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Drosophila TRIM32 cooperates with glycolytic enzymes to promote cell growth

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poster
posted on 20.04.2020 by 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
Cell growth and/or proliferation may require the reprogramming of metabolic pathways, whereby a switch from oxidative to glycolytic metabolism diverts glycolytic
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 Drosophila TRIM32, encoded by thin (tn), shows
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
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
glycolysis in the context of both normal development and tumor growth.

Funding

National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS)

United States Department of Health and Human Services

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National Institute of General Medical Sciences (NIGMS)

United States Department of Health and Human Services

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NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES (NIAMS)

United States Department of Health and Human Services

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