Abstract
The interaction between tyrosme phosphorylated growth-factor receptors and Src Homology 2 (SH2)-domain-containing proteins plays a critical role in growth-factor mediated signal transduction (1). The SH2 domains bind to receptors at phosphotyrosine residues with specificity dictated by ammo acids that lie carboxy-terminal to the phosphotyrosme. Identification of new SH2-domain proteins has provided great insight into signaling by growth-factor receptors. Our work has focused on cloning new SH2-domain proteins by screening bacterial-expression libraries with tyrosine phosphorylated epidermal growth-factor receptor (EGF-receptor). We call this method CORT for cloning of receptor targets and the proteins isolated Grbs for growth-factor receptor bound (2–6) The clomng of Grb2 with this technique helped to elucldate the signaling pathway that leads from growth-factor receptors to Ras (7),
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© 1998 Humana Press Inc.
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Yajnik, V., Blaikie, P., Margolis, B. (1998). Cloning and Mutational Analysis of the Shc-Phosphotyrosine Interaction/Phosphotyrosine-Binding Domain. In: Bar-Sagi, D. (eds) Transmembrane Signaling Protocols. Methods In Molecular Biology™, vol 84. Humana Press. https://doi.org/10.1385/0-89603-488-7:223
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DOI: https://doi.org/10.1385/0-89603-488-7:223
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