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IL20RA is an alpha-chain with a long intracellular domain. IL20RA, along with the IL-20 receptor, beta subunit, form the heterodimeric interleukin-20 receptor, which binds the cytokines IL-19, IL-20 and IL-24. IL20RA also forms a complex with the IL-10 receptor, beta subunit, which binds the cytokine IL-26.[5]
Receptors made up of IL20RA signal through a JAK-STAT signaling pathway.[5] In this pathway, after a cytokine binds IL20RA and the beta subunit, JAKs linked to intracellulardomains of IL20R activate and phosphorylate tyrosine residues found in the longer alpha chains of IL20RA. STAT then binds to docking sites created by JAK phosphorylation and becomes phosphorylated by JAK. STATs then dimerize and move to the nucleus to act as transcription factors. The specific genes expressed are dependent on the specific JAK, STAT, as well as by SOCS proteins, which can inhibit the JAK-STAT signal, regulating it.where the transcription factor STAT3 binds to IL20RA and STAT3 becomes activated.[1] IL20RA has multiple docking sites for STAT3.[5][9]
Research indicates that IL20RA is found in some immune cells. For example, IL20RA is sometimes found in lung macrophages. Research indicates that IL20RA presence may be related to disease. In people with rheumatoid arthiritis, IL20RA is present in blood monocytes.[8]
IL20RA has also been linked with psoriasis, and atherosclerosis, all diseases associated with inflammation. The specific role of IL20RA in these diseases is unknown.[7]
Pletnev S, Magracheva E, Kozlov S, et al. (2003). "Characterization of the recombinant extracellular domains of human interleukin-20 receptors and their complexes with interleukin-19 and interleukin-20". Biochemistry. 42 (43): 12617–12624. doi:10.1021/bi0354583. PMID14580208.