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Open AccessReview

O-GlcNAc Code’ Mediated Biological Functions of Downstream Proteins

by Linhong Zhao 1, Junaid Ali Shah 1, Yong Cai 1,2,3 and Jingji Jin 1,2,3,*
1
School of Life Sciences, Jilin University, Changchun 130012, China
2
National Engineering Laboratory for AIDS Vaccine, Jilin University, Changchun 130012, China
3
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
Molecules 2018, 23(8), 1967; https://doi.org/10.3390/molecules23081967
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)
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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MDPI and ACS Style

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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