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http://purl.uniprot.org/citations/17374615http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17374615http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17374615http://www.w3.org/2000/01/rdf-schema#comment"NOXA is a BH3-only protein whose expression is induced by certain p53-depenent or independent apoptotic stimuli. Both NOXA and Bim are avid binders of Mcl-1, but a functional linkage between these BH3-only proteins has not yet been reported. In this study, we demonstrate that Mcl-1 binding of endogenously induced NOXA interferes with the ability of Mcl-1 to efficiently sequester endogenous Bim, as Bim is displaced from its complex with Mcl-1. Induced NOXA significantly enhances the UV sensitivity of cells, and the ensuing mitochondrial depolarization is entirely abrogated by Bim knockdown. These results demonstrate a Mcl-1-mediated cross-talk between endogenous NOXA and Bim that occurs upstream of the Bak/Bax-dependent execution of UV-induced mitochondrial depolarization. The current findings demonstrate that the mitochondrial response to an induced expression of NOXA is executed by endogenous Bim and suggest a plausible mechanism for the observed NOXA-Bim linkage."xsd:string
http://purl.uniprot.org/citations/17374615http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m611186200"xsd:string
http://purl.uniprot.org/citations/17374615http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m611186200"xsd:string
http://purl.uniprot.org/citations/17374615http://purl.uniprot.org/core/author"Hou W."xsd:string
http://purl.uniprot.org/citations/17374615http://purl.uniprot.org/core/author"Hou W."xsd:string
http://purl.uniprot.org/citations/17374615http://purl.uniprot.org/core/author"Han J."xsd:string
http://purl.uniprot.org/citations/17374615http://purl.uniprot.org/core/author"Han J."xsd:string
http://purl.uniprot.org/citations/17374615http://purl.uniprot.org/core/author"Goldstein L.A."xsd:string
http://purl.uniprot.org/citations/17374615http://purl.uniprot.org/core/author"Goldstein L.A."xsd:string
http://purl.uniprot.org/citations/17374615http://purl.uniprot.org/core/author"Rabinowich H."xsd:string
http://purl.uniprot.org/citations/17374615http://purl.uniprot.org/core/author"Rabinowich H."xsd:string
http://purl.uniprot.org/citations/17374615http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17374615http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17374615http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17374615http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17374615http://purl.uniprot.org/core/pages"16223-16231"xsd:string
http://purl.uniprot.org/citations/17374615http://purl.uniprot.org/core/pages"16223-16231"xsd:string
http://purl.uniprot.org/citations/17374615http://purl.uniprot.org/core/title"Functional linkage between NOXA and Bim in mitochondrial apoptotic events."xsd:string
http://purl.uniprot.org/citations/17374615http://purl.uniprot.org/core/title"Functional linkage between NOXA and Bim in mitochondrial apoptotic events."xsd:string
http://purl.uniprot.org/citations/17374615http://purl.uniprot.org/core/volume"282"xsd:string
http://purl.uniprot.org/citations/17374615http://purl.uniprot.org/core/volume"282"xsd:string
http://purl.uniprot.org/citations/17374615http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17374615
http://purl.uniprot.org/citations/17374615http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17374615