ERK1-mediated GLYCTK2 phosphorylation promotes fructolysis to sustain glioblastoma survival under glucose deprivation

Abstract Metabolic plasticity sustains glioblastoma (GBM) survival under nutrient stress, yet how fructolytic adaptation compensates for glucose deprivation remains unclear. Here, we identify glycerate kinase 2 (GLYCTK2) as a glucose-sensing metabolic checkpoint that maintains GBM cell viability thr...

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Main Authors: Yingping Li, Fenna Zhang, Fumin Hu, Rui Tong, Yueqi Wen, Guokai Fu, Xueli Bian
Format: Article
Language:English
Published: Nature Publishing Group 2025-06-01
Series:Cell Death Discovery
Online Access:https://doi.org/10.1038/s41420-025-02544-3
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author Yingping Li
Fenna Zhang
Fumin Hu
Rui Tong
Yueqi Wen
Guokai Fu
Xueli Bian
author_facet Yingping Li
Fenna Zhang
Fumin Hu
Rui Tong
Yueqi Wen
Guokai Fu
Xueli Bian
author_sort Yingping Li
collection DOAJ
description Abstract Metabolic plasticity sustains glioblastoma (GBM) survival under nutrient stress, yet how fructolytic adaptation compensates for glucose deprivation remains unclear. Here, we identify glycerate kinase 2 (GLYCTK2) as a glucose-sensing metabolic checkpoint that maintains GBM cell viability through ERK1-mediated phosphorylation. Mechanistically, glucose deprivation-activated ERK1 phosphorylates GLYCTK2 at serine 220 directly, which prevents STUB1 (ubiquitin E3 ligase) binding, thereby abrogating the ubiquitination and degradation of GLYCTK2. Importantly, Functional studies demonstrated that fructose supplementation rescues glucose deprivation-induced death in wild-type GBM cells, but fails to protect GLYCTK2-depleted cells, establishing GLYCTK2 as the gatekeeper of fructolytic salvage pathways. These findings demonstrate an important mechanism by which GBM cells rewire glucose metabolism to fructose metabolism via phosphorylating and stabilizing GLYCTK2 to maintain GBM cell survival under glucose deprivation condition, underscoring the potential to target GLYCTK2 for the treatment of patients with GBM.
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publishDate 2025-06-01
publisher Nature Publishing Group
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series Cell Death Discovery
spelling doaj-art-84b7c0839a4e44e98ded2c87c077e5c42025-08-20T02:30:43ZengNature Publishing GroupCell Death Discovery2058-77162025-06-0111111210.1038/s41420-025-02544-3ERK1-mediated GLYCTK2 phosphorylation promotes fructolysis to sustain glioblastoma survival under glucose deprivationYingping Li0Fenna Zhang1Fumin Hu2Rui Tong3Yueqi Wen4Guokai Fu5Xueli Bian6Department of Clinical Nutrition, The Second Affiliated Hospital, Jiangxi Medical College, Nanchang UniversityThe First Affiliated Hospital of Xi’an Medical UniversityThe MOE Basic Research and Innovation Center for the Targeted Therapeutics of Solid Tumors, School of Basic Medical Sciences, Jiangxi Medical College, Nanchang UniversityThe MOE Basic Research and Innovation Center for the Targeted Therapeutics of Solid Tumors, School of Basic Medical Sciences, Jiangxi Medical College, Nanchang UniversityThe MOE Basic Research and Innovation Center for the Targeted Therapeutics of Solid Tumors, School of Basic Medical Sciences, Jiangxi Medical College, Nanchang UniversityThe MOE Basic Research and Innovation Center for the Targeted Therapeutics of Solid Tumors, School of Basic Medical Sciences, Jiangxi Medical College, Nanchang UniversityDepartment of Clinical Nutrition, The Second Affiliated Hospital, Jiangxi Medical College, Nanchang UniversityAbstract Metabolic plasticity sustains glioblastoma (GBM) survival under nutrient stress, yet how fructolytic adaptation compensates for glucose deprivation remains unclear. Here, we identify glycerate kinase 2 (GLYCTK2) as a glucose-sensing metabolic checkpoint that maintains GBM cell viability through ERK1-mediated phosphorylation. Mechanistically, glucose deprivation-activated ERK1 phosphorylates GLYCTK2 at serine 220 directly, which prevents STUB1 (ubiquitin E3 ligase) binding, thereby abrogating the ubiquitination and degradation of GLYCTK2. Importantly, Functional studies demonstrated that fructose supplementation rescues glucose deprivation-induced death in wild-type GBM cells, but fails to protect GLYCTK2-depleted cells, establishing GLYCTK2 as the gatekeeper of fructolytic salvage pathways. These findings demonstrate an important mechanism by which GBM cells rewire glucose metabolism to fructose metabolism via phosphorylating and stabilizing GLYCTK2 to maintain GBM cell survival under glucose deprivation condition, underscoring the potential to target GLYCTK2 for the treatment of patients with GBM.https://doi.org/10.1038/s41420-025-02544-3
spellingShingle Yingping Li
Fenna Zhang
Fumin Hu
Rui Tong
Yueqi Wen
Guokai Fu
Xueli Bian
ERK1-mediated GLYCTK2 phosphorylation promotes fructolysis to sustain glioblastoma survival under glucose deprivation
Cell Death Discovery
title ERK1-mediated GLYCTK2 phosphorylation promotes fructolysis to sustain glioblastoma survival under glucose deprivation
title_full ERK1-mediated GLYCTK2 phosphorylation promotes fructolysis to sustain glioblastoma survival under glucose deprivation
title_fullStr ERK1-mediated GLYCTK2 phosphorylation promotes fructolysis to sustain glioblastoma survival under glucose deprivation
title_full_unstemmed ERK1-mediated GLYCTK2 phosphorylation promotes fructolysis to sustain glioblastoma survival under glucose deprivation
title_short ERK1-mediated GLYCTK2 phosphorylation promotes fructolysis to sustain glioblastoma survival under glucose deprivation
title_sort erk1 mediated glyctk2 phosphorylation promotes fructolysis to sustain glioblastoma survival under glucose deprivation
url https://doi.org/10.1038/s41420-025-02544-3
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