Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Ota J,Sato K,Kimura F,Wakimoto N,Nakamura Y,Nagata N,Suzu S,Yamada M,Shimamura S,Motoyoshi Kdoi
10.1016/s0014-5793(99)01767-6keywords:
subject
Has Abstractpub_date
2000-01-21 00:00:00pages
96-100issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(99)01767-6journal_volume
466pub_type
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