CG32803 is the fly homolog of LDAF1 and influences lipid storage in vivo

The Seipin protein is a conserved key component in the biogenesis of lipid droplets (LDs). Recently, a cooperation between human Seipin and the Lipid droplet assembly factor 1 (LDAF1) was described. LDAF1 physically interacts with Seipin and the holocomplex safeguards regular LD biogenesis. The function of LDAF1 proteins outside mammals is less clear. In yeast, the lipid droplet organization (LDO) proteins, which also cooperate with Seipin, are the putative homologs of LDAF1. While certain functional aspects are shared between the LDO and mammalian LDAF1 proteins, the relationship between the proteins is under debate. Here, we identify the Drosophila melanogaster protein CG32803, which we re-named to dmLDAF1, as an insect member of this protein family. dmLDAF1 decorates LDs in cultured cells and in vivo and the protein is linked to the fly and mouse Seipin proteins. Altering the dmLDAF1 abundance affects LD size, number and overall lipid storage amounts. Our results suggest that the LDAF1 proteins thus fulfill an evolutionarily conserved function in the biogenesis and biology of LDs.

Automated summary

Seipin protein plays a key role in lipid droplets (LDs) biogenesis, with recent findings showing a cooperation between human Seipin and Lipid droplet assembly factor 1 (LDAF1). LDAF1 proteins may have an evolutionarily conserved function in LDs biogenesis, with certain functional aspects shared between LDO and mammalian LDAF1 proteins. The relationship between LDO and LDAF1 proteins is still under debate.