Interleukin-13 receptor subunit alpha-2 (IL-13Rα2), also known as CD213A2 (cluster of differentiation 213A2), is a membrane bound protein that in humans is encoded by the IL13RA2 gene.
Function
IL-13Rα2 is closely related to IL-13Rα1, a subunit of the interleukin-13 receptor complex. This protein binds IL13 with high affinity, but lacks any significant cytoplasmic domain, and does not appear to function as a signal mediator. It is, however, able to regulate the effects of both IL-13 and IL-4, despite the fact it is unable to bind directly to the latter. It is also reported to play a role in the internalization of IL13.
IL-13Rα2 was initially considered a “decoy receptor” because its short intracellular domain and lack of a conventional JAK/STAT signaling motif suggested that it primarily functioned by binding and sequestering IL-13 without initiating downstream signaling. However, subsequent studies have demonstrated that IL-13Rα2 can activate distinct signaling pathways, including AP-1 and TGF-β production. These findings have established a more active role for IL-13Rα2 in cancer biology, where it has been implicated in tumor proliferation, invasion, and metastasis..
Clinical significance
IL-13Rα2 has been found to be over-expressed in a variety of cancers, including pancreatic, ovarian, melanomas, and malignant gliomas.
See also Interleukin-13 receptor
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