Linked Life Data

48887BiochemicalReaction1678

Source:http://www.reactome.org/biopax/48887BiochemicalReaction1678

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Authored: Orlic-Milacic, M, 2011-11-04, Edited: D'Eustachio, P, 2011-11-07, Edited: Matthews, L, 2011-11-07, Edited: Wu, G, 2011-11-07, Reviewed: Greulich, H, 2011-11-15, Reviewed: Savas, S, 2011-11-15, Tyrosine residue Y992, a docking site for PLC-gamma 1 (PLCG1), is phosphorylated in EGFR cancer mutants and expected to recruit PLC-gamma 1 in the same way as the wild-type EGFR receptor. Phosphorylation of Y992 (corresponding to Y1016 when counting from the first amino acid of the EGFR precursor, prior to cleavage of the 24-amino acid signal peptide at the N-terminus) has been directly demonstrated for the following EGFR cancer mutants: EGFR L858R mutant (Sordella et al. 2004, Choi et al. 2007); EGFR G719S mutant (Choi et al. 2007); EGFR L747_P753delinsS mutant (Sordella et al. 2004, Choi et ak, 2007); EGFR L861Q mutant (Choi et al. 2007); EGFRvIII mutant (Grandal et al. 2007); EGFR A289V mutant (Lee et al. 2006); EGFR D770_N771insNPG mutant (Xu et al. 2007); EGFR D770_N771insNPH mutant (Xu et al. 2007); EGFR V738_K739insKIPVAI mutant (Xu et al. 2007); EGFR M766_A767insASV mutant (Xu et al. 2007).
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PLC-gamma 1 binds to p-EGFR mutants
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