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Title: The colony-stimulating factor 1 receptor: pleiotropy of signal-response coupling. Author: Sherr CJ. Journal: Lymphokine Res; 1990; 9(4):543-8. PubMed ID: 2090881. Abstract: The colony-stimulating factor 1 receptor (CSF-1R) is a cell surface glycoprotein consisting of an extracellular ligand-binding domain, a single membrane-spanning segment, and an intracellular tyrosine kinase domain. Binding of CSF-1 activates the receptor kinase, leading to "autophosphorylation" of receptor subunits and the concomitant phosphorylation of a series of cellular proteins on tyrosine residues. The diverse effects of CSF-1 on mononuclear phagocyte proliferation, differentiation, survival, and macrophage effector function appear to reflect the ability of CSF-1R to simultaneously modulate the activities of a series of intracellular proteins that function in relaying biochemical signals. Sequences surrounding sites of ligand-induced tyrosine phosphorylation within CSF-1R may serve as targets for interactions with cellular effector proteins whose activities are modified by receptor binding, tyrosine phosphorylation, or both. The specificity of the cellular response to CSF-1 may depend, at least in part, on the differential coupling of the receptor to these "downstream" effectors in different cell types.[Abstract] [Full Text] [Related] [New Search]