Azzah Momenh
National Institutes of Health, USA
Title: Protein Stabilization and Purification by Targeted domain swapping
Biography
Biography: Azzah Momenh
Abstract
O-GlcNAcylation is a dynamic post-translational modification (PTM) of thousands of nuclear, cytoplasmic and mitochondrial proteins. This PTM targets serine or threonine residues of proteins, resulting in crosstalk with phosphorylation. The protein phosphorylation is controlled by many different kinases and phosphatases, whereas only two enzymes regulate O-GlcNAcylation. The addition of N-Acetylglucosamine onto target proteins is controlled by O-GlcNActransferase(OGT), while removal of this molecule is catalyzed by O-GlcNAcase(OGA). OGT uses UDP-GlcNAc(uridine diphosphate-N-acetylglucosamine) as a donor, which is the product of the hexosamine biosynthetic pathway. Since, nutrient derivative molecules, including glucose, glutamine, acetyl CoA and uridine diphosphate are all used to synthesize UDP-GlcNAc, O-GlcNAc cycling is susceptible to cellular nutrient levels. Therefore, O-GlcNAc is suggested to connect the nutrient status to cellular machineries. Moreover, O-GlcNAc cycling is involved in many fundamental functions, including transcription, translation, cell signaling, and protein trafficking. Deregulation of O-GlcNAcylation dynamics is involved in the etiology of diverse pathologies, such as type 2-diabetes, Alzheimer and cancers.