O-GlcNAcylation is the reversible modification of serine and threonine residues with <i>N</i>-acetylglucosamine (O-GlcNAc). This modification is attached by O-GlcNAc transferase (OGT) in the presence of sugar donor uridine diphosphate <i>N</i>-acetylglucosamine (UDP-GlcNAc), and can be removed by O-GlcNAcase (OGA). O-GlcNAcylation dynamically modulates the functions of over 1,000 intracellular proteins in transcription, translation, and signal transduction, among others.  Aberrant O-GlcNAcylation has been detected in many diseases such as cancer, diabetes, and Alzheimer’s disease. Hence, there is a significant interest in understanding how OGT and OGA regulate this modification on a broad range of substrates that lack apparent sequence motifs. This talk presents our new chemical biology and structural approaches to elucidate the molecular basis underlying the substrate binding and recognition of OGT and OGA.

Substrate recognition of reversible O-GlcNAcylation

255th National Meeting (2018)

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