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Chemical Arsenal for the Study of O-GlcNAc

Department of Science Education-Chemistry Major, Daegu University, Gyeongbuk 712-714, Korea
Molecules 2011, 16(3), 1987-2022;
Received: 27 December 2010 / Revised: 3 February 2011 / Accepted: 15 February 2011 / Published: 28 February 2011
(This article belongs to the Special Issue Glycosides)
The concepts of both protein glycosylation and cellular signaling have been influenced by O-linked-β-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) on the hydroxyl group of serine or threonine residues. Unlike conventional protein glycosylation, O-GlcNAcylation is localized in the nucleocytoplasm and its cycling is a dynamic process that operates in a highly regulated manner in response to various cellular stimuli. These characteristics render O-GlcNAcylation similar to phosphorylation, which has long been considered a major regulatory mechanism in cellular processes. Various efficient chemical approaches and novel mass spectrometric (MS) techniques have uncovered numerous O-GlcNAcylated proteins that are involved in the regulation of many important cellular events. These discoveries imply that O-GlcNAcylation is another major regulator of cellular signaling. However, in contrast to phosphorylation, which is regulated by hundreds of kinases and phosphatases, dynamic O-GlcNAc cycling is catalyzed by only two enzymes: uridine diphospho-N-acetyl-glucosamine:polypeptide β-N-acetylglucosaminyl transferase (OGT) and β-D-N-acetylglucosaminidase (OGA). Many useful chemical tools have recently been used to greatly expand our understanding of the extensive crosstalk between O-GlcNAcylation and phosphorylation and hence of cellular signaling. This review article describes the various useful chemical tools that have been developed and discusses the considerable advances made in the O-GlcNAc field. View Full-Text
Keywords: phosphorylation; O-GlcNAcylation; OGT; OGA; chemical tools phosphorylation; O-GlcNAcylation; OGT; OGA; chemical tools
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Kim, E.J. Chemical Arsenal for the Study of O-GlcNAc. Molecules 2011, 16, 1987-2022.

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