원문정보
초록
영어
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.