Hyeon Gyu Seo, Joo Hwan Ryum, Han Byeol Kim, Jin Won Cho
언어
영어(ENG)
URL
https://www.earticle.net/Article/A212738
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원문정보
초록
영어
It has been reported that one of the downstream molecules generated from glucose is uridine diphosphate-N-acetly glucosamine(UDP-GlcNAc) via the hexoamine biopsynthetic 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 itself as well. O-GlcNAcylation on N-terminal domain of tetratricopeptide (TPR) repeats plays an important role in nuclear localization of ncOGT. Specific nuclear localization signals (NLS) in ncOGT has not been identified. We characterized the three amino acid motif as NLS because this motif is required for the nuclear import of non-diffusible β-galactosidase. Also, we show that ncOGT binds kayropherin α proteins, and the association between kayopherin α proteins and ncOGT is interfered by O-GlcNAcylation on TPR domain. Our finding suggests the mechanism how ncOGT can be localized in the nucleus and cytosol at the same time. Therefore our data may contribute to better understanding of the key enzyme of O-GlcNAc metabolism.
저자
Hyeon Gyu Seo [ Department of Integrated OMICS for Biomedical Science Yonsei University ]
Joo Hwan Ryum [ Department of Integrated OMICS for Biomedical Science Yonsei University ]
Han Byeol Kim [ Department of Integrated OMICS for Biomedical Science Yonsei University ]
Jin Won Cho [ Department of Integrated OMICS for Biomedical Science Yonsei University ]
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.