Association of Cbl with Fms and p85 in response to macrophage colony-stimulating factor.

Tyrosine phosphorylation of Cbl and its association with signal-transducing molecules in response to macrophage colony-stimulating factor (M-CSF) were analyzed by using cell lines which express the wild-type and a mutant M-CSF receptor, Fms. We found that in a clone, F723 TF-1 cells expressing mutant Fms in which tyrosine 723 had ...
been substituted with phenylalanine, the M-CSF stimulation-dependent association between Cbl and Fms was markedly impaired. However, phosphorylation of Cbl and its association with the p85 subunit of phosphatidylinositol 3-kinase were induced in these mutant cells as seen in the wild-type fms transfectant. These results suggest that phosphorylation of tyrosine 723 is particularly important for the recruitment of Cbl to the M-CSF receptor, but is not required for the phosphorylation and binding of Cbl to signal-transducing molecules such as p85.
Mesh Terms:
Amidohydrolases, Amino Acid Substitution, Aminopeptidases, Animals, Base Sequence, Clone Cells, DNA Primers, Humans, Macrophage Colony-Stimulating Factor, Mice, Mutagenesis, Site-Directed, Phosphatidylinositol 3-Kinases, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-cbl, Receptor, Macrophage Colony-Stimulating Factor, Recombinant Proteins, Signal Transduction, Substrate Specificity, Transfection, Tyrosine, Ubiquitin-Protein Ligases
FEBS Lett.
Date: Jan. 21, 2000
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