Grad student Danielle Schmitt has had a paper just accepted into the American Chemical Society journal, ACS Chemical Biology. Her paper, co-authored with mentor, Songon An, and collaborators in the Department of Mathematics and Statistics is: Sequestration-Mediated Downregulation of de Novo Purine Biosynthesis by AMPK. Briefly, dynamic partitioning of de novo purine biosynthetic enzymes into multienzyme compartments, purinosomes, has been
associated with the increased flux of de novo purine biosynthesis in human cells. However, a mechanism, by which de novo purine biosynthesis would be downregulated in cells, has been elusive for several decades. Using various fluorescence single-cell microscopic techniques, Schmitt et al. have identified that the spatial sequestration of one enzyme from the rest of the pathway enzymes is the mechanism by which cells downregulate de novo purine biosynthesis.
Collectively, we finally understand how human de novo purine biosynthesis is turned on and off in subcellular levels. Danielle is also a recipient of the ASBMB 2016 Thematic Best Poster award from the ASBMB Annual Meeting in San Diego.