Review summarizes O-GlcNAcylation's role in regulating tumor progression and immune responses, suggesting it as a therapeutic target.
O-GlcNAcylation is a dynamic post-translational modification of serine/threonine residues in proteins that modulates cellular activities by influencing the function of protein substrates, including their cellular localization, stability, and protein-protein interactions. The hexosamine biosynthesis pathway (HBP) utilizes various metabolites to synthesize uridine diphosphate N-acetylglucosamine, which serves as the substrate for O-GlcNAcylation. Metabolic reprogramming of tumors modulates HBP flux, thereby influencing O-GlcNAcylation levels. O-GlcNAcylation plays a pivotal role in regulating immune signaling pathways and their targets. Consequently, O-GlcNAcylation may act as a central node linking metabolic reprogramming and immune evasion. In this review, we summarize the current progress in understanding the role of O-GlcNAcylation in immunometabolism and explore how O-GlcNAcylation serves as a metabolic-immune translator that regulates tumor progression and therapeutic responses. Furthermore, we discuss the potential of O-GlcNAcylation as a therapeutic target, providing a promising new approach for cancer treatment.
No takes yet. Share an insight, caveat, or question.
Zhao et al. (2026) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: