The α/β-hydrolase domain-containing 4- and 5-related phospholipase Pummelig controls energy storage in .

Triglycerides (TGs) are the main energy storage form that accommodates changing organismal energy demands. In , the TG lipase Brummer is centrally important for body fat mobilization. Its gene () encodes the ortholog of mammalian adipose TG lipase, which becomes activated by α/β-hydrolase domain-containing 5 (ABHD5/CGI-58), one member of the paralogous gene pair, α/β-hydrolase domain-containing 4 () and In , the () gene encodes the single sequence-related protein to mammalian ABHD4/ABHD5 with unknown function. We generated deletion mutant flies, that were short-lived as a result of lipid metabolism changes, stored excess body fat at the expense of glycogen, and exhibited ectopic fat storage with altered TG FA profile in the fly kidneys, called Malpighian tubules. TG accumulation in mutants was not associated with increased food intake but with elevated lipogenesis; starvation-induced lipid mobilization remained functional. Despite its structural similarity to mammalian ABHD5, Puml did not stimulate TG lipase activity of Bmm in vitro. Rather, Puml acted as a phospholipase that localized on lipid droplets, mitochondria, and peroxisomes. Together, these results show that the ABHD4/5 family member Puml is a versatile phospholipase that regulates body fat storage and energy metabolism.