Ligand-induced tyrosine kinase activity of the colony-stimulating factor 1 receptor in a murine macrophage cell line.
Metabolic labeling of simian virus 40-immortalized murine macrophages with 32Pi and immunoblotting with antibodies to phosphotyrosine demonstrated that the c-fms proto-oncogene product (colony-stimulating factor 1 [CSF-1] receptor) was phosphorylated on tyrosine in vivo and rapidly degraded in response to CSF-1. Stimulation of the CSF-1 receptor also induced immediate phosphorylation of several other cellular proteins on tyrosine. By contrast, the mature cell surface glycoprotein encoded by the v-fms oncogene was phosphorylated on tyrosine in the absence of CSF-1, suggesting that it functions as a ligand-independent kinase.
Downing
J R
JR
Department of Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105.
Rettenmier
C W
CW
Sherr
C J
CJ
D000818:Animals; D002460:Cell Line; D003115:Colony-Stimulating Factors / Q000378:metabolism*; D007700:Kinetics; D008024:Ligands; D008264:Macrophages / Q000378:metabolism; D051379:Mice; D010761:Phosphorus Radioisotopes; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D011519:Proto-Oncogenes; D011956:Receptors, Cell Surface / Q000378:metabolism*; D016184:Receptors, Colony-Stimulating Factor
D003115:Colony-Stimulating Factors; D008024:Ligands; D010761:Phosphorus Radioisotopes; D011956:Receptors, Cell Surface; D016184:Receptors, Colony-Stimulating Factor; D011505:Protein-Tyrosine Kinases