Dr. Elsa Garcin
UMBC, Dept. of Chemistry
From housekeeping to moonlighting: the many faces of glyceraldehyde-3-phosphate dehydrogenase
Glyceraldehyde-3-phosphate dehydrogenase is best known for its key role in glycolysis, and because it is often used as a model protein in enzyme kinetics and as a control for gene or protein analyses. Mounting evidence has shown that this “housekeeping” enzyme is in fact a multifunctional protein that can perform a wide range of functions in the cell. GAPDH is ubiquitously expressed in mammalian cells and has been found in most subcellular compartments. To date, studies have demonstrated the involvement of this protein in membrane fusion, tubulin polymerization, nuclear tRNA export, apoptosis, autophagy, nucleic acid binding, DNA replication and repair, oxidative stress response, neurodegenerative disorders, malaria, tumorigenesis, viral RNA replication and synthesis, heme incorporation, and posttranscriptional regulation of mRNA stability. In this talk, I will present our recent biophysical, structural, and in-cellulo metabolism assay results highlighting GAPDH role as a potential novel anti-cancer target, and as a non-canonical RNA binding protein.