IL-6 receptor pathway

Interleukin 6 (IL-6), otherwise known as B-cell stimulatory factor (BSF), was first identified as a cytokine that stimulates B-cell differentiation into immunoglobulin-producing cells. This pathway displays how the IL-6 receptor interacts with IL-6 and gp130 in order to induce transcription through the JAK/STAT and ERK pathways.

​​​​​Since its discovery, IL-6 has been shown to be involved in a number of autoimmune diseases including diabetes, atherosclerosis and rheumatoid arthritis.The classical signaling pathway of IL-6 involves its binding to the membrane-bound IL-6 receptor. This induces gp130 dimerization, which activates the Janus kinases (JAK). JAKs then phosphorylate tyrosine residues on the intracellular domain of gp130, leading to the recruitment of SHP2 and subsequent activation of the ERK pathway. Alternatively, phosphorylated gp130 can directly recruit STAT3, which - after phosphorylation by JAKs - can homodimerize and translocate to the nucleus where it induces transcription of its target genes.

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