Synergistic interaction of p185c-neu and the EGF receptor leads to transformation of rodent fibroblasts

Yasuo Kokai, Jeffrey N. Myers, Takuro Wada, Valerie I. Brown, Charles M. LeVea, James G. Davis, Kunio Dobashi, Mark I. Greene

Research output: Contribution to journalArticlepeer-review

284 Scopus citations


The protein product of the rodent neu oncogene, p185neu, is a tyrosine kinase with structural similarity to the epidermal growth factor receptor (EGFR). Transfection and subsequent overexpression of the human p185c-erbB-2 protein transforms NIH 3T3 cells in vitro. However, NIH 3T3 cells are not transformed by overexpressed rodent p185c-neu. NIH 3T3 transfectants overexpressing EGF receptors are not transformed unless EGF is added to the cultures, and, even then, they are incompletely transformed. Several groups have recently demonstrated EGF-induced, EGFR-mediated phosphorylation of p185c-neu. During efforts to characterize the interaction of p185c-neu with EGFR further, we created cell lines that simultaneously overexpress both p185c-neu and EGFR and observed that these cells become transformed. These observations demonstrate that two distinct, overexpressed tyrosine kinases can act synergistically to transform NIH 3T3 cells, thus identifying a novel mechanism that can lead to transformation.

Original languageEnglish (US)
Pages (from-to)287-292
Number of pages6
Issue number2
StatePublished - Jul 28 1989

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)


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