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http://purl.uniprot.org/citations/7541045http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7541045http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7541045http://www.w3.org/2000/01/rdf-schema#comment"Insulin receptor substrate-1 (IRS-1) and SHC become rapidly phosphorylated upon tyrosines after insulin-like growth factor I receptor (IGFIR) activation. In this study we demonstrate that IRS-1, SHC, and the p85 subunit of phosphatidylinositol 3-kinase interact directly and specifically with the IGFIR. The interaction of all three proteins is dependent upon IGFIR kinase activity and, furthermore, substitution of Tyr-950 with Phe within the NPEY motif of the IGFIR eliminated interaction with both SHC and IRS-1 but had no effect upon p85 interaction. We show that residues 160-516 of IRS-1 and 1-238 of SHC are sufficient and necessary for receptor interaction in the yeast two-hybrid assay. We also demonstrate a direct in vitro interaction between the IGFIR and a fusion protein containing SHC amino acids 1-238. No interaction was observed with a SHC protein containing only the SH2 domain. We conclude that SHC and IRS-1 interact with the tyrosine-phosphorylated NPEY motif of the IGFIR, and that both proteins interact via related motifs located in their amino termini. We conclude that the interactions of SHC and IRS-1 with the IGFIR are similar to those which we have previously defined with the insulin receptor."xsd:string
http://purl.uniprot.org/citations/7541045http://purl.org/dc/terms/identifier"doi:10.1074/jbc.270.26.15639"xsd:string
http://purl.uniprot.org/citations/7541045http://purl.org/dc/terms/identifier"doi:10.1074/jbc.270.26.15639"xsd:string
http://purl.uniprot.org/citations/7541045http://purl.uniprot.org/core/author"Gustafson T.A."xsd:string
http://purl.uniprot.org/citations/7541045http://purl.uniprot.org/core/author"Gustafson T.A."xsd:string
http://purl.uniprot.org/citations/7541045http://purl.uniprot.org/core/author"O'Neill T.J."xsd:string
http://purl.uniprot.org/citations/7541045http://purl.uniprot.org/core/author"O'Neill T.J."xsd:string
http://purl.uniprot.org/citations/7541045http://purl.uniprot.org/core/author"Craparo A."xsd:string
http://purl.uniprot.org/citations/7541045http://purl.uniprot.org/core/author"Craparo A."xsd:string
http://purl.uniprot.org/citations/7541045http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7541045http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7541045http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7541045http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7541045http://purl.uniprot.org/core/pages"15639-15643"xsd:string
http://purl.uniprot.org/citations/7541045http://purl.uniprot.org/core/pages"15639-15643"xsd:string
http://purl.uniprot.org/citations/7541045http://purl.uniprot.org/core/title"Non-SH2 domains within insulin receptor substrate-1 and SHC mediate their phosphotyrosine-dependent interaction with the NPEY motif of the insulin-like growth factor I receptor."xsd:string
http://purl.uniprot.org/citations/7541045http://purl.uniprot.org/core/title"Non-SH2 domains within insulin receptor substrate-1 and SHC mediate their phosphotyrosine-dependent interaction with the NPEY motif of the insulin-like growth factor I receptor."xsd:string
http://purl.uniprot.org/citations/7541045http://purl.uniprot.org/core/volume"270"xsd:string
http://purl.uniprot.org/citations/7541045http://purl.uniprot.org/core/volume"270"xsd:string
http://purl.uniprot.org/citations/7541045http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7541045
http://purl.uniprot.org/citations/7541045http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7541045
http://purl.uniprot.org/citations/7541045http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7541045
http://purl.uniprot.org/citations/7541045http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7541045