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Drosophila TRIM32 cooperates with glycolytic enzymes to promote cell growth

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 bio...

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Autores principales: Bawa, Simranjot, Brooks, David S, Neville, Kathryn E, Tipping, Marla, Sagar, Md Abdul, Kollhoff, Joseph A, Chawla, Geetanjali, Geisbrecht, Brian V, Tennessen, Jason M, Eliceiri, Kevin W, Geisbrecht, Erika R
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7105379/
https://www.ncbi.nlm.nih.gov/pubmed/32223900
http://dx.doi.org/10.7554/eLife.52358
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author Bawa, Simranjot
Brooks, David S
Neville, Kathryn E
Tipping, Marla
Sagar, Md Abdul
Kollhoff, Joseph A
Chawla, Geetanjali
Geisbrecht, Brian V
Tennessen, Jason M
Eliceiri, Kevin W
Geisbrecht, Erika R
author_facet Bawa, Simranjot
Brooks, David S
Neville, Kathryn E
Tipping, Marla
Sagar, Md Abdul
Kollhoff, Joseph A
Chawla, Geetanjali
Geisbrecht, Brian V
Tennessen, Jason M
Eliceiri, Kevin W
Geisbrecht, Erika R
author_sort Bawa, Simranjot
collection PubMed
description 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.
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spelling pubmed-71053792020-04-01 Drosophila TRIM32 cooperates with glycolytic enzymes to promote cell growth Bawa, Simranjot Brooks, David S Neville, Kathryn E Tipping, Marla Sagar, Md Abdul Kollhoff, Joseph A Chawla, Geetanjali Geisbrecht, Brian V Tennessen, Jason M Eliceiri, Kevin W Geisbrecht, Erika R eLife Cancer Biology 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. eLife Sciences Publications, Ltd 2020-03-30 /pmc/articles/PMC7105379/ /pubmed/32223900 http://dx.doi.org/10.7554/eLife.52358 Text en © 2020, Bawa et al http://creativecommons.org/licenses/by/4.0/ http://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited.
spellingShingle Cancer Biology
Bawa, Simranjot
Brooks, David S
Neville, Kathryn E
Tipping, Marla
Sagar, Md Abdul
Kollhoff, Joseph A
Chawla, Geetanjali
Geisbrecht, Brian V
Tennessen, Jason M
Eliceiri, Kevin W
Geisbrecht, Erika R
Drosophila TRIM32 cooperates with glycolytic enzymes to promote cell growth
title Drosophila TRIM32 cooperates with glycolytic enzymes to promote cell growth
title_full Drosophila TRIM32 cooperates with glycolytic enzymes to promote cell growth
title_fullStr Drosophila TRIM32 cooperates with glycolytic enzymes to promote cell growth
title_full_unstemmed Drosophila TRIM32 cooperates with glycolytic enzymes to promote cell growth
title_short Drosophila TRIM32 cooperates with glycolytic enzymes to promote cell growth
title_sort drosophila trim32 cooperates with glycolytic enzymes to promote cell growth
topic Cancer Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7105379/
https://www.ncbi.nlm.nih.gov/pubmed/32223900
http://dx.doi.org/10.7554/eLife.52358
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