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Crystal Structure of the NHL Repeat Region of D. melanogaster ThinCrystal Structure of the NHL Repeat Region of D. melanogaster Thin
Structural highlights
FunctionPublication Abstract from PubMedCell 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. Drosophila TRIM32 cooperates with glycolytic enzymes to promote cell growth.,Bawa S, Brooks DS, Neville KE, Tipping M, Sagar MA, Kollhoff JA, Chawla G, Geisbrecht BV, Tennessen JM, Eliceiri KW, Geisbrecht ER Elife. 2020 Mar 30;9. pii: 52358. doi: 10.7554/eLife.52358. PMID:32223900[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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