FRS2 family docking proteins with overlapping roles in activation of MAP kinase have distinct spatial‐temporal patterns of expression of their transcripts

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Abstract
FRS2α and FRS2β, two members of the FRS2 family of docking proteins, become tyrosine phosphorylated in response to fibroblast growth factor (FGF) or nerve growth factor (NGF) stimulation. Tyrosine phosphorylated FRS2α serves as a platform for the recruitment of multiple signaling proteins for activation of the Ras‐mitogen‐activated protein (MAP) kinase signaling cascade. We report that Frs2α and Frs2β have distinct spatio‐temporal expression patterns in mouse embryos. We further show that FRS2β can compensate for the loss of FRS2α for activation of MAP kinase when expressed in fibroblasts from Frs2α −/− mouse embryos. We propose that the FRS2 family proteins have distinct roles in vivo through activation of common signaling proteins including MAP kinase.