cancer Metabolism O-GlcNAc OGT Signaling Transcription
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.
•The post-translational modification O-GlcNAcylation is found to be elevated in nearly all cancers.•This nutrient sensitive intracellular glycosylation can regulate a diverse set of cytosolic and nuclear proteins.•O-GlcNAcylation regulates signaling pathways including transcription, metabolic and immune regulation in cancer cells.•This review highlight most recent understanding of mechanisms by which O-GlcNAcylation regulates cancer cell signaling.