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http://purl.uniprot.org/citations/21212262http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21212262http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21212262http://www.w3.org/2000/01/rdf-schema#comment"Mammalian Sterile 20-like kinase 1 (MST1) protein kinase plays an important role in the apoptosis induced by a variety of stresses. The MST1 is a serine/threonine kinase that is activated upon apoptotic stimulation, which in turn activates its downstream targets, JNK/p38, histone H2B and FOXO. It has been reported that overexpression of MST1 initiates apoptosis by activating p53. However, the molecular mechanisms underlying MST1-p53 signaling during apoptosis are unclear. Here, we report that MST1 promotes genotoxic agent-induced apoptosis in a p53-dependent manner. We found that MST1 increases p53 acetylation and transactivation by inhibiting the deacetylation of Sirtuin 1 (Sirt1) and its interaction with p53 and that Sirt1 can be phosphorylated by MST1 leading to the inhibition of Sirt1 activity. Collectively, these findings define a novel regulatory mechanism involving the phosphorylation of Sirt1 by MST1 kinase which leads to p53 activation, with implications for our understanding of signaling mechanisms during DNA damage-induced apoptosis."xsd:string
http://purl.uniprot.org/citations/21212262http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.182543"xsd:string
http://purl.uniprot.org/citations/21212262http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.182543"xsd:string
http://purl.uniprot.org/citations/21212262http://purl.uniprot.org/core/author"Bai Y."xsd:string
http://purl.uniprot.org/citations/21212262http://purl.uniprot.org/core/author"Bai Y."xsd:string
http://purl.uniprot.org/citations/21212262http://purl.uniprot.org/core/author"Dong Y."xsd:string
http://purl.uniprot.org/citations/21212262http://purl.uniprot.org/core/author"Dong Y."xsd:string
http://purl.uniprot.org/citations/21212262http://purl.uniprot.org/core/author"Wu J."xsd:string
http://purl.uniprot.org/citations/21212262http://purl.uniprot.org/core/author"Wu J."xsd:string
http://purl.uniprot.org/citations/21212262http://purl.uniprot.org/core/author"Wang Y."xsd:string
http://purl.uniprot.org/citations/21212262http://purl.uniprot.org/core/author"Wang Y."xsd:string
http://purl.uniprot.org/citations/21212262http://purl.uniprot.org/core/author"Yuan F."xsd:string
http://purl.uniprot.org/citations/21212262http://purl.uniprot.org/core/author"Yuan F."xsd:string
http://purl.uniprot.org/citations/21212262http://purl.uniprot.org/core/author"Yuan Z."xsd:string
http://purl.uniprot.org/citations/21212262http://purl.uniprot.org/core/author"Yuan Z."xsd:string
http://purl.uniprot.org/citations/21212262http://purl.uniprot.org/core/author"Xie Q."xsd:string
http://purl.uniprot.org/citations/21212262http://purl.uniprot.org/core/author"Xie Q."xsd:string
http://purl.uniprot.org/citations/21212262http://purl.uniprot.org/core/author"Bi W."xsd:string
http://purl.uniprot.org/citations/21212262http://purl.uniprot.org/core/author"Bi W."xsd:string
http://purl.uniprot.org/citations/21212262http://purl.uniprot.org/core/author"Ji G."xsd:string
http://purl.uniprot.org/citations/21212262http://purl.uniprot.org/core/author"Ji G."xsd:string
http://purl.uniprot.org/citations/21212262http://purl.uniprot.org/core/author"Tao W."xsd:string
http://purl.uniprot.org/citations/21212262http://purl.uniprot.org/core/author"Tao W."xsd:string