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The interleukin-2 receptor (IL-2R) signaling complex is a heterotrimeric protein complex found on the surface of certain immune cells, primarily lymphocytes. It mediates cellular responses to the cytokine interleukin-2 (IL-2), which is a central regulator of immune system function and acts as a growth factor for T cells. The high-affinity IL-2 receptor consists of three noncovalently linked subunits: alpha chain (IL-2Ralpha, CD25, p55), beta chain (IL-2Rbeta, CD122, p75), and gamma chain (gamma c, IL-2Rgamma, CD132). Only complexes containing both beta and gamma chains are capable of initiating intracellular signaling, involving activation of cytosolic kinases such as JAKs leading to downstream pathways including Ras/MAPK/ERK cascade and mTORC1 activation.
Modulation of IL-2 signaling
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