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Volume 270, Number 35, Issue of September 01, pp. 20242-20245, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Tyrosine Phosphorylation of the c-cbl Proto-oncogene Protein Product and Association with Epidermal Growth Factor (EGF) Receptor upon EGF Stimulation

(Received for publication, May 25, 1995; and in revised form, July 7, 1995)

Maria L. Galisteo ,&nbsp;<WBR> Ivan Dikic ,&nbsp;<WBR> Andreas G. Batzer ,&nbsp;<WBR> Wallace Y. Langdon ,&nbsp;<WBR> Joseph Schlessinger

The murine retroviral oncogene v-cbl induces pre-B cell lymphomas and myelogenous leukemias. The protein product of the mammalian c-cbl proto-oncogene is a widely expressed cytoplasmic 120-kDa protein (p120) whose normal cellular function has not been determined. Here we show that upon stimulation of human epidermal growth factor (EGF) receptor, p120 becomes strongly tyrosine-phosphorylated and associates with activated EGF receptor in vivo. A GST fusion protein containing amino acids 1-486 of p120, including a region highly conserved in nematodes, binds directly to the autophosphorylated carboxyl-terminal tail of the EGF receptor. Platelet-derived growth factor (PDGF), fibroblast growth factor (FGF), or nerve growth factor (NGF) stimulation also results in tyrosine phosphorylation of p120. Recent genetic studies in Caenorhabditis elegans indicate that Sli-1, a p120 homologue, plays a negative regulatory role in control of the Ras signaling pathway initiated by the C. elegans EGF receptor homologue. Our results indicate that p120 is involved in an early step in the EGF signaling pathway that is conserved from nematodes to mammals.



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