Ceramide phosphoethanolamine biosynthesis in Drosophila is mediated by a unique ethanolamine phosphotransferase in the golgi lumen

Abstract

Background: Many invertebrates contain ceramide phosphoethanolamine (CPE) rather than sphingomyelin as key membrane component. Results: Insect-specific CPE synthase belongs to a novel branch of CDP-alcohol phosphotransferases with unique membrane topology. Conclusion: CPE production is catalyzed by a CDP-ethanolamine:ceramide ethanolamine phosphotransferase in the Golgi lumen. Significance: Identification of CPE synthase provides a novel opportunity to elucidate the biological role of an enigmatic but widespread sphingolipid. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.