The role of glucose metabolism and O-GlcNAc glycosylation in the regulation of immunity
OGlcNAc glycosylation involves addition of a single sugar, β-N-acetylglucosamine, to serine or threonine residues of proteins. It is a unique type of glycosylation found on nuclear and cytoplasmic proteins. The addition and removal of OGlcNAc is catalysed by OGlcNAc transferase (OGT) and OGlcNAse (OGA) respectively. It is a rapidly reversibly modification akin to phosphorylation. Indeed, OGlcNAc glycosylation occurs in dynamic interplay with phosphorylation, either on the same or adjacent residues. The cross-talk between these two modifications in turn regulates various cellular processes. We are characterising the function of OGlcNAc glycosylation in immune cells by identifying changes in patterns of glycosylation in different metabolic states and upon encounter of pathogens. The function of glycosylated proteins will be further studied to understand the relevance of their OGlcNAc status in various immune cell activities.
Dr Nishma Gupta
Professor Jose Villadangos
Professor Malcolm McConville (University of Melbourne)
Dr Justine Mintern (University of Melbourne)
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