Abstract: Human O-GlcNAcase (OGA) is the unique enzyme that controls the hydrolysis of O-GlcNAcylation, an essential protein glycosylation that modulates an enormous number of intracellular proteins. Aberrant OGA expression has been observed in various types of diseases. However, lacking the information of conserved motif, how OGA controls its substrate specificity remains a mystery. Our previous study of human OGA crystal structure showed that the substrate-binding cleft of OGA could contribute to its substrate recognition. Here, we applied quantitative and bioinformatic analyses, as well as biochemical and cellular characterizations, to investigate the OGA substrates. Our study revealed a new functional role of OGA involved in signaling regulation.

Substrate dysregulation reveals a new regulatory role of OGA in cell signaling

2019 Fall National Meeting

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.