ligase complex, which degrades TIAM1 and subsequently suppresses RAC1 signaling. Recent evidence reveals that GABARAP lipidation on STING vesicles activates the transcription factor TFEB, promoting lysosomal biogenesis and pathogen clearance independent of TBK1 23. During lysosomal damage, GABARAP recruitment regulates stress granule formation and mTOR inactivation through interaction with core stress response proteins 4. At damaged lysosomes, GABARAP also facilitates LRRK2 kinase activation via the CASM pathway, linking the protein to Parkinson's disease biology 5. These multifaceted functions position GABARAP as a critical hub coordinating autophagy, organellar quality control, and stress responses.