The study identifies Nix as a selective autophagy receptor for mitochondrial clearance. Nix binds to LC3/GABARAP proteins through two potential LC3-interacting regions (LIRs), with LIR-W35 being the most important for binding. In cultured cells, Nix recruits GABARAP-L1 to damaged mitochondria via its LIR-W35. Ablation of the Nix/LC3/GABARAP interaction impairs mitochondrial clearance in maturing murine reticulocytes, suggesting that Nix functions as an autophagy receptor mediating mitochondrial clearance after damage and during erythrocyte differentiation. The findings highlight the role of Nix in the selective autophagy of mitochondria and provide insights into the molecular mechanisms underlying this process.The study identifies Nix as a selective autophagy receptor for mitochondrial clearance. Nix binds to LC3/GABARAP proteins through two potential LC3-interacting regions (LIRs), with LIR-W35 being the most important for binding. In cultured cells, Nix recruits GABARAP-L1 to damaged mitochondria via its LIR-W35. Ablation of the Nix/LC3/GABARAP interaction impairs mitochondrial clearance in maturing murine reticulocytes, suggesting that Nix functions as an autophagy receptor mediating mitochondrial clearance after damage and during erythrocyte differentiation. The findings highlight the role of Nix in the selective autophagy of mitochondria and provide insights into the molecular mechanisms underlying this process.