O-GlcNAcylation regulation of cellular signaling in cancer

O-GlcNAcylation is a post-translational modification occurring on serine/threonine residues of nuclear and cytoplasmic proteins, mediated by the enzymes OGT and OGA which catalyze the addition or removal of the UDP-GlcNAc moieties, respectively. Structural changes brought by this modification lead to alternations of protein stability, protein-protein interactions, and phosphorylation. Importantly, O-GlcNAcylation is a nutrient sensor by coupling nutrient sensing with cellular signaling. Elevated levels of OGT and O-GlcNAc have been reported in a variety of cancers and has been linked to regulation of multiple cancer signaling pathways. In this review, we discuss the most recent findings on the role of O-GlcNAcylation as a metabolic sensor in signaling pathways and immune response in cancer.

Automated summary

O-GlcNAcylation is a post-translational modification affecting protein stability, interactions, and phosphorylation, playing a crucial role in nutrient sensing and regulation of cancer signaling pathways. Its elevated levels have been linked to various cancers, making it a potential target for cancer treatment.