Receptor tyrosine kinases (RTKs) are a major class of cell surface proteins involved in Signal Transduction. Human cells contain ~60 RTKs, grouped into 20 subfamilies based on their domain architecture. All RTK subfamilies are characterized by an extracellular ligand-binding domain, a single transmembrane region and an intracellular region consisting of the tyrosine kinase domain and additional regulatory and protein interaction domains. In general, RTKs associate into dimers upon ligand binding and are activated by autophosphorylation on conserved intracellular tyrosine residues. Autophosphorylation increases the catalytic efficiency of the receptor and provides binding sites for the assembly of downstream signaling complexes (reveiwed in Lemmon and Schlessinger, 2010). Common signaling pathways activated downstream of RTK activation include RAF/MAP kinase cascades (reviewed in McKay and Morrison, 2007 and Wellbrock et al 2004), AKT signaling (reviewed in Manning and Cantley, 2007) and PLC-gamma mediated signaling (reviewed in Patterson et al). Activation of these pathways ultimately results in changes in gene expression and cellular metabolism.