Drosophila Perilipin/ADRP homologue Lsd2 regulates lipid metabolism

Luís Teixeira*, Catherine Rabouille, Pernille Rørth, Anne Ephrussi, Nathalie F. Vanzo

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

121 Citations (Scopus)


Many cells store neutral lipids, as triacylglycerol and sterol esters, in droplets. PAT-domain proteins form a conserved family of proteins that are localized at the surface of neutral lipid droplets. Two mammalian members of this family, Perilipin and adipose differentiation-related protein, are involved in lipid storage and regulate lipolysis. Here, we describe the Drosophila PAT-family member Lsd2. We showed that Lsd2 is predominantly expressed in tissues engaged in high levels of lipid metabolism, the fat body and the germ line of females. Ultrastructural analysis in the germ line showed that Lsd2 localizes to the surface of lipid droplets. We have generated an Lsd2 mutant and described its phenotype. Mutant adults have a reduced level of neutral lipid content compared to wild type, showing that Lsd2 is required for normal lipid storage. In addition, ovaries from Lsd2 mutant females exhibit an abnormal pattern of accumulation of neutral lipids from mid-oogenesis, which results in reduced deposition of lipids in the egg. Consistent with its expression in the female germ line, we showed that Lsd2 is a maternal effect gene that is required for normal embryogenesis. This work demonstrates that Lsd2 has an evolutionarily conserved function in lipid metabolism and establishes Drosophila melanogaster as a new in vivo model for studies on the PAT-family of proteins.

Original languageEnglish
Pages (from-to)1071-1081
Number of pages11
JournalMechanisms of Development
Issue number9
Publication statusPublished - Sept 2003
Externally publishedYes


  • Drosophila
  • Fat body
  • Lsd2
  • Neutral lipid
  • Oogenesis
  • PAT-family
  • Triacylglycerol


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