6D69

Crystal Structure of the NHL Repeat Region of D. melanogaster Thin

Summary for 6D69

• Entry DOI: 10.2210/pdb6d69/pdb
• Descriptor: NHL Repeat Region of D. melanogaster Thin, GLYCEROL (3 entities in total)
• Functional Keywords: protein-protein interaction, beta-propeller, limb girdle muscular dystrophy type 2h, protein binding
• Biological source: Drosophila melanogaster (Fruit fly)
• Total number of polymer chains: 1
• Total formula weight: 33255.74

Authors

Ramyar, K.X.,McWhorter, W.J.,Geisbrecht, B.V. (deposition date: 2018-04-20, release date: 2019-04-24, Last modification date: 2023-10-04)

Primary citation

Bawa, S.,Brooks, D.S.,Neville, K.E.,Tipping, M.,Sagar, M.A.,Kollhoff, J.A.,Chawla, G.,Geisbrecht, B.V.,Tennessen, J.M.,Eliceiri, K.W.,Geisbrecht, E.R.
DrosophilaTRIM32 cooperates with glycolytic enzymes to promote cell growth.
Elife, 9:-, 2020

PubMed Abstract: 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 TRIM32, encoded by , 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 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.

PubMed: 32223900
DOI: 10.7554/eLife.52358

Experimental method

X-RAY DIFFRACTION (2.601 Å)