SHP2 binds to the active receptor

Stable Identifier
Reaction [binding]
Homo sapiens
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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.
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.
Literature References
PubMed ID Title Journal Year
9739761 Signal transduction via platelet-derived growth factor receptors

Ostman, A, Heldin, CH, Rönnstrand, L

Biochim Biophys Acta 1998
7691811 Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor

Bennett, AM, Shoelson, SE, Kashishian, AS, Neel, BG, Sugimoto, S, Lechleider, RJ, Walsh, CT, Cooper, JA

J Biol Chem 1993
Orthologous Events
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