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http://purl.uniprot.org/citations/25772236http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25772236http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25772236http://www.w3.org/2000/01/rdf-schema#comment"Although modulation of the cellular tumor-suppressor p53 is considered to have the major role in E1A/E1B-55K-mediated tumorigenesis, other promyelocytic leukemia nuclear body (PML-NB)/PML oncogenic domain (POD)-associated factors including SUMO, Mre11, Daxx, as well as the integrity of these nuclear bodies contribute to the transformation process. However, the biochemical consequences and oncogenic alterations of PML-associated E1B-55K by SUMO-dependent PML-IV and PML-V interaction have so far remained elusive. We performed mutational analysis to define a PML interaction motif within the E1B-55K polypeptide. Our results showed that E1B-55K/PML binding is not required for p53, Mre11 and Daxx interaction. We also observed that E1B-55K lacking subnuclear PML localization because of either PML-IV or PML-V-binding deficiency was no longer capable of mediating E1B-55K-dependent SUMOylation of p53, inhibition of p53-mediated transactivation or efficiently transforming primary rodent cells. These results together with the observation that E1B-55K-dependent SUMOylation of p53 is required for efficient cell transformation, provides evidence for the idea that the SUMO ligase activity of the E1B-55K viral oncoprotein is intimately linked to its growth-promoting oncogenic activities."xsd:string
http://purl.uniprot.org/citations/25772236http://purl.org/dc/terms/identifier"doi:10.1038/onc.2015.63"xsd:string
http://purl.uniprot.org/citations/25772236http://purl.org/dc/terms/identifier"doi:10.1038/onc.2015.63"xsd:string
http://purl.uniprot.org/citations/25772236http://purl.uniprot.org/core/author"Hay R.T."xsd:string
http://purl.uniprot.org/citations/25772236http://purl.uniprot.org/core/author"Hay R.T."xsd:string
http://purl.uniprot.org/citations/25772236http://purl.uniprot.org/core/author"Berscheminski J."xsd:string
http://purl.uniprot.org/citations/25772236http://purl.uniprot.org/core/author"Berscheminski J."xsd:string
http://purl.uniprot.org/citations/25772236http://purl.uniprot.org/core/author"Blanchette P."xsd:string
http://purl.uniprot.org/citations/25772236http://purl.uniprot.org/core/author"Blanchette P."xsd:string
http://purl.uniprot.org/citations/25772236http://purl.uniprot.org/core/author"Branton P.E."xsd:string
http://purl.uniprot.org/citations/25772236http://purl.uniprot.org/core/author"Branton P.E."xsd:string
http://purl.uniprot.org/citations/25772236http://purl.uniprot.org/core/author"Dobner T."xsd:string
http://purl.uniprot.org/citations/25772236http://purl.uniprot.org/core/author"Dobner T."xsd:string
http://purl.uniprot.org/citations/25772236http://purl.uniprot.org/core/author"Groitl P."xsd:string
http://purl.uniprot.org/citations/25772236http://purl.uniprot.org/core/author"Groitl P."xsd:string
http://purl.uniprot.org/citations/25772236http://purl.uniprot.org/core/author"Schreiner S."xsd:string
http://purl.uniprot.org/citations/25772236http://purl.uniprot.org/core/author"Schreiner S."xsd:string
http://purl.uniprot.org/citations/25772236http://purl.uniprot.org/core/author"Wimmer P."xsd:string
http://purl.uniprot.org/citations/25772236http://purl.uniprot.org/core/author"Wimmer P."xsd:string
http://purl.uniprot.org/citations/25772236http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/25772236http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/25772236http://purl.uniprot.org/core/name"Oncogene"xsd:string
http://purl.uniprot.org/citations/25772236http://purl.uniprot.org/core/name"Oncogene"xsd:string