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Abstract
Monocyte colony-stimulating factor (M-CSF) is required for the proliferation of mononuclear phagocytes. The activated M-CSF receptor associates with phosphatidylinositol 3-kinase (PI 3-kinase). In the present studies, we demonstrate that M-CSF also induces direct interaction of PI 3-kinase (p85 alpha subunit) with the SH2/SH3 adaptor protein Grb2. Tyrosine-phosphorylated PI 3-kinase interacts with the SH2 domain of Grb2. A pYRNE (pY408) site in PI 3-kinase is potentially involved in this interaction. The results also demonstrate that the PI 3-kinase.Grb2 complex associates with the guanine nucleotide exchange protein Sos. Since Sos binds to the SH3 domains of Grb2 and thereby associates with Ras at the cell membrane, formation of the PI 3-kinase.Grb2.Sos complex provides a potential mechanism for growth factor-induced interactions of PI 3-kinase and Ras.
Highlights
Monocyte colony-stimulating factor (M-CSF) is required for the proliferation of mononuclear phagocytes
We demonstrate that M-CSF induces direct interaction of PI 3-kinase (p85a subunit) with the SH2/SH3 adaptor protein Grb2
Studies have demonstrated that Tyr721 serves as a binding site for PI 3-kinase [4], whereas the adaptor protein Grb2 associates with phosphotyrosine 697 [5]
Summary
Monocyte colony-stimulating factor (M-CSF) is required for the proliferation of mononuclear phagocytes. We demonstrate that M-CSF induces direct interaction of PI 3-kinase (p85a subunit) with the SH2/SH3 adaptor protein Grb2. The results demonstrate that the PI 3-kinase·Grb2 complex associates with the guanine nucleotide exchange protein Sos. Since Sos binds to the SH3 domains ofGrb2 and thereby associates with Has at the cell membrane, formation of the PI 3-kinase·Grb2·Sos complex provides a potential mechanism for growth factor-induced interactions of PI 3-kinase and Ras. The M-CSF1 receptor is a transmembrane protein tyrosine kinase encoded by the c-fms gene [1, 2].
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