Interleukin-5 receptor alpha subunit binds Interleukin-5

Stable Identifier
Reaction [binding]
Homo sapiens
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The Interleukin-5 receptor alpha subunit (IL5Ra) has a single transmembrane domain, a glycosylated extracellular domain and a short (58 amino acids) cytoplasmic tail, containing no tyrosine kinase domain. It binds IL-5 with a relatively low affinity and is not capable of signaling by itself. The alpha subunit has alternatively spliced soluble forms that are capable of binding IL-5 and act as natural antagonists of IL-5 signaling. The cytoplasmic domain of the alpha chain appears to be critical for IL-5 signaling (Takaki et al. 1993). IL5R alpha chain was found to be constitutively associated with JAK2 (Ogata et al. 1998); the same study found that JAK1 was constitutively associated with Bc, though the consensus is that JAK2 is associated with Bc.

Literature References
PubMed ID Title Journal Year
1833065 A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific alpha chain and a beta chain shared with the receptor for GM-CSF

Fiers, W, Devos, R, Van der Heyden, J, Plaetinck, G, Tuypens, T, Tavernier, J, Cornelis, S

Cell 1991
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