首页    期刊浏览 2024年11月30日 星期六
登录注册

文章基本信息

  • 标题:Identification of the nuclear localisation signal of O-GlcNAc transferase and its nuclear import regulation
  • 本地全文:下载
  • 作者:Hyeon Gyu Seo ; Han Byeol Kim ; Min Jueng Kang
  • 期刊名称:Scientific Reports
  • 电子版ISSN:2045-2322
  • 出版年度:2016
  • 卷号:6
  • 期号:1
  • DOI:10.1038/srep34614
  • 语种:English
  • 出版社:Springer Nature
  • 摘要: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.
国家哲学社会科学文献中心版权所有