{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Haowei Z"],"funding":["Shenzhen Science and Technology Innovation Commission","Science and Technology Department of Henan Province (Henan Provincial Department of Science and Technology)","National Natural Science Foundation of China (National Science Foundation of China)"],"pagination":["225"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12921045"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(1)"],"pubmed_abstract":["The mitochondria-localized deubiquitinase USP30 regulates mitophagy and mitochondrial homeostasis, playing a significant role in the progression of neurodegenerative diseases. However, its role in cancer remains poorly understood. Through metabolism-related gene set enrichment analysis, we identified USP30 as a key modulator of glucose metabolism in cancer cells. Utilizing quantitative proteomic and ubiquitinomic approaches coupled with co-immunoprecipitation assays, we elucidated that USP30 regulates glycolysis by interacting with hexokinase HK1 and HK2, a process dependent on its enzymatic activity. USP30 modulates the ubiquitination profile of HK1 and HK2 by preferentially removing atypical ubiquitin chains, thereby enhancing their stability, mitochondrial localization, VDAC1 binding an"],"journal":["Cell death & disease"],"pubmed_title":["USP30-mediated Deubiquitination of Hexokinase 2 controls the metabolic fate of glucose and tumor progression."],"pmcid":["PMC12921045"],"funding_grant_id":["32200438, 32301053","252102310403","JCYJ20240813142003005"],"pubmed_authors":["Jiang Y","Yang H","Li X","Li Y","Xie W","Xu N","Zhang Y","Liao W","Haowei Z","Qin X","Zeng H"],"additional_accession":[]},"is_claimable":false,"name":"USP30-mediated Deubiquitination of Hexokinase 2 controls the metabolic fate of glucose and tumor progression.","description":"The mitochondria-localized deubiquitinase USP30 regulates mitophagy and mitochondrial homeostasis, playing a significant role in the progression of neurodegenerative diseases. However, its role in cancer remains poorly understood. Through metabolism-related gene set enrichment analysis, we identified USP30 as a key modulator of glucose metabolism in cancer cells. Utilizing quantitative proteomic and ubiquitinomic approaches coupled with co-immunoprecipitation assays, we elucidated that USP30 regulates glycolysis by interacting with hexokinase HK1 and HK2, a process dependent on its enzymatic activity. USP30 modulates the ubiquitination profile of HK1 and HK2 by preferentially removing atypical ubiquitin chains, thereby enhancing their stability, mitochondrial localization, VDAC1 binding an","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Feb","modification":"2026-07-16T12:33:35.994Z","creation":"2026-07-09T10:55:29.764Z"},"accession":"S-EPMC12921045","cross_references":{"pubmed":["41688443"],"doi":["10.1038/s41419-026-08459-w"]}}