Reactome | Binding of Gab2 to tyrosine phosphorylated Shc promotes the ...

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created	[InstanceEdit:912521] Jupe, S, 2010-07-09
dbId	912524
displayName	Binding of Gab2 to tyrosine phosphorylated Shc promotes the ...
literatureReference	[LiteratureReference:507990] Gab2 is phosphorylated on tyrosine upon interleukin-2/interleukin-15 stimulation in mycosis-fungoides-derived tumor T cells and associates inducibly with SHP-2 and Stat5a [LiteratureReference:508013] Cloning of p97/Gab2, the major SHP2-binding protein in hematopoietic cells, reveals a novel pathway for cytokine-induced gene activation [LiteratureReference:507926] New role for Shc in activation of the phosphatidylinositol 3-kinase/Akt pathway
modified	[InstanceEdit:975849] Jupe, S, 2010-10-05
schemaClass	Summation
text	Binding of Gab2 to tyrosine phosphorylated Shc promotes the phosphorylation of Gab2 by an unknown kinase. Gab2 becomes tyrosine phosphorylated in response to IL-2 (Brockdorff et al. 2001) and IL-3 (Gu et al. 1998). Chimeric receptors were used to demonstrate that Shc is sufficient for Gab2 tyrosine phosphorylation. In response to IL-3, Grb2 was also required, reflecting that Gab2 is recruited to the activated cytokine receptor complex as a complex of Gab2:Grb2 (Gu et al. 2000).

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