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

ABSTRACT: 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.

SUBMITTER: Biwi J

PROVIDER: S-EPMC6278486 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature

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

Biwi James J Biot Christophe C Guerardel Yann Y Vercoutter-Edouart Anne-Sophie AS Lefebvre Tony T

Molecules (Basel, Switzerland) 20181102 11

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 leve ...[more]

PMID: 30400201

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