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Procollagen lysyl hydroxylase 1 (PLOD1) is identified as a key regulator of adaptive metabolic remodeling in TMZ\u2010resistant GBM. Elevated PLOD1 promotes a hyper\u2010glycolytic phenotype by maintaining the stability of the glycolytic enzyme alpha\u2010enolase (ENO1). Mechanistically, PLOD1 catalytic activity increases an ENO1\u2010associated hydroxylation signal, promotes ENO1 stability, and limits FBXW7\u2010dependent ubiquitination and proteasomal degradation. Structural and functional analyses reveal that the central Ndst region of PLOD1 mediates substrate interaction, whereas its catalytic domain is required for ENO1 stabilization and downstream metabolic regulation. Clinically, PLOD1 and ENO1 expression levels are positively correlated in GBM specimens, and their co\u2010expression is associated with unfavorable patient outcomes. In xenograft models, inhibition of the PLOD1\u2010ENO1 axis suppresses tumor progression and enhances TMZ responsiveness. These findings establish the PLOD1\u2010FBXW7\u2010ENO1 regulatory axis as a critical mediator of GBM metabolic adaptation and therapeutic resistance, highlighting its potential as a prognostic biomarker and therapeutic target.<\/jats:p>","DOI":"10.1002\/advs.78070","type":"journal-article","created":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T18:00:31Z","timestamp":1790532031000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["PLOD1 Catalytic Activity Stabilizes ENO1 by Limiting FBXW7\u2010dependent Degradation to Promote Glycolysis and TMZ Resistance in Glioblastoma"],"prefix":"10.1002","author":[{"ORCID":"https:\/\/orcid.org\/0009-0002-3361-1206","authenticated-orcid":false,"given":"Fen","family":"Xue","sequence":"first","affiliation":[{"name":"Department of Radiation Oncology Fudan University Shanghai Cancer Center  Shanghai China"},{"name":"Department of Oncology Shanghai Medical College Fudan 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