Identification of the nuclear localisation signal of O-GlcNAc transferase and its nuclear import regulation View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-10-07

AUTHORS

Hyeon Gyu Seo, Han Byeol Kim, Min Jueng Kang, Joo Hwan Ryum, Eugene C. Yi, Jin Won Cho

ABSTRACT

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. More... »

PAGES

34614

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/srep34614

DOI

http://dx.doi.org/10.1038/srep34614

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1019709382

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27713473


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