Several tyrosine residues are present in the intracellular domain of Kdr; some have been shown to be critical for the recruitment of specific SH2 (Src homology 2) domain-containing adapter and target proteins to trigger downstream signaling events. Binding to and phosphorylation of Plcg1 leads to increased activity of the enzyme and formation of the second messengers IP3 and DAG; DAG activates Prkca, b and/or z which leads to activation of the RAF/MEK/ERK pathway.