Interleukin-6 receptor complex (IL-6R complex)

The interleukin-6 receptor complex is a transmembrane and soluble protein complex consisting of two primary components: the IL-6 receptor alpha subunit (IL-6Rα, also known as CD126) and the signal-transducing beta subunit glycoprotein 130 (gp130, also called IL6ST). The complex forms a hexamer consisting of two IL-6 molecules, two IL-6Rα units, and two gp130 units, enabling high-affinity binding and signal transduction. IL-6Rα exists in both membrane-bound and soluble forms, facilitating two major modes of signaling: classic (via membrane-bound IL-6R, limited to select cell types like hepatocytes, neutrophils, and some lymphocytes) and trans-signaling (via soluble IL-6R in complex with IL-6, activating cells expressing only gp130)[1][2][4][5][6][7][8]. Activation of the IL-6 receptor complex triggers intracellular signaling via the JAK-STAT and MAPK pathways, governing immune response, inflammation, and hematopoiesis. This receptor complex plays a key role in pathophysiology of numerous diseases, and its blockade has become a clinically validated therapeutic strategy for inflammatory and autoimmune conditions[2][4][5][6][7].

Other names

Interleukin-6 receptorIL-6 receptor complexIL6 receptor complexIL-6RIL-6Rα/gp130 complexCD126/gp130 complex

Inhibition of IL-6 binding (monoclonal antibodies block the IL-6R, preventing IL-6 from initiating downstream signaling) - Inhibition of receptor signaling (antagonists disrupt the formation of the IL-6/IL-6R/gp130 complex) - Downregulation of the JAK/STAT3 pathway