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MPIase is a glycolipid that is involved in membrane protein integration. Despite evaluation of its functions  in vitro , the lack of information on MPIase biosynthesis hampered verification of its involvement  in vivo . In this study, we found that depletion of CdsA, a CDP-diacylglycerol synthase, caused not only a defect in phospholipid biosynthesis but also MPIase depletion with accumulation of the precursors of both membrane protein M13 coat protein and secretory protein OmpA. Yeast Tam41p, a mitochondrial CDP-diacylglycerol synthase, suppressed the defect in phospholipid biosynthesis, but restored neither MPIase biosynthesis, precursor processing, nor cell growth, indicating that MPIase is essential for membrane protein integration and therefore for cell growth. Consistently, we observed a severe defect in protein integration into MPIase-depleted membrane vesicles  in vitro . Thus, the function of MPIase as a factor involved in protein integration was proven  in vivo  as well as  in vitro . Moreover, Cds1p, a eukaryotic CdsA homologue, showed a potential for MPIase biosynthesis. From these results, we speculate the presence of a eukaryotic MPIase homologue.

CdsA is involved in biosynthesis of glycolipid MPIase essential for membrane protein integration in vivo