Src homology 2 (SH2) domains bind specifically to tyrosine-phosphorylated proteins that temporally participate in signal transduction events (1). Shc-like protein (Sck) is a neuronal adaptor protein that contains an N-terminal PTB (phosphotyrosine binding) domain, a collagen homology (CH) domain, and a conserved C-terminal SH2 domain (2,3). Human Sck transcripts are present at high levels in liver, pancreas, prostate and ovary (4,5). In vascular endothelial cells, Sck participates in VEGF-induced signal transduction (6). Treatment of human umbilical vein endothelial (HUVEC) cells with VEGF induces recruitment of Sck to tyrosine-1175 of the kinase insert domain-containing receptor (KDR) and enhances Sck tyrosine phosphorylation (7,8).