earticle

영어

O-GlcNAcylation, the addition of β-N-acetylglucosamine(O-GlcNAc) to serine or threonine, is one of post-translational modification occurs on myriad proteins in nucleus and cytosol. It cycles on proteins with a time-scale similar to protein phosphorylation, and has surprisingly extensive cross talk with phosphorylation, where is serves as a nutrient/stress sensor to modulate signaling, transc ription, and cytoskeletal functions. O-GlcNAcylated proteins in Drosophila were analyzed using 2 D gel electrophoresis and MALDI/TOF-MS, and ATP synthase β was identified as a novel O-Gl cNAcylated protein in Drosophila SL2 cell. F1F0-ATPsynthase complex produces ATP from ADP in the presence of a proton gradient across mitochondrial membrane which is generated by electr on transport of the respiration, and β subunit has ATPase activity. By immunoprecipiation and i mmunoblotting, O-GlcNAcylation of ATP synthase β was confirmed. Interestingly, we found that O-GlcNAcylation of ATP synthase β is increased by nucleocytoplasmic O-GlcNAc transferase. H ence we will concentrate on demonstrating how the ATP synthase β is modified with O-GlcNAc and what the functional roles of O-GlcNAcylation on ATP synthase β are.