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The p97 [Eps8] protein, a substrate for EGF-R tyrosine kinase, contains an SH3 domain, but lacks a functional SH2 domain. Antibodies to Eps8 recognize the 97 kDa protein and a less abundant 68 kDa protein. Both forms are tyrosine-phosphorylated following treatment of cells with EGF. It is likely that p68 [Eps8] is synthesized from an alternatively spliced mRNA since two major Eps8-specific mRNAs are detected by Northern analysis. Co-immunoprecipitation studies have demonstrated a physical association between the Eps8 protein and the EGF-R both in vivo and in vitro. For many EGF-R substrates, this interaction is mediated through an SH2 domain of the substrate. Since Eps8 lacks a well defined SH2 domain and a fusion protein containing the SH2-like region of Eps8 could not bind EGF-R, the mechanism of Eps8-EGF-R association remains unclear. Overexpression of Eps8 in fibroblasts and hematopoietic cells results in an increased mitogenic response to EGF, suggesting that Eps8 has a role in the modulation of EGF-R function.
