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

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

Research output: Contribution to journalArticle

14 Citations (Scopus)

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.

Original languageEnglish
Article number34614
JournalScientific reports
Volume6
DOIs
Publication statusPublished - 2016 Oct 7

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Nuclear Localization Signals
Cell Nucleus Active Transport
Isoflurophate
Galactosidases
Karyopherins
O-GlcNAc transferase
Threonine
Hydroxyl Radical
Cytosol
Serine
Amino Acids

All Science Journal Classification (ASJC) codes

  • General

Cite this

Seo, Hyeon Gyu ; Kim, Han Byeol ; Kang, Min Jueng ; Ryum, Joo Hwan ; Yi, Eugene C. ; Cho, Jin Won. / Identification of the nuclear localisation signal of O-GlcNAc transferase and its nuclear import regulation. In: Scientific reports. 2016 ; Vol. 6.
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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.",
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Identification of the nuclear localisation signal of O-GlcNAc transferase and its nuclear import regulation. / Seo, Hyeon Gyu; Kim, Han Byeol; Kang, Min Jueng; Ryum, Joo Hwan; Yi, Eugene C.; Cho, Jin Won.

In: Scientific reports, Vol. 6, 34614, 07.10.2016.

Research output: Contribution to journalArticle

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