Nix is a selective autophagy receptor for mitochondrial clearance. The study identifies Nix as a mitochondrial protein that binds to LC3/GABARAP proteins, which are essential for autophagosomal membrane growth. Nix recruits GABARAP-L1 to damaged mitochondria through its amino-terminal LC3-interacting region (LIR). Ablation of the Nix:LC3/GABARAP interaction retards mitochondrial clearance in maturing murine reticulocytes. Nix functions as an autophagy receptor, mediating mitochondrial clearance after mitochondrial damage and during erythrocyte differentiation. Nix contains two potential LIRs, LIR-W35 and LIR-W139/143. Mutation of the conserved W35 residue in the N-terminal LIR ablates most of Nix binding to LC3A. The LIR-W35 is the main Atg8-family protein-interaction site in Nix, whereas LIR-W139/143 has a minor role. Nix recruits GABARAP-L1 to depolarized mitochondria, and this recruitment is partly dependent on the Nix-W35 LIR motif. Mitochondrial clearance is partly mediated by LIR-35. Nix deficiency in mice leads to impaired mitochondrial clearance during reticulocyte maturation. The study shows that Nix binds to LC3/GABARAP through LIR-W35, which is essential for mitophagy. Nix may mediate mitochondrial clearance in an LC3/GABARAP-independent or autophagy-independent manner. The study suggests that Nix-dependent recruitment of LC3/GABARAP proteins to mitochondria may be one factor in mediating membrane tethering and/or hemifusion of mitochondria with autophagosomes. Other signals, such as ubiquitination of mitochondrial proteins or interactions with lysosomal components, might mediate the full incorporation of mitochondria into autophagosomes. The study also highlights the importance of Nix in programmed mitochondrial clearance during reticulocyte maturation.Nix is a selective autophagy receptor for mitochondrial clearance. The study identifies Nix as a mitochondrial protein that binds to LC3/GABARAP proteins, which are essential for autophagosomal membrane growth. Nix recruits GABARAP-L1 to damaged mitochondria through its amino-terminal LC3-interacting region (LIR). Ablation of the Nix:LC3/GABARAP interaction retards mitochondrial clearance in maturing murine reticulocytes. Nix functions as an autophagy receptor, mediating mitochondrial clearance after mitochondrial damage and during erythrocyte differentiation. Nix contains two potential LIRs, LIR-W35 and LIR-W139/143. Mutation of the conserved W35 residue in the N-terminal LIR ablates most of Nix binding to LC3A. The LIR-W35 is the main Atg8-family protein-interaction site in Nix, whereas LIR-W139/143 has a minor role. Nix recruits GABARAP-L1 to depolarized mitochondria, and this recruitment is partly dependent on the Nix-W35 LIR motif. Mitochondrial clearance is partly mediated by LIR-35. Nix deficiency in mice leads to impaired mitochondrial clearance during reticulocyte maturation. The study shows that Nix binds to LC3/GABARAP through LIR-W35, which is essential for mitophagy. Nix may mediate mitochondrial clearance in an LC3/GABARAP-independent or autophagy-independent manner. The study suggests that Nix-dependent recruitment of LC3/GABARAP proteins to mitochondria may be one factor in mediating membrane tethering and/or hemifusion of mitochondria with autophagosomes. Other signals, such as ubiquitination of mitochondrial proteins or interactions with lysosomal components, might mediate the full incorporation of mitochondria into autophagosomes. The study also highlights the importance of Nix in programmed mitochondrial clearance during reticulocyte maturation.