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http://purl.uniprot.org/citations/19837670http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19837670http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19837670http://www.w3.org/2000/01/rdf-schema#comment"Although metastasis-associated protein 1 (MTA1) has recently been shown as a DNA damage responsive protein, the underlying mechanism for its role in DNA double-strand break (DSB) repair remains unknown. Here, we show that MTA1 controls p53 stability through inhibiting its ubiquitination by E3 ubiquitin ligases mouse double minute 2 (Mdm2) and constitutive photomorphogenic protein 1 (COP1). The underlying mechanisms involve the ability of MTA1 to compete with COP1 to bind to p53 and/or to destabilize COP1 and Mdm2. Consequently, MTA1 regulates the p53-dependent transcription of p53R2, a direct p53 target gene for supplying nucleotides to repair damaged DNA. Depletion of MTA1 impairs p53-dependent p53R2 transcription and compromises DNA repair. Interestingly, these events could be reversed by MTA1 reintroduction, indicating that MTA1 interjects into the p53-dependent DNA repair. Given the fact that MTA1 is widely up-regulated in human cancers, these findings in conjunction with our earlier finding of a crucial role of MTA1 in DSB repair suggest an inherent role of the MTA1-p53-p53R2 pathway in DNA damage response in cancer cells."xsd:string
http://purl.uniprot.org/citations/19837670http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m109.056499"xsd:string
http://purl.uniprot.org/citations/19837670http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m109.056499"xsd:string
http://purl.uniprot.org/citations/19837670http://purl.uniprot.org/core/author"Kumar R."xsd:string
http://purl.uniprot.org/citations/19837670http://purl.uniprot.org/core/author"Kumar R."xsd:string
http://purl.uniprot.org/citations/19837670http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/19837670http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/19837670http://purl.uniprot.org/core/author"Wu X."xsd:string
http://purl.uniprot.org/citations/19837670http://purl.uniprot.org/core/author"Wu X."xsd:string
http://purl.uniprot.org/citations/19837670http://purl.uniprot.org/core/author"Pakala S.B."xsd:string
http://purl.uniprot.org/citations/19837670http://purl.uniprot.org/core/author"Pakala S.B."xsd:string
http://purl.uniprot.org/citations/19837670http://purl.uniprot.org/core/author"Rayala S.K."xsd:string
http://purl.uniprot.org/citations/19837670http://purl.uniprot.org/core/author"Rayala S.K."xsd:string
http://purl.uniprot.org/citations/19837670http://purl.uniprot.org/core/author"Li D.Q."xsd:string
http://purl.uniprot.org/citations/19837670http://purl.uniprot.org/core/author"Li D.Q."xsd:string
http://purl.uniprot.org/citations/19837670http://purl.uniprot.org/core/author"Divijendra Natha Reddy S."xsd:string
http://purl.uniprot.org/citations/19837670http://purl.uniprot.org/core/author"Divijendra Natha Reddy S."xsd:string
http://purl.uniprot.org/citations/19837670http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19837670http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19837670http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/19837670http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/19837670http://purl.uniprot.org/core/pages"34545-34552"xsd:string
http://purl.uniprot.org/citations/19837670http://purl.uniprot.org/core/pages"34545-34552"xsd:string