Regulation of glycosphingolipids biosynthesis by multi-spanning transmembrane protein family TMBIMs and their molecular machinery

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In this study, I examined new functions of FAIM2, a member of TMBIM family, based on my previous report that TMBIM family members reduced a glycosphingolipid, Gb3. Consequently, I found the following points: (1) FAIM2 interacted with NEDD4 E3 ligase family proteins through the N-terminal cytosolic domain of FAIM2; (2) an aspartate residue that is commonly observed in the multi-spanning membrane domains of TMBIM family was critical for two activities of FAIM2, the inhibitory activity to FAS-mediated apoptosis and Gb3-reducing activity. On the other hand, as a new tool to analyze glycolipid metabolism, I established a series of HeLa cell mutants deficient in sphingolipid-related genes including glucosylceramide synthase using TALENs.