{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Senatore E"],"funding":["Ministero dell'Università e della Ricerca (MUR)","European Regional Development Fund (POR Campania FESR 2021-2027)","Fondazione AIRC per la ricerca sul cancro ETS (AIRC)"],"pagination":["2347-2377"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12069581"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["26(9)"],"pubmed_abstract":["Glioblastoma multiforme (GBM) is the most lethal form of malignant brain tumor in adults. Dysregulation of protein synthesis contributes to cancer cell plasticity, driving GBM cell heterogeneity, metastatic behavior, and drug resistance. Understanding the complex network and signaling pathways governing protein translation, is therefore an important goal for GBM treatment. Here we identify a novel signaling network centered on the E3 ubiquitin ligase praja2 that controls protein translation in GBM. Praja2 forms a multimeric complex with the RNA helicase DDX6, which inhibits translation of target RNAs within processing bodies (P-bodies). Stimulation of cAMP signaling through activation of G-protein-coupled receptors induces P-body assembly through praja2-mediated non-proteolytic polyubiquit"],"journal":["EMBO reports"],"pubmed_title":["Praja2 controls P-body assembly and translation in glioblastoma by non-proteolytic ubiquitylation of DDX6."],"pmcid":["PMC12069581"],"funding_grant_id":["PE0000006","E53D23009690006","E63C22000940007","IG2023-29124","E53D23021760001","RARE.Glials"],"pubmed_authors":["Toiron Y","Arcella A","Memoli D","Flammia R","Senatore E","Rinaldi L","Camoin L","Oliva MA","Scaloni A","Turacchio G","Bianco AG","Avolio R","D'Ambrosio C","Ambrosino C","Feliciello A","Mimoune SI","Chiuso F","Pagnotta SM","Audebert S","Dalla E","Lignitto L"],"additional_accession":[]},"is_claimable":false,"name":"Praja2 controls P-body assembly and translation in glioblastoma by non-proteolytic ubiquitylation of DDX6.","description":"Glioblastoma multiforme (GBM) is the most lethal form of malignant brain tumor in adults. Dysregulation of protein synthesis contributes to cancer cell plasticity, driving GBM cell heterogeneity, metastatic behavior, and drug resistance. Understanding the complex network and signaling pathways governing protein translation, is therefore an important goal for GBM treatment. Here we identify a novel signaling network centered on the E3 ubiquitin ligase praja2 that controls protein translation in GBM. Praja2 forms a multimeric complex with the RNA helicase DDX6, which inhibits translation of target RNAs within processing bodies (P-bodies). Stimulation of cAMP signaling through activation of G-protein-coupled receptors induces P-body assembly through praja2-mediated non-proteolytic polyubiquit","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 May","modification":"2026-06-01T22:23:17.144Z","creation":"2026-05-22T03:08:22.578Z"},"accession":"S-EPMC12069581","cross_references":{"pubmed":["40148504"],"doi":["10.1038/s44319-025-00425-5"]}}