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Hyeon Gyu Seo,Han Byeol Kim,Min Jueng Kang,Joo Hwan Rym,Eugene C. Yi,Jin Won Cho 한국당과학회 2016 한국당과학회 학술대회 Vol.2016 No.07
Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues. Although the cellular localisation of OGT is important to regulate a variety of cellular processes, the molecular mechanisms regulating the nuclear localisation of OGT is unclear. Here, we characterised three amino acids (DFP; residues 451–453) as the nuclear localisation signal of OGT and demonstrated that this motif mediated the nuclear import of non-diffusible β-galactosidase. OGT bound the importin α5 protein, and this association was abolished when the DFP motif of OGT was mutated or deleted. We also revealed that O-GlcNAcylation of Ser389, which resides in the tetratricopeptide repeats, plays an important role in the nuclear localisation of OGT. Our findings may explain how OGT, which possesses a NLS, exists in the nucleus and cytosol simultaneously.
The mechanism and signal for the nuclear import of O-GlcNAc transferase
Hyeon Gyu Seo,Han Byeol Kim,Min Jueng Kang,Joo Hwan Rym,Eugene C. Yi,Jin Won Cho 한국당과학회 2016 한국당과학회 학술대회 Vol.2016 No.01
Uridine diphosphate-N-acetyl glucosamine, generated from glucose via the hexosamine biosynthetic pathway, is a substrate for O -linked-N-acetylglucosamine (O -GlcNAc). Addition and removal of O -linked-N-acetylglucosamine to Ser/Thr residues is a dynamic cycle and is involved in the regulation of nuclear and cytoplasmic proteins. Nucleocytoplasmic O -GlcNActransferase (OGT) attaches a single GlcNAc onto hydroxyl groups of serine and threonine residues. Although the cellular localization of OGT is important to regulate a variety of cellular processes, the molecular mechanism regulating the nuclear localization of OGT is unclear. Here, we characterized the NLS motif in OGT and this motif is required for the nuclear import of non-diffusible β -galactosidase. OGT bound the importin α5 protein, and this association was abolished when the NLS motif of ncOGT was mutated or deleted. We also revealed that O -GlcNAcylation on tetratricopeptide repeats (TPR) plays an important role in nuclear localization of OGT. Our finding suggests the mechanism behind how OGT can be localized in the nucleus and cytosol simultaneously.