A putative role for the phosphotyrosine adaptor protein ShcD in Vav2-mediated cell signaling
ShcD is the newest member of the Shc family of molecular adaptors. Its signaling potential is alluded to by the presence of both PTB and SH2 phosphotyrosine binding domains, as well as recognition sequences for SH3, SH2, and PTB domains. These physical features facilitate aggregation of signaling complexes for stringent regulation of cellular processes. In the developing mouse embryo, ShcD is tyrosine phosphorylated and widely expressed; however, over time ShcD is largely restricted to the brain. Recent literature suggests that alterations in ShcD expression may impair differentiation and promote migration, and that ShcD is upregulated in several nervous system cancers and promotes a metastatic phenotype in melanoma. Here we demonstrate that colorectal adenocarcinoma represents an additional cell model with which to study ShcD, and provide evidence for molecular interaction with Vav2 in vitro. These data provide important insights into the role of ShcD in signaling pathways that control cellular function.