Title : Hierarchy of binding sites for Grb2 and Shc on the epidermal growth factor receptor.

Pub. Date : 1994 Aug

PMID : 7518560






5 Functional Relationships(s)
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Protein Name
Organism
1 Results of co-immunoprecipitation experiments suggest that phosphotyrosines Y-1068 and Y-1173 mediate the binding of Grb2 to the EGFR. phosphotyrosines y-1068 growth factor receptor bound protein 2 Homo sapiens
2 Results of co-immunoprecipitation experiments suggest that phosphotyrosines Y-1068 and Y-1173 mediate the binding of Grb2 to the EGFR. Y-1173 growth factor receptor bound protein 2 Homo sapiens
3 Competition experiments with synthetic phosphopeptides corresponding to known autophosphorylation sites on the EGFR demonstrated that phosphopeptides containing Y-1068, and to a lesser extent Y-1086, were able to inhibit the binding of Grb2 to the EGFR, while a Y-1173 peptide did not. y-1068 growth factor receptor bound protein 2 Homo sapiens
4 These findings were confirmed by using a dephosphorylation protection assay and by measuring the dissociation constants of Grb2"s SH2 domain to tyrosine-phosphorylated peptides, using real-time biospecific interaction analysis (BIAcore). Tyrosine growth factor receptor bound protein 2 Homo sapiens
5 These analyses reveal a hierarchy of interactions between Grb2 and Shc with the EGFR and indicate that Grb2 can bind the tyrosine-phosphorylated EGFR directly, as well as indirectly via Shc. Tyrosine growth factor receptor bound protein 2 Homo sapiens