Journal
MOLECULES
Volume 23, Issue 11, Pages -Publisher
MDPI
DOI: 10.3390/molecules23112858
Keywords
O-GlcNAc; O-GlcNAcylation; OGT; O-GlcNAc transferase; OGA; O-GlcNAcase; glycosylation
Funding
- University of Lille
- Centre National de la Recherche Scientifique (CNRS)
- Marie Curie Innovative Training Networks (ITN) [H2020-EU.1.3.1, 676421]
- FRABio [FR 3688]
- Marie Curie Actions (MSCA) [676421] Funding Source: Marie Curie Actions (MSCA)
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available