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Molecules 2018, 23(8), 1967;

O-GlcNAc Code’ Mediated Biological Functions of Downstream Proteins

School of Life Sciences, Jilin University, Changchun 130012, China
National Engineering Laboratory for AIDS Vaccine, Jilin University, Changchun 130012, China
Key Laboratory for Molecular Enzymology and Engineering, the Ministry of Education, Jilin University, Changchun 130012, China
Author to whom correspondence should be addressed.
Academic Editors: Franz-Georg Hanisch and Isabelle Breloy
Received: 17 July 2018 / Revised: 31 July 2018 / Accepted: 4 August 2018 / Published: 6 August 2018
(This article belongs to the Special Issue Functional Roles of Protein O-Glycosylation)
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As one of the post-translational modifications, O-linked β-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) often occurs on serine (Ser) and threonine (Thr) residues of specific substrate cellular proteins via the addition of O-GlcNAc group by O-GlcNAc transferase (OGT). Maintenance of normal intracellular levels of O-GlcNAcylation is controlled by OGT and glycoside hydrolase O-GlcNAcase (OGA). Unbalanced O-GlcNAcylation levels have been involved in many diseases, including diabetes, cancer, and neurodegenerative disease. Recent research data reveal that O-GlcNAcylation at histones or non-histone proteins may provide recognition platforms for subsequent protein recruitment and further initiate intracellular biological processes. Here, we review the current understanding of the ‘O-GlcNAc code’ mediated intracellular biological functions of downstream proteins. View Full-Text
Keywords: post-translational modifications; O-GlcNAcylation; OGT; OGA post-translational modifications; O-GlcNAcylation; OGT; OGA

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Zhao, L.; Shah, J.A.; Cai, Y.; Jin, J. ‘O-GlcNAc Code’ Mediated Biological Functions of Downstream Proteins. Molecules 2018, 23, 1967.

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