The autophagy pathway targets cellular material destined for degradation by enclosing it in a double-membraned vesicle called the autophagosome, which after maturation fuses with a lysosome. The progression of autophagy relies on the recruitment of membrane and autophagy-related (ATG) proteins, including the lipid scramblase ATG9A. Moreover, autophagy intersects with endocytic networks, but less is known with regard to how trafficking of proteins and lipids between these pathways occurs, and how it influences autophagic flux. In this study, Harald Stenmark and colleagues (Ravussin et al., 2021) set out to investigate the trafficking of ATG9A from endolysosomes. They first show that the phosphatidylinositol 3-phosphate (PI3P)-binding protein sorting nexin-4 (SNX4), which regulates protein trafficking in the endosomal network, partially colocalises with ATG9A at endolysosomes and early endosomes. In SNX4-depleted cells, ATG9A localisation increased on endolysosomal structures and autolysosomes but decreased on early-endosomal structures when autophagy was induced by starvation, indicating a role for SNX4 in trafficking of ATG9A during autophagy. Furthermore, SNX4 depletion inhibited autophagic flux in amino acid-starved cells. Taken together, these results suggest that by promoting ATG9A recycling from endolysosomes and autolysosomes, SNX4 prevents the exhaustion of the available ATG9A pool and thus helps to sustain autophagy.