Individual epidermal growth factor receptor autophosphorylation sites do not stringently define association motifs for several SH2-containing proteins.

摘要: To determine whether individual autophosphorylation sites in the epidermal growth factor (EGF) receptor define specific interaction for vivo association of signal transduction proteins that contain src homology 2 (SH2) domains, capacity wild-type and mutant EGF receptors to associate with several SH2 domain-containing has been assayed. Mutants included single site mutations at each five which multiple were removed by point mutation or deletion carboxyl-terminal residues. Receptor association, as measured coimmunoprecipitation, determined phospholipase C-gamma 1, ras GTPase-activating protein, p85 subunit phosphatidylinositol 3-kinase, collagen protein. In contrast data obtained mutants other tyrosine kinases, none was dramatically impaired its any these SH2-containing proteins. However, completely abrogated when all mutated deletion. These results indicate are not stringently required recognition different substrates. Thus, seem be flexible and/or compensatory their mediate four