Using a combination of genetics, metabolomics, biochemistry, and immunocytochemistry, Folick et al. explored the molecular mechanisms by which lysosomal LIPL-4 activation regulates aging in C. elegans. They show that worms overexpressing LIPL-4 live substantially longer than normal worms and produce increased amounts of several bioactive lipids, notably the fatty acid oleoylethanolamide (OEA). OEA is likely generated by the breakdown of more complex lipids in the lysosome by LIPL-4. LIPL-4–overexpressing worms also exhibit an increased amount of a fatty acid binding protein called lipidbinding protein-8 [(LBP-8); the human homolog is fatty acid binding protein (FABP)]. Elegantly coupling fluorescence imaging with mutations that alter protein targeting to the lysosome, Folick et al. demonstrate that LIPL-4 must reside within the lysosome to extend life span. By contrast, LBP-8 translocates from the lysosome into the nucleus to ensure increased longevity. As LBP-8 can directly bind to OEA, these results suggest that LBP-8 is a lipid chaperone assisting OEA entry into the nucleus (see the figure).