Evidence That MonoADPRibosylation Of CtBP1Pubs Regulates Lipid Storage

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Mono-ADP-ribosylation is emerging as a significant posttranslational modification that modulates a variety of cell signaling pathways. Here, we present proof that mono-ADP-ribosylation of the transcriptional corepressor C terminal binding proteins, brefeldin A (BFA)-induced ADP-ribosylated substrate (CtBP1/BARS) regulates neutral lipid storage space in droplets that are surrounded by a monolayer of phospholipid and associated proteins. CtBP1/BARS can be an NAD-binding proteins that becomes ribosylated when cells are exposed to BFA. Both endogenous lipid droplets and droplets enlarged by oleate treatment are dropped after 12-h contact with BFA. Lipid reduction requires new protein synthesis, in fact it is blocked by multiple ribosylation inhibitors, nonetheless it isn't stimulated by disruption of the Golgi apparatus or the endoplasmic reticulum unfolded protein response. Small interfering RNA knockdown of CtBP1/BARS mimics the effect of BFA, and mouse embryonic fibroblasts derived from embryos that are deficient in CtBP1/BARS appear to be defective in lipid accumulation. We conclude that mono-ADP-ribosylation of CtBP1/Pubs inactivates its repressor function, that leads to the activation of genes that regulate neutral lipid storage space.


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