Association between phosphatidylinositol-3 kinase, Cbl and other tyrosine phosphorylated proteins in colony-stimulating factor-1-stimulated macrophages

Abstract

Colony stimulating factor-1 (CSF-1) stimulation of the macrophage cell line BAC1.2F5 and murine bone marrow-derived macrophages resulted in tyrosine phosphorylation of phosphatidylinositol-3 kinase (PI-3 kinase) p85 alpha and its stable association with several tyrosine phosphorylated proteins, including CSF-1 receptor (p165), p120, p95 and p55-p60. p120 co-migrated with the product of the protooncogene c-cb1 in anti-p85 alpha immunoprecipitates, and associated with p85 alpha in a rapid and transient manner. Reciprocal experiments confirmed the presence of p85 alpha in anti-Cb1 immunoprecipitates on CSF-1 stimulation of macrophages. PI-3 kinase immunoprecipitates from the myeloid FDC-P1 cell..