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http://purl.uniprot.org/citations/16873060http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16873060http://www.w3.org/2000/01/rdf-schema#comment"The PML tumor suppressor controls key pathways for growth suppression, induction of apoptosis, and cellular senescence. PML loss occurs frequently in human tumors through unknown posttranslational mechanisms. Casein kinase 2 (CK2) is oncogenic and frequently upregulated in human tumors. Here we show that CK2 regulates PML protein levels by promoting its ubiquitin-mediated degradation dependent on direct phosphorylation at Ser517. Consequently, PML mutants that are resistant to CK2 phosphorylation display increased tumor-suppressive functions. In a faithful mouse model of lung cancer, we demonstrate that Pml inactivation leads to increased tumorigenesis. Furthermore, CK2 pharmacological inhibition enhances the PML tumor-suppressive property in vivo. Importantly, we found an inverse correlation between CK2 kinase activity and PML protein levels in human lung cancer-derived cell lines and primary specimens. These data identify a key posttranslational mechanism that controls PML protein levels and provide therapeutic means toward PML restoration through CK2 inhibition."xsd:string
http://purl.uniprot.org/citations/16873060http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2006.05.041"xsd:string
http://purl.uniprot.org/citations/16873060http://purl.uniprot.org/core/author"Singh B."xsd:string
http://purl.uniprot.org/citations/16873060http://purl.uniprot.org/core/author"Tempst P."xsd:string
http://purl.uniprot.org/citations/16873060http://purl.uniprot.org/core/author"Erdjument-Bromage H."xsd:string
http://purl.uniprot.org/citations/16873060http://purl.uniprot.org/core/author"Pandolfi P.P."xsd:string
http://purl.uniprot.org/citations/16873060http://purl.uniprot.org/core/author"Teruya-Feldstein J."xsd:string
http://purl.uniprot.org/citations/16873060http://purl.uniprot.org/core/author"Scaglioni P.P."xsd:string
http://purl.uniprot.org/citations/16873060http://purl.uniprot.org/core/author"Yung T.M."xsd:string
http://purl.uniprot.org/citations/16873060http://purl.uniprot.org/core/author"Cai L.F."xsd:string
http://purl.uniprot.org/citations/16873060http://purl.uniprot.org/core/author"Kaufman A.J."xsd:string
http://purl.uniprot.org/citations/16873060http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16873060http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/16873060http://purl.uniprot.org/core/pages"269-283"xsd:string
http://purl.uniprot.org/citations/16873060http://purl.uniprot.org/core/title"A CK2-dependent mechanism for degradation of the PML tumor suppressor."xsd:string
http://purl.uniprot.org/citations/16873060http://purl.uniprot.org/core/volume"126"xsd:string
http://purl.uniprot.org/citations/16873060http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16873060
http://purl.uniprot.org/citations/16873060http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16873060
http://purl.uniprot.org/uniprot/#_A0A068EW80-mappedCitation-16873060http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16873060
http://purl.uniprot.org/uniprot/#_D3YXR5-mappedCitation-16873060http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16873060
http://purl.uniprot.org/uniprot/#_F6XUT1-mappedCitation-16873060http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16873060
http://purl.uniprot.org/uniprot/#_D3Z2V0-mappedCitation-16873060http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16873060
http://purl.uniprot.org/uniprot/#_D3Z3A6-mappedCitation-16873060http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16873060
http://purl.uniprot.org/uniprot/#_D6RII9-mappedCitation-16873060http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16873060