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http://purl.uniprot.org/citations/10358069http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10358069http://www.w3.org/2000/01/rdf-schema#comment"Phosphorylation at serine 15 of the human p53 tumor suppressor protein is induced by DNA damage and correlates with accumulation of p53 and its activation as a transcription factor. The DNA-dependent protein kinase (DNA-PK) can phosphorylate serine 15 of human p53 and the homologous serine 18 of murine p53 in vitro. Contradictory reports exist about the requirement for DNA-PK in vivo for p53 activation and cell cycle arrest in response to ionizing radiation. While primary SCID (severe combined immunodeficiency) cells, that have defective DNA-PK, show normal p53 activation and cell cycle arrest, a transcriptionally inert form of p53 is induced in the SCID cell line SCGR11. In order to unambiguously define the role of the DNA-PK catalytic subunit (DNA-PKcs) in p53 activation, we examined p53 phosphorylation in mouse embryonic fibroblasts (MEFs) from DNA-PKcs-null mice. We found a similar pattern of serine 18 phosphorylation and accumulation of p53 in response to irradiation in both control and DNA-PKcs-null MEFs. The induced p53 was capable of sequence-specific DNA binding even in the absence of DNA-PKcs. Transactivation of the cyclin-dependent-kinase inhibitor p21, a downstream target of p53, and the G1 cell cycle checkpoint were also found to be normal in the DNA-PKcs -/-MEFs. Our results demonstrate that DNA-PKcs, unlike the related ATM protein, is not essential for the activation of p53 and G1 cell cycle arrest in response to ionizing radiation."xsd:string
http://purl.uniprot.org/citations/10358069http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.24.17139"xsd:string
http://purl.uniprot.org/citations/10358069http://purl.uniprot.org/core/author"Xie G."xsd:string
http://purl.uniprot.org/citations/10358069http://purl.uniprot.org/core/author"Abe M."xsd:string
http://purl.uniprot.org/citations/10358069http://purl.uniprot.org/core/author"Taya Y."xsd:string
http://purl.uniprot.org/citations/10358069http://purl.uniprot.org/core/author"Chen D.J."xsd:string
http://purl.uniprot.org/citations/10358069http://purl.uniprot.org/core/author"Li G.C."xsd:string
http://purl.uniprot.org/citations/10358069http://purl.uniprot.org/core/author"Burma S."xsd:string
http://purl.uniprot.org/citations/10358069http://purl.uniprot.org/core/author"Kurimasa A."xsd:string
http://purl.uniprot.org/citations/10358069http://purl.uniprot.org/core/author"Ouyang H."xsd:string
http://purl.uniprot.org/citations/10358069http://purl.uniprot.org/core/author"Araki R."xsd:string
http://purl.uniprot.org/citations/10358069http://purl.uniprot.org/core/author"Crissman H.A."xsd:string
http://purl.uniprot.org/citations/10358069http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10358069http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/10358069http://purl.uniprot.org/core/pages"17139-17143"xsd:string
http://purl.uniprot.org/citations/10358069http://purl.uniprot.org/core/title"DNA-dependent protein kinase-independent activation of p53 in response to DNA damage."xsd:string
http://purl.uniprot.org/citations/10358069http://purl.uniprot.org/core/volume"274"xsd:string
http://purl.uniprot.org/citations/10358069http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10358069
http://purl.uniprot.org/citations/10358069http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10358069
http://purl.uniprot.org/uniprot/#_P97313-mappedCitation-10358069http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10358069
http://purl.uniprot.org/uniprot/P97313http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10358069