{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Mahlokozera T"],"funding":["U.S. Department of Health & Human Services | NIH | National Institute of Neurological Disorders and Stroke","NINDS NIH HHS","NCI NIH HHS","NIH HHS"],"pagination":["6321"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8566473"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(1)"],"pubmed_abstract":["The pluripotency transcription factor SOX2 is essential for the maintenance of glioblastoma stem cells (GSC), which are thought to underlie tumor growth, treatment resistance, and recurrence. To understand how SOX2 is regulated in GSCs, we utilized a proteomic approach and identified the E3 ubiquitin ligase TRIM26 as a direct SOX2-interacting protein. Unexpectedly, we found TRIM26 depletion decreased SOX2 protein levels and increased SOX2 polyubiquitination in patient-derived GSCs, suggesting TRIM26 promotes SOX2 protein stability. Accordingly, TRIM26 knockdown disrupted the SOX2 gene network and inhibited both self-renewal capacity as well as in vivo tumorigenicity in multiple GSC lines. Mechanistically, we found TRIM26, via its C-terminal PRYSPRY domain, but independent of its RING domai"],"journal":["Nature communications"],"pubmed_title":["Competitive binding of E3 ligases TRIM26 and WWP2 controls SOX2 in glioblastoma."],"pmcid":["PMC8566473"],"funding_grant_id":["P30 CA091842","R01 NS106612","S10 OD027042","S10 OD021629","R01 NS051255","R01 NS111014","R01 NS094670"],"pubmed_authors":["Salehi A","Patel B","Mahlokozera T","Mao DD","Chen H","Desouza P","Kim AH","Gujar AD","Paturu M","Yang W","Petti AA","Hafez D","Taiwo R","Dunn GP","Yano H","Qu X","Mosammaparast N"],"additional_accession":[]},"is_claimable":false,"name":"Competitive binding of E3 ligases TRIM26 and WWP2 controls SOX2 in glioblastoma.","description":"The pluripotency transcription factor SOX2 is essential for the maintenance of glioblastoma stem cells (GSC), which are thought to underlie tumor growth, treatment resistance, and recurrence. To understand how SOX2 is regulated in GSCs, we utilized a proteomic approach and identified the E3 ubiquitin ligase TRIM26 as a direct SOX2-interacting protein. Unexpectedly, we found TRIM26 depletion decreased SOX2 protein levels and increased SOX2 polyubiquitination in patient-derived GSCs, suggesting TRIM26 promotes SOX2 protein stability. Accordingly, TRIM26 knockdown disrupted the SOX2 gene network and inhibited both self-renewal capacity as well as in vivo tumorigenicity in multiple GSC lines. Mechanistically, we found TRIM26, via its C-terminal PRYSPRY domain, but independent of its RING domai","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Nov","modification":"2026-05-08T23:44:17.165Z","creation":"2026-04-08T00:27:38.051Z"},"accession":"S-EPMC8566473","cross_references":{"pubmed":["34732716"],"doi":["10.1038/s41467-021-26653-6"]}}