The FRS family of scaffolding adaptor proteins has two members, FRS2 (also known as FRS2 alpha) and FRS3 (also known as FRS2beta or SNT-2). Activation of FGFR tyrosine kinase allows FRS proteins to become phosphorylated on tyrosine residues and then bind to the adaptor GRB2 and the tyrosine phosphatase PPTN11/SHP2. Subsequently, PPTN11 activates the RAS-MAP kinase pathway and GRB2 activates the RAS-MAP kinase , PI-3-kinase and ubiquitinations/degradation pathways by binding to SOS, GAB1 and CBL, respectively, via the SH3 domains of GRB2. FRS2 acts as a central mediator in FGF signaling mainly because it induces sustained levels of activation of ERK with ubiquitous expression.
Schlessinger, J, Kouhara, H, Lax, I, Gotoh, N, Hadari, YR
Gotoh, N
Schlessinger, J, Eswarakumar, VP, Lax, I
Hays, S, Kern, FG, Rentz, SS, Qu, Z, Manuvakhova, M, Thottassery, JV, Westbrook, L
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