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J. Biol. Chem., Vol. 256, Issue 22, 11381-11384, 11, 1981
E Erikson, DJ Shealy and RL Erikson
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.
Evidence that viral transforming gene products and epidermal growth factor stimulate phosphorylation of the same cellular protein with similar specificity
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