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http://purl.uniprot.org/citations/9885561http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9885561http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9885561http://www.w3.org/2000/01/rdf-schema#comment"Several components in cytokine signaling remain unidentified. We report the cloning and initial characterization of one such component, p97, a widely expressed scaffolding protein distantly related to Drosophila DOS and mammalian Gab1. Upon cytokine, growth factor, or antigen receptor stimulation, p97 becomes tyrosyl phosphorylated and associates with several SH2 domain-containing proteins, including SHP2. Expression of p97 mutants unable to bind SHP2 blocks cytokine-induced c-fos promoter activation, inhibiting Elk1-mediated and STAT5-mediated transactivation. Surprisingly, such mutants do not inhibit MAPK activation. Our results identify p97 as an important regulator of receptor signaling that controls a novel pathway to immediate-early gene activation and suggest multiple functions for SHP2 in cytokine receptor signaling."xsd:string
http://purl.uniprot.org/citations/9885561http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(00)80288-9"xsd:string
http://purl.uniprot.org/citations/9885561http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(00)80288-9"xsd:string
http://purl.uniprot.org/citations/9885561http://purl.uniprot.org/core/author"Gu H."xsd:string
http://purl.uniprot.org/citations/9885561http://purl.uniprot.org/core/author"Gu H."xsd:string
http://purl.uniprot.org/citations/9885561http://purl.uniprot.org/core/author"Burakoff S.J."xsd:string
http://purl.uniprot.org/citations/9885561http://purl.uniprot.org/core/author"Burakoff S.J."xsd:string
http://purl.uniprot.org/citations/9885561http://purl.uniprot.org/core/author"Neel B.G."xsd:string
http://purl.uniprot.org/citations/9885561http://purl.uniprot.org/core/author"Neel B.G."xsd:string
http://purl.uniprot.org/citations/9885561http://purl.uniprot.org/core/author"Pratt J.C."xsd:string
http://purl.uniprot.org/citations/9885561http://purl.uniprot.org/core/author"Pratt J.C."xsd:string
http://purl.uniprot.org/citations/9885561http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9885561http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9885561http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/9885561http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/9885561http://purl.uniprot.org/core/pages"729-740"xsd:string
http://purl.uniprot.org/citations/9885561http://purl.uniprot.org/core/pages"729-740"xsd:string
http://purl.uniprot.org/citations/9885561http://purl.uniprot.org/core/title"Cloning of p97/Gab2, the major SHP2-binding protein in hematopoietic cells, reveals a novel pathway for cytokine-induced gene activation."xsd:string
http://purl.uniprot.org/citations/9885561http://purl.uniprot.org/core/title"Cloning of p97/Gab2, the major SHP2-binding protein in hematopoietic cells, reveals a novel pathway for cytokine-induced gene activation."xsd:string
http://purl.uniprot.org/citations/9885561http://purl.uniprot.org/core/volume"2"xsd:string
http://purl.uniprot.org/citations/9885561http://purl.uniprot.org/core/volume"2"xsd:string
http://purl.uniprot.org/citations/9885561http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9885561
http://purl.uniprot.org/citations/9885561http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9885561