Identification of multiple novel polypeptide substrates of the v-src, v-yes, v-fps, v-ros, and v-erb-B oncogenic tyrosine protein kinases utilizing antisera against phosphotyrosine.

Antibodies to phosphotyrosine were used to identify proteins phosphorylated on tyrosine in chicken embryo fibroblasts transformed by the oncogenes, v-src, v-yes, v-fps, v-ros, or v-erb-B. These antibodies allowed detection of a minimum of 50, 44, and 47 bands in immunoblots of cellular lysates from fibroblasts transformed by v-src, v-yes, or v-fps respectively. Eight of these bands were also detected in fibroblasts transformed by v-ros and v-erb-B, suggesting that the cellular transformation induced by v-ros, v-erb-B, v-src, v-yes, and v-fps may be achieved by the phosphorylation of some of the same proteins. The viruses SD10 and SD11 are point mutants of the Prague-C strain of Rous sarcoma virus that encode non-myristylated p60v-src. They do not induce the transformation of chicken fibroblasts. Approximately thirty bands were detected by antibodies to phosphotyrosine in fibroblasts transformed by wild-type Prague-RSV-C, only four of which were not substrates nonmyristylated mutant p60v-src. This suggests that the phosphorylation of a large subset of the substrates of p60v-src is not sufficient for transformation.