Evidence that viral transforming gene products and epidermal growth factor stimulate phosphorylation of the same cellular protein with similar specificity.

Abstract

Treatment of A-431 human epidermoid carcinoma cells with epidermal growth factor (EGF) was shown to enhance the phosphorylation of a Mr = 34,000 protein. Because the phosphorylation of an analogous protein is enhanced in various cell lines transformed by Rous sarcoma virus (RSV) (Erikson, E., and Erikson, R. L. (1980) Cell 21, 829-836), we characterized the phosphorylation of the A-431 Mr = 34,000 protein under these two conditions in order to determine whether there are common pathways between viral transformation and EGF stimulation. The results of tryptic phosphopeptide mapping and phosphoamino acid analysis showed that the Mr = 34,000 protein was phosphorylated in an identical manner by the EGF-stimulated protein kinase activity and by the protein kinase activity of the RSV transformation-specific protein or of its normal cell homolog. Although the specific protein kinase that phosphorylates the Mr = 34,000 protein under conditions of EGF-stimulation is not yet identified, these studies demonstrate that at least one consequence of EGF stimulation is identical with one of the consequences of viral transformation.