SHP2 binds to the active receptor Authored: Garapati, P V, Jassal, B, 2008-11-24 10:14:27 Edited: Garapati, P V, Jassal, B, 2008-11-24 10:14:27 Protein-tyrosine phosphatase 2C (SHP2) is ubiquitously expressed and has two SH2 domains, both of which need to be bound to phosphorylated tyrosine residues for full activation of catalytic activity. SHP-2 binds with high affinity to Tyr 1009 of the PDGF beta-receptor and with lower affinity to Tyr 763; it also binds to the alpha-receptor and Tyr 720 in the interkinase domain has been implicated in this binding. <br>The phosphatase is able to dephosphorylate autophosphorylated PDGF receptors and substrates for PDGF receptors so SHP2 can be thought of as a negative regulator of signaling from PDGF receptors. SHP2 may be involved in positive signaling by binding Grb2/Sos1 and dephosphorylating the COOH-terminal tyrosine of Src, factors important for Src activation. Pubmed7691811 Pubmed9739761 Reactome Database ID Release 43186778 Reactome, http://www.reactome.org ReactomeREACT_16960 Reviewed: Heldin, CH, 2008-11-23 19:29:34 PDGF:Phospho-PDGF receptor dimer:SHP2 PDGF:Phospho-PDGF receptor dimer