Earticle

초록

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 O-phosphorylation, and has surprisingly extensive cross talk with O-phosphorylation, where is serves as a nutrient/stress sensor to modulate signaling, transcription, and cytoskeletal functions. O-GlcNAcylated proteins in Drosophila were analyzed using 2D gel electrophoresis and MALDI/TOF-MS, and ATP synthase β was identified as a novel O-GlcNAcylated protein in Drosophila SL2 cell. F1F0 ATP synthase complex produces ATP from ADP in the presence of a proton gradient across mitochondrial membrane which is generated by electron transport of the respiration, and β subunit has ATPase activity. By immunoprecipiation and immunoblotting, 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. Hence 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.

저자

• Joo-hwan Ryum [ Department of Integrated OMICS for Biomedical Science, Yonsei University, Seoul, Korea ]
• Jin-won Cho [ Department of Integrated OMICS for Biomedical Science, Yonsei University, Seoul, Korea ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국당과학회 학술대회

• 간기

  연간

• 수록기간

  2006~2022

• 십진분류

  KDC 517 DDC 614