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http://purl.uniprot.org/citations/11717309http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11717309http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11717309http://www.w3.org/2000/01/rdf-schema#comment"Bad is a pro-apoptotic member of the Bcl-2 family of proteins that is thought to exert a death-promoting effect by heterodimerization with Bcl-X(L), nullifying its anti-apoptotic activity. Growth factors may promote cell survival at least partially through phosphorylation of Bad at one or more of Ser-112, -136, or -155. Our previous work showed that Bad is also phosphorylated in response to cytokines at another site, which we now identify as Ser-170. The functional role of this novel phosphorylation site was assessed by site-directed mutagenesis and analysis of the pro-apoptotic function of Bad in transiently transfected HEK293 and COS-7 cells or by stable expression in the cytokine-dependent cell line, MC/9. In general, mutation of Ser-170 to Ala results in a protein with increased ability to induce apoptosis, similar to the S112A mutant. Mutation of Ser-170 to Asp, mimicking a constitutively phosphorylated site, results in a protein that is virtually unable to induce apoptosis. Similarly, the S112A/S170D double mutant does not cause apoptosis in HEK293 and MC/9 cell lines. These data strongly suggest that phosphorylation of Bad at Ser-170 is a critical event in blocking the pro-apoptotic activity of Bad."xsd:string
http://purl.uniprot.org/citations/11717309http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m109990200"xsd:string
http://purl.uniprot.org/citations/11717309http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m109990200"xsd:string
http://purl.uniprot.org/citations/11717309http://purl.uniprot.org/core/author"Aebersold R."xsd:string
http://purl.uniprot.org/citations/11717309http://purl.uniprot.org/core/author"Aebersold R."xsd:string
http://purl.uniprot.org/citations/11717309http://purl.uniprot.org/core/author"Chen X."xsd:string
http://purl.uniprot.org/citations/11717309http://purl.uniprot.org/core/author"Chen X."xsd:string
http://purl.uniprot.org/citations/11717309http://purl.uniprot.org/core/author"Goodlett D.R."xsd:string
http://purl.uniprot.org/citations/11717309http://purl.uniprot.org/core/author"Goodlett D.R."xsd:string
http://purl.uniprot.org/citations/11717309http://purl.uniprot.org/core/author"Dramsi S."xsd:string
http://purl.uniprot.org/citations/11717309http://purl.uniprot.org/core/author"Dramsi S."xsd:string
http://purl.uniprot.org/citations/11717309http://purl.uniprot.org/core/author"Schubert K."xsd:string
http://purl.uniprot.org/citations/11717309http://purl.uniprot.org/core/author"Schubert K."xsd:string
http://purl.uniprot.org/citations/11717309http://purl.uniprot.org/core/author"Duronio V."xsd:string
http://purl.uniprot.org/citations/11717309http://purl.uniprot.org/core/author"Duronio V."xsd:string
http://purl.uniprot.org/citations/11717309http://purl.uniprot.org/core/author"Hojabrpour P."xsd:string
http://purl.uniprot.org/citations/11717309http://purl.uniprot.org/core/author"Hojabrpour P."xsd:string
http://purl.uniprot.org/citations/11717309http://purl.uniprot.org/core/author"Maiti A."xsd:string
http://purl.uniprot.org/citations/11717309http://purl.uniprot.org/core/author"Maiti A."xsd:string
http://purl.uniprot.org/citations/11717309http://purl.uniprot.org/core/author"Scheid M.P."xsd:string
http://purl.uniprot.org/citations/11717309http://purl.uniprot.org/core/author"Scheid M.P."xsd:string
http://purl.uniprot.org/citations/11717309http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11717309http://purl.uniprot.org/core/date"2002"xsd:gYear