It has been reported that one downstreameffector produced from glucose is uridine diphosphate-N-acetly glucosamine(UDP-GlcNAc) via the hexoamine biosynthetic pathway (HBP). The dynamic cycle of addition and removal of O-linked-N-acetlyglucosamine (O-GlcNAc) to Ser/Thr residues is involved in regulating nuclear and cytoplasmic proteins. Nucleocytoplasmic O-GlcNAc transferase (ncOGT) adds a single GlcNAc onto hydroxyl groups of serine and threonine residues. Interestingly, O-GlcNAc glycosylation occurs in ncOGT as well and several putative sites have been reported mainly within TPR domain. However, the mechanism by which nuclear translocation of O-GlcNAc transferase is not clear. Here, we identified specific nuclear localization signals (NLS) in O-GlcNAc transferase that is required for nuclear transport. A 3 amino acid domain inserts a non-diffusible protein to the nucleus autonomously. Also, we show that ncOGT binds importin α proteins and the association between importin α proteins and ncOGT is interfered by O-GlcNAcylation on TPR domain. This ongoing effort would give us clear understanding of the key enzyme of O-GlcNAc metabolism.
저자
Hyeon Gyu Seo [ Department of Systems Biology, Yonsei University, Seodaemun-gu, Seoul, Korea ]
Ryum Joo Hwan [ Department of Systems Biology, Yonsei University, Seodaemun-gu, Seoul, Korea ]
Jin Won Cho [ Department of Systems Biology, Yonsei University, Seodaemun-gu, Seoul, Korea ]
본 학회는 화학, 생화학, 분자생물학, 미생물학, 식품공학, 의학, 약학, 유전공학 및 생물공학, 환경 및 기타 공업 등 전 분야의 탄수화물관련 이론과 기술을 연구 발전시키고 산학협동을 통해 이를 보급하여 국내 관련 산업의 발전 및 국민생활의 과학화에 기여하고자 하며, 이러한 목표와 비젼의 실현을 위해 회원들이 적극적인 참여와 활동을 전개하고자 한다.