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Molecules 2018, 23(11), 2858;

The Many Ways by Which O-GlcNAcylation May Orchestrate the Diversity of Complex Glycosylations

Unité de Glycobiologie Structurale et Fonctionnelle, Université de Lille, CNRS, UMR 8576, UGSF, 59000 Lille, France
Author to whom correspondence should be addressed.
Academic Editor: Franz-Georg Hanisch
Received: 14 September 2018 / Revised: 25 October 2018 / Accepted: 30 October 2018 / Published: 2 November 2018
(This article belongs to the Special Issue Functional Roles of Protein O-Glycosylation)
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Unlike complex glycosylations, O-GlcNAcylation consists of the addition of a single N-acetylglucosamine unit to serine and threonine residues of target proteins, and is confined within the nucleocytoplasmic and mitochondrial compartments. Nevertheless, a number of clues tend to show that O-GlcNAcylation is a pivotal regulatory element of its complex counterparts. In this perspective, we gather the evidence reported to date regarding this connection. We propose different levels of regulation that encompass the competition for the nucleotide sugar UDP-GlcNAc, and that control the wide class of glycosylation enzymes via their expression, catalytic activity, and trafficking. We sought to better envision that nutrient fluxes control the elaboration of glycans, not only at the level of their structure composition, but also through sweet regulating actors. View Full-Text
Keywords: O-GlcNAc; O-GlcNAcylation; OGT; O-GlcNAc transferase; OGA; O-GlcNAcase; glycosylation O-GlcNAc; O-GlcNAcylation; OGT; O-GlcNAc transferase; OGA; O-GlcNAcase; glycosylation

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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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Biwi, J.; Biot, C.; Guerardel, Y.; Vercoutter-Edouart, A.-S.; Lefebvre, T. The Many Ways by Which O-GlcNAcylation May Orchestrate the Diversity of Complex Glycosylations. Molecules 2018, 23, 2858.

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