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.
Aic2b; beta common cytokine receptor; CD antigen CD131; CD131; CDw131; colony stimulating factor 2 receptor, beta, low-affinity (granulocyte-macrophage); colony-stimulating factor-2 receptor, beta, low-affinity; CSF2RB; Csf2rb1; Cytokine receptor common subunit beta; GM-CSF IL-3 IL-5 receptor common beta subunit; GM-CSF/IL-3/IL-5 receptor common beta subunit; GM-CSF/IL-3/IL-5 receptor common beta-chain; IL-3 RB; IL-3 Receptor beta; Il3rb1; interleukin 3 receptor/granulocyte-macrophage colony stimulating factor 3 receptor, beta (high affinity)
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