Drosophila TRIM32 cooperates with glycolytic enzymes to promote cell growth Simran Bawa David S Brooks Kathryn E Neville Marla Tipping Md Abdul Kader Sagar Joseph Kollhoff Geetanjali Chawla Brian V. Geisbrecht Jason M. Tennessen Kevin W. Eliceiri Erika R. Geisbrecht 10.6084/m9.figshare.12150138.v1 https://tagc2020.figshare.com/articles/poster/Drosophila_TRIM32_cooperates_with_glycolytic_enzymes_to_promote_cell_growth/12150138 <div>Cell growth and/or proliferation may require the reprogramming of metabolic pathways, whereby a switch from oxidative to glycolytic metabolism diverts glycolytic</div><div>intermediates towards anabolic pathways. Herein, we identify a novel role for TRIM32 in the maintenance of glycolytic flux mediated by biochemical interactions with the glycolytic enzymes Aldolase and Phosphoglycerate mutase. Loss of<i> Drosophila </i>TRIM32, encoded by thin (tn), shows</div><div>reduced levels of glycolytic intermediates and amino acids. This altered metabolic profile correlates with a reduction in the size of glycolytic larval muscle and brain tissue. Consistent with a role for metabolic intermediates in glycolysis-driven biomass production, dietary amino acid</div><div>supplementation in tn mutants improves muscle mass. Remarkably, TRIM32 is also required for ectopic growth - loss of TRIM32 in a wing disc-associated tumor model reduces glycolytic metabolism and restricts growth. Overall, our results reveal a novel role for TRIM32 for controlling</div><div>glycolysis in the context of both normal development and tumor growth.</div> 2020-04-20 22:12:40 Metabolism Muscle Cancer Cell Metabolism Cancer Cell Biology