Human O-GlcNAcase (OGA) is the unique enzyme responsible for the hydrolysis of O-GlcNAcylation, an essential protein glycosylation that modulates the function of numerous cellular proteins in response to nutrient and stress. Dysregulation of OGA has been linked to many diseases, and there is a widespread interest in understanding how OGA’s function and substrate specificity is regulated. We previously determined the crystal structures of a human OGA and discovered that the substrate-binding cleft of OGA could contribute to its substrate recognition. In this talk, I will present our quantitative analysis of the protein substrates and networks of OGA, as well as biochemical and cellular characterizations, which led to the discovery of a new pathway linking OGA to cancer.

New pathway linking OGA to cancer

2019 Fall National Meeting

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