The human IL-3, IL-5 and GM-CSF receptors are each composed of both unique a subunits and a common beta subunit. The a subunits are low affinity ligand binding proteins while the beta subunits do not themselves bind ligand, but are required for high affinity binding by the a subunits. In contrast, the mouse IL-3 receptor has two distinct beta subunits, one that functions only in IL-3 mediated cell signaling and a second that is shared with IL-5 and GM-CSF. The murine beta-subunits are 91% homologous at the amino acid level but only 56% homologous to the human beta subunit. Although neither the murine nor the human beta subunit contains tyrosine kinase domains, both activate tyrosine phosphorylation mediated signaling pathways.
CD116; CD116 antigen; CDw116; colony stimulating factor 2 receptor, alpha, low-affinity (granulocyte-macrophage); CSF2R; CSF2RAX; CSF2RAY; CSF2RX; CSF2RY; GM-CSF receptor alpha subunit; GM-CSF-R-alpha; GMCSFR; GMCSFR-alpha; GMR; GMR-alpha; granulocyte-macrophage colony-stimulating factor receptor alpha chain; Granulocyte-macrophage colony-stimulating factor receptor subunit alpha; MGC3848; MGC4838
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