Unité de Glycobiologie Structurale et Fonctionnelle, Université de Lille, CNRS, UMR 8576, UGSF, 59000 Lille, France.
Molecules. 2018 Nov 2;23(11):2858. doi: 10.3390/molecules23112858.
Unlike complex glycosylations, -GlcNAcylation consists of the addition of a single -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 -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.
与复杂的糖基化不同，-GlcNAcylation 由单个乙酰葡萄糖胺单元添加到靶蛋白的丝氨酸和苏氨酸残基上，并局限于核质和线粒体区室中。然而，有一些线索表明 -GlcNAcylation 是其复杂对应物的关键调节元件。在这方面，我们收集了迄今为止关于这种联系的报告证据。我们提出了不同的调节水平，包括对核苷酸糖 UDP-GlcNAc 的竞争，以及通过它们的表达、催化活性和运输来控制广泛的糖基化酶类。我们试图更好地设想营养物质通量控制聚糖的形成，不仅在其结构组成的水平上，而且还通过甜味调节因子。
