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http://purl.uniprot.org/citations/34385184http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/34385184http://www.w3.org/2000/01/rdf-schema#comment"Chromosomal translocations generate oncogenic fusion proteins in approximately one-third of sarcomas, but how these proteins promote tumorigenesis is not well understood. Interestingly, some translocation-driven cancers exhibit dramatic clinical responses to therapy, such as radiotherapy, although the precise mechanism has not been elucidated. Here we reveal a molecular mechanism by which the fusion oncoprotein FUS-CHOP promotes tumor maintenance that also explains the remarkable sensitivity of myxoid liposarcomas to radiation therapy. FUS-CHOP interacted with chromatin remodeling complexes to regulate sarcoma cell proliferation. One of these chromatin remodelers, SNF2H, colocalized with FUS-CHOP genome-wide at active enhancers. Following ionizing radiation, DNA damage response kinases phosphorylated the prion-like domain of FUS-CHOP to impede these protein-protein interactions, which are required for transformation. Therefore, the DNA damage response after irradiation disrupted oncogenic targeting of chromatin remodelers required for FUS-CHOP-driven sarcomagenesis. This mechanism of disruption links phosphorylation of the prion-like domain of an oncogenic fusion protein to DNA damage after ionizing radiation and reveals that a dependence on oncogenic chromatin remodeling underlies sensitivity to radiation therapy in myxoid liposarcoma. SIGNIFICANCE: Prion-like domains, which are frequently translocated in cancers as oncogenic fusion proteins that drive global epigenetic changes, confer sensitivity to radiation via disruption of oncogenic interactions."xsd:string
http://purl.uniprot.org/citations/34385184http://purl.org/dc/terms/identifier"doi:10.1158/0008-5472.can-20-1497"xsd:string
http://purl.uniprot.org/citations/34385184http://purl.uniprot.org/core/author"Chen M."xsd:string
http://purl.uniprot.org/citations/34385184http://purl.uniprot.org/core/author"Davis I.J."xsd:string
http://purl.uniprot.org/citations/34385184http://purl.uniprot.org/core/author"Xu E."xsd:string
http://purl.uniprot.org/citations/34385184http://purl.uniprot.org/core/author"Kirsch D.G."xsd:string
http://purl.uniprot.org/citations/34385184http://purl.uniprot.org/core/author"Daniel A.R."xsd:string
http://purl.uniprot.org/citations/34385184http://purl.uniprot.org/core/author"Foster J.P."xsd:string
http://purl.uniprot.org/citations/34385184http://purl.uniprot.org/core/author"Leisenring N.H."xsd:string
http://purl.uniprot.org/citations/34385184http://purl.uniprot.org/core/author"Floyd W."xsd:string
http://purl.uniprot.org/citations/34385184http://purl.uniprot.org/core/author"Lock I.C."xsd:string
http://purl.uniprot.org/citations/34385184http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/34385184http://purl.uniprot.org/core/name"Cancer Res"xsd:string
http://purl.uniprot.org/citations/34385184http://purl.uniprot.org/core/pages"4939-4948"xsd:string
http://purl.uniprot.org/citations/34385184http://purl.uniprot.org/core/title"Radiation-Induced Phosphorylation of a Prion-Like Domain Regulates Transformation by FUS-CHOP."xsd:string
http://purl.uniprot.org/citations/34385184http://purl.uniprot.org/core/volume"81"xsd:string
http://purl.uniprot.org/citations/34385184http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/34385184
http://purl.uniprot.org/citations/34385184http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/34385184
http://purl.uniprot.org/uniprot/#_P35638-mappedCitation-34385184http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34385184
http://purl.uniprot.org/uniprot/#_P0DPQ6-mappedCitation-34385184http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34385184
http://purl.uniprot.org/uniprot/#_Q53YD1-mappedCitation-34385184http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34385184
http://purl.uniprot.org/uniprot/P35638http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34385184
http://purl.uniprot.org/uniprot/Q53YD1http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34385184
http://purl.uniprot.org/uniprot/P0DPQ6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34385184