Description
Interleukin 5 Receptor alpha (IL-5 Ralpha), also known as CD125, is a hematopoietin receptor that plays a dominant role in eosinophil biology. Mature mouse IL-5 Ralpha consists of a 322 amino acid (aa) extracellular domain (ECD) with a WSxWS motif and a four cysteine motif, a 22 aa transmembrane segment, and a 54 aa cytoplasmic domain. The high affinity receptor for IL-5 is a complex that consists of the ligand binding IL-5 Ralpha and the transmembrane common beta chain (betac/CD131) which is shared with the receptor complexes for IL-3 and GM-CSF. IL-5 Ralpha binds IL-5 at low affinity and then associates with preformed betac oligomers to form the signaling-competent receptor complex. IL-5 stimulation of CD34+ hematopoietic progenitor cells induces the up-regulation of transmembrane IL-5 Ralpha followed by eosinophilic differentiation and activation. IL-5 Ralpha also promotes the differentiation of basophils and B cells. Exposure of mature eosinophils to IL-5 attenuates their IL-5 responsiveness by inducing the down-regulation of surface IL-5 Ralpha and increased production of soluble IL-5 Ralpha