Research Projects

O-GlcNAc 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 reversible 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. 

In this project we will characterise the function of OGlcNAc glycosylation in a type of immune cells (Denditic cells, DC) that play a critical role in immunity against infection and cancer. We will identify 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. Finally, we will characterize how OGT and OGA recognize their substrates and the mechanisms that regulate their function. These studies may allow us to design therapeutic drugs that target O-GlcNAc glycosylation to manipulate immune responses against pathogens or cancer.

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