6D69
Crystal Structure of the NHL Repeat Region of D. melanogaster Thin
6D69 の概要
| エントリーDOI | 10.2210/pdb6d69/pdb |
| 分子名称 | NHL Repeat Region of D. melanogaster Thin, GLYCEROL (3 entities in total) |
| 機能のキーワード | protein-protein interaction, beta-propeller, limb girdle muscular dystrophy type 2h, protein binding |
| 由来する生物種 | Drosophila melanogaster (Fruit fly) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 33255.74 |
| 構造登録者 | |
| 主引用文献 | 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 Cited by 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: 32223900DOI: 10.7554/eLife.52358 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.601 Å) |
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