Identification of the major tyrosine kinase substrate in signaling complexes formed after engagement of Fc gamma receptors.
We have recently identified the protein product of the c-cbl proto-oncogene as an SH3 binding protein expressed in macrophages. To investigate the possibility that p120c-cbl is involved in signaling pathways initiated by cell surface receptors for IgG (Fc gamma R), lysates of HL60 cells were examined for tyrosine phosphorylation of ... p120c-cbl upon Fc gamma R engagement. Our findings demonstrate that p120c-cbl is tyrosine-phosphorylated upon Fc gamma R engagement and that this molecule represents the major tyrosine kinase substrate in this signaling pathway. Protein complexes containing p120c-cbl, p72syk, and p56lyn were observed either in resting or activated cells. In vitro studies showed that the direct association between p120c-cbl and p56lyn was mediated by the SH3 domain of p56lyn.
Mesh Terms:
Enzyme Precursors, Humans, Intracellular Signaling Peptides and Proteins, Phosphorylation, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-cbl, Receptors, IgG, Tumor Cells, Cultured, Tyrosine, Ubiquitin-Protein Ligases, src-Family Kinases
Enzyme Precursors, Humans, Intracellular Signaling Peptides and Proteins, Phosphorylation, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-cbl, Receptors, IgG, Tumor Cells, Cultured, Tyrosine, Ubiquitin-Protein Ligases, src-Family Kinases
J. Biol. Chem.
Date: Apr. 21, 1995
PubMed ID: 7721825
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