GAB2 in Active FLT3:GRB2:GAB2 is phosphorylated

Stable Identifier
Reaction [omitted]
Homo sapiens
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Feline McDonough Sarcoma-like tyrosine kinase (FLT3) is a member of the class III tyrosine kinase receptor family. Ligand binding induces conformational changes in the FLT3 receptor, which facilitates its dimerization and autophosphorylation. Once fully active, FLT3 receptors can associate with growth factor receptor-bound protein 2 (GRB2), which then recruits GRB2-associated-binding protein 2 (GAB2). Consequently, GAB2 is phosphorylated (Zhang et al. 2000, Masson et al. 2009, Chonabayashi et al. 2013). The precise phosphorylation mechanism of GAB2 is unclear. Experiments confirming this event were performed in mouse cells.
Literature References
PubMed ID Title Journal Year
19438505 A role of Gab2 association in Flt3 ITD mediated Stat5 phosphorylation and cell survival

Masson, K, Sun, J, Khan, R, Liu, T, Rönnstrand, L

Br. J. Haematol. 2009
11027663 Flt3 ligand induces tyrosine phosphorylation of gab1 and gab2 and their association with shp-2, grb2, and PI3 kinase

Zhang, S, Broxmeyer, HE

Biochem. Biophys. Res. Commun. 2000
23168613 Direct binding of Grb2 has an important role in the development of myeloproliferative disease induced by ETV6/FLT3

Ishikawa, T, Kawamata, S, Ohno, T, Chonabayashi, K, Hishizawa, M, Uchiyama, T, Nagai, Y, Takaori-Kondo, A

Leukemia 2013
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