c-Cbl is inducibly tyrosine-phosphorylated by epidermal growth factor stimulation in fibroblasts, and constitutively tyrosine-phosphorylated and associated with v-Src in v-src-transformed fibroblasts.

The c-cbl gene was cloned as the cellular homolog of the v-cbl oncogene that is the transforming component of a murine tumorigenic retrovirus, CAS NS-1, though the biological roles of c-Cbl remain to be elucidated. We have previously reported that c-Cbl is implicated in the signal transduction triggered by granulocyte-macrophage ...
colony-stimulating factor or erythropoietin in hematopoietic cells. Here, we observed tyrosine phosphorylation of C-cbl in cells expressing epidermal growth factor receptor depending on EGF stimulation and in v-src transformed cells. Furthermore, c-Cbl was revealed to associate with v-Src in vivo. By means of binding experiments using glutathione S-transferase fusion proteins, we have found that the SH2 and SH3 domains of many proteins bind to c-Cbl. These findings strongly suggest that c-Cbl is implicated in a wide variety of signal transduction pathways, including those of EGF receptor and Src protein, as well as in the signaling pathways of hematopoietic cells.
Mesh Terms:
3T3 Cells, Adaptor Proteins, Signal Transducing, Animals, Cell Line, Transformed, Epidermal Growth Factor, Fibroblasts, GRB2 Adaptor Protein, Humans, Leukemia, Mice, Oncogene Protein pp60(v-src), Phosphorylation, Protein Processing, Post-Translational, Proteins, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-cbl, Receptor, Epidermal Growth Factor, Signal Transduction, Tumor Cells, Cultured, Tyrosine, Ubiquitin-Protein Ligases, src Homology Domains
Jpn. J. Cancer Res.
Date: Dec. 01, 1995
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