Interleukin 5 (IL-5) is a soluble T cell-derived factor, also known as T cell replacing factor (TRF), that induces B cell and eosinophil growth and differentiation. IL-5 exerts its biological activity through the IL-5 receptor (IL-5R), which is composed of two chains: an alpha chain that binds IL-5 with low affinity and a beta chain that does not bind IL-5, but together with the IL-5 alpha chain, constitutes the high affinity IL-5 receptor. The cytoplasmic domain of both the alpha and beta chains is essential for signal transduction. Specifically, the membrane-proximal proline-rich sequence of the cytoplasmic domain of the IL-5R receptor alpha subunit, IL-5Ralpha, is critical for the IL-5 induced proliferative response, expression of nuclear proto-oncogenes and tyrosine phosphorylation of cellular proteins, such as JAK1 and JAK2.View more
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