CD131

CD131, the common beta chain (βc or CSF2RB), is the shared signal-transducing subunit of the GM-CSF, IL-3 and IL-5 receptor complexes. This 130 kDa type I transmembrane glycoprotein binds its cytokine-occupied α chains (GM-CSFRα/CD116, IL-3Rα/CD123, IL-5Rα/CD125) to form high-affinity receptors, and its large cytoplasmic domain-associated with JAK2-carries multiple tyrosine residues that, once phosphorylated, dock STAT5, SHC-Grb2 and PI3K effectors to propagate proliferation and survival signals. CD131 is expressed broadly on myeloid cells, hematopoietic progenitors, eosinophils and basophils, explaining why βc cytokines collectively govern granulocyte, macrophage and eosinophil production and activation. Somatic CSF2RB mutations occur in acute myeloid leukemia and promote growth factor independence; conversely, a naturally occurring soluble βc variant acts as a cytokine antagonist. Because βc is indispensable for eosinophil responsiveness to IL-5, targeting CD131 has been explored for eosinophilic disorders.