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cbl was identified in the genome of a transforming retrovirus from a mouse pre-B cell lymphoma. The product of mammalian c-cbl, p120[cbl], is a widely expressed cytoplasmic protein with several distinctive domains including a RING finger motif and a large proline-rich domain. Although the normal cellular function of c-Cbl has not yet been determined, it associates with many well known signal transduction proteins. In lymphoid cells, c-Cbl is a substrate of TCR-activated protein tyrosine kinases. In addition, stimulation with EGF, PDGF, FGF, or NGF results in tyrosine-phosphorylation of c-Cbl in lymphoid and other cell types. It forms a signaling complex with Grb2 in T cells and is a SH3 and SH2 binding protein which associates with many other cytoplasmic signaling proteins including Btk, Src, fyn, lck, and the β isoform of PI-3 kinase. Thus, c-Cbl may be an important adaptor protein in growth factor and T-cell receptor signaling pathways.Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blotting
