ATG2A is a lipid transfer protein that mediates autophagosome biogenesis through direct lipid transport from the endoplasmic reticulum (ER) to the isolation membrane (phagophore) 1. The protein tethers the ER to the phagophore edge and extracts phospholipids from ER exit sites, transferring them via ATG9A to the isolation membrane for expansion 12. ATG2A's lipid transfer activity is enhanced by WIPI1 and WDR45/WIPI4 through promotion of ATG2A association with phosphatidylinositol-3-phosphate-containing membranes 2. Beyond autophagosome biogenesis, ATG2A serves as a tether protein facilitating autophagosome-lysosome fusion in neural cells by interacting with SNARE proteins STX17, SNAP29, and VAMP8 3. The protein also regulates lipid droplet morphology and distribution 4, and remarkably transfers both phospholipids and triglycerides at lipid droplets 5. ATG2A function is dynamically regulated by S-palmitoylation; depalmitoylation during starvation-induced autophagy enables phagophore interaction and growth 6. Disease relevance includes chr11 kidney disease, where HCK-mediated ATG2A inhibition suppresses macrophage inflammation and renal fibrosis 7, and hepatocellular carcinoma, where hypoxia-induced YTHDF1 promotes ATG2A translation to enhance autophagy-dependent tumor progression 8. ATG2A transcriptional upregulation by E2F4 supports gastric cancer growth through zinc homeostasis maintenance 9.