TECPR1 is a tethering factor that mediates autophagosome maturation and selective autophagy through multiple mechanisms. Structurally, TECPR1 contains WD-repeat and PH domains that enable binding to ATG12-ATG5 conjugates and phosphatidylinositol lipids (PtdIns3P and PtdIns4P) on autophagosomal and lysosomal membranes 1. In canonical autophagy, TECPR1 recruits autophagosomes to lysosomes for fusion, a process essential for autophagy completion 1. Beyond canonical pathways, TECPR1 mediates noncanonical autophagy (CASM) by recognizing damage-induced sphingomyelin exposure on compromised membranes via its DysF domains, triggering ATG8 lipidation independent of ATG16L1 2. TECPR1 also repairs damaged lysosomes during energy stress by recruiting KIF1A to facilitate tubule formation and removal of compromised membrane regions, thereby protecting cells during metabolic crisis 3. In neurodegenerative contexts, TECPR1 promotes aggrephagy by recruiting LC3C-decorated autophagosomes to lysosomes, facilitating protein aggregate clearance 4. Clinically, TECPR1 shows potential as a therapeutic target: its downregulation associates with bladder cancer (urinary TECPR1 levels show 90% sensitivity and 81.9% specificity for cancer detection) 5, while overexpression ameliorates cognitive dysfunction in tau-pathology models by restoring autophagy flux 6.