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标题：The α/β-hydrolase domain-containing 4- and 5-related phospholipase Pummelig controls energy storage in Drosophila
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作者：Philip Hehlert ; Vinzenz Hofferek ; Philip Hehlert 等
期刊名称：JLR Papers In Press
印刷版ISSN：0022-2275
电子版ISSN：1539-7262
出版年度：2019
卷号：60
期号：8
页码：1365-1378
DOI：10.1194/jlr.M092817
出版社：American Society for Biochemistry and Molecular Biology
摘要：Triglycerides (TGs) are the main energy storage form that accommodates changing organismal energy demands. In Drosophila melanogaster , the TG lipase Brummer is centrally important for body fat mobilization. Its gene brummer ( bmm ) 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 ( ABHD4 ) and ABHD5 . In Drosophila , the pummelig ( puml ) gene encodes the single sequence-related protein to mammalian ABHD4/ABHD5 with unknown function. We generated puml 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 puml 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 Drosophila body fat storage and energy metabolism.
关键词：lipid and lipoprotein metabolism ; obesity ; storage diseases ; phospholipids/metabolism ; Malpighian tubules ; adipose triglyceride lipase ; Brummer ( Drosophila melanogaster adipose triglyceride lipase)