{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Dias MH"],"funding":["X-omics Initiative","Dutch Ministry of Health, Welfare and Sport","Lixte Biotechnology Holdings","Dutch Cancer Society","National Science Center","Oncode Institute"],"pagination":["2220-2238"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11094086"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["25(5)"],"pubmed_abstract":["Perturbation of protein phosphorylation represents an attractive approach to cancer treatment. Besides kinase inhibitors, protein phosphatase inhibitors have been shown to have anti-cancer activity. A prime example is the small molecule LB-100, an inhibitor of protein phosphatases 2A/5 (PP2A/PP5), enzymes that affect cellular physiology. LB-100 has proven effective in pre-clinical models in combination with immunotherapy, but the molecular underpinnings of this synergy remain understood poorly. We report here a sensitivity of the mRNA splicing machinery to phosphorylation changes in response to LB-100 in colorectal adenocarcinoma. We observe enrichment for differentially phosphorylated sites within cancer-critical splicing nodes of U2 snRNP, SRSF and hnRNP proteins. Altered phosphorylation"],"journal":["EMBO reports"],"pubmed_title":["The phosphatase inhibitor LB-100 creates neoantigens in colon cancer cells through perturbation of mRNA splicing."],"pmcid":["PMC11094086"],"funding_grant_id":["UMO-2022/46/E/NZ3/00141","UMO-2021/43/B/NZ3/01177","Project 184.034.019","Rene R Bernards"],"pubmed_authors":["Liudkovska V","Dias MH","Papagianni C","Montenegro Navarro J","Champagne J","Agami R","Ciesla M","Bleijerveld OB","Giebel L","Velds A","Bernards R"],"additional_accession":[]},"is_claimable":false,"name":"The phosphatase inhibitor LB-100 creates neoantigens in colon cancer cells through perturbation of mRNA splicing.","description":"Perturbation of protein phosphorylation represents an attractive approach to cancer treatment. Besides kinase inhibitors, protein phosphatase inhibitors have been shown to have anti-cancer activity. A prime example is the small molecule LB-100, an inhibitor of protein phosphatases 2A/5 (PP2A/PP5), enzymes that affect cellular physiology. LB-100 has proven effective in pre-clinical models in combination with immunotherapy, but the molecular underpinnings of this synergy remain understood poorly. We report here a sensitivity of the mRNA splicing machinery to phosphorylation changes in response to LB-100 in colorectal adenocarcinoma. We observe enrichment for differentially phosphorylated sites within cancer-critical splicing nodes of U2 snRNP, SRSF and hnRNP proteins. Altered phosphorylation","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-06-03T06:54:15.995Z","creation":"2026-04-25T03:22:34.703Z"},"accession":"S-EPMC11094086","cross_references":{"pubmed":["38600345"],"doi":["10.1038/s44319-024-00128-3"]}}