| http://purl.uniprot.org/citations/8776723 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8776723 | http://www.w3.org/2000/01/rdf-schema#comment | "We have used the yeast two-hybrid system to study the interaction between the IGF-I receptor and two putative substrates, IRS-1 and Shc. In addition, we have identified Grb10 as a protein that binds to the insulin-like growth factor I (IGF-I) receptor. This two-hybrid system (the interaction trap) utilizes a hybrid protein containing the LexA DNA-binding domain fused to the intracellular portion of the IGF-I receptor (LexA-IGFIR beta) and hybrids containing an activation domain fused to either IRS-1 (Ad-IRS-1), Shc (Ad-Shc), or a cDNA library. A positive interaction of LexA-IGFIR beta with the activation domain hybrid results in activation of reporter genes, LacZ and LEU2, in the yeast. Western blotting of extracts from transformed yeast demonstrated that the LexA-IGFIR beta fusion protein was expressed and phosphorylated on tyrosine residues. Coexpression of LexA-IGFIR beta with Ad-IRS-1 resulted in strong activation of both reporter genes; activation did not occur with a kinase-negative receptor mutant. IRS-1 residues 160-516 were sufficient for this strong interaction. Coexpression of LexA-IGFIR beta with Ad-Shc also resulted in strong activation of both LacZ and LEU2 reporter genes. This interaction was also dependent upon a tyrosine kinase-active receptor and required tyrosine 950 in the juxtamembrane region of the receptor. An N-terminal fragment of Shc (amino acids 1-232) interacted almost as strongly as full-length Shc whereas the Shc SH2 domain only activated the more sensitive LEU2 reporter. Full-length Shc was phosphorylated on tyrosine when coexpressed with IGFIR beta but not when coexpressed with the kinase-negative receptor mutant. To identify additional proteins that interact with the IGFIRs, a human fetal brain cDNA library was screened using the interaction trap system. This analysis identified partial cDNAs for Grb10. Coexpression of LexA-IGFIR beta with Ad-Grb10 resulted in strong activation of both LacZ and LEU2 reporter genes; this interaction was dependent upon a tyrosine kinase-active receptor but did not require tyrosine 950."xsd:string |
| http://purl.uniprot.org/citations/8776723 | http://purl.org/dc/terms/identifier | "doi:10.1210/mend.10.6.8776723"xsd:string |
| http://purl.uniprot.org/citations/8776723 | http://purl.uniprot.org/core/author | "Nissley S.P."xsd:string |
| http://purl.uniprot.org/citations/8776723 | http://purl.uniprot.org/core/author | "Dey B.R."xsd:string |
| http://purl.uniprot.org/citations/8776723 | http://purl.uniprot.org/core/author | "Furlanetto R.W."xsd:string |
| http://purl.uniprot.org/citations/8776723 | http://purl.uniprot.org/core/author | "Lopaczynski W."xsd:string |
| http://purl.uniprot.org/citations/8776723 | http://purl.uniprot.org/core/author | "Frick K."xsd:string |
| http://purl.uniprot.org/citations/8776723 | http://purl.uniprot.org/core/date | "1996"xsd:gYear |
| http://purl.uniprot.org/citations/8776723 | http://purl.uniprot.org/core/name | "Mol Endocrinol"xsd:string |
| http://purl.uniprot.org/citations/8776723 | http://purl.uniprot.org/core/pages | "631-641"xsd:string |
| http://purl.uniprot.org/citations/8776723 | http://purl.uniprot.org/core/title | "Evidence for the direct interaction of the insulin-like growth factor I receptor with IRS-1, Shc, and Grb10."xsd:string |
| http://purl.uniprot.org/citations/8776723 | http://purl.uniprot.org/core/volume | "10"xsd:string |
| http://purl.uniprot.org/citations/8776723 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8776723 |
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