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How receptor tyrosine kinases activate ras

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      The RTKs activated by dimerization induce autophosphorylations at the multiple tyrosine residues, and that provide docking sites for several different proteins with src homology 2 (SH2) domain such as p110 subunit of phosphatidylinositide 3-kinases (PI3K), Shc, SHP-2, and growth factor receptor bound protein 2 (GRB2) etc. (Porter and Vaillancourt, 1998; Reuter et al., 2000). Autophosphorylated receptor binds to the SH2 domain of Grb2, which is bound to Sos via its SH3 domain, followed by activation of RAS by exchanging GDP to GTP guanine nucleotide (Porter and Vaillancourt, 1998; Reuter et al., 2000; Schlessinger, 1993) (Fig. 2). The activated GTP bound RAS further transmits its signal to the downstream RAF-MEK-ERK and PI3K-Akt signaling cascades (Daum et al., 1994; Van Aelst et al., 1994).

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