interleukin-11 binding

Definition

Target type: molecularfunction

Binding to interleukin-11. [GOC:jl]

Interleukin-11 (IL-11) binding is a crucial step in the initiation of IL-11 signaling, a multifaceted pathway involved in a wide range of biological processes. IL-11, a pleiotropic cytokine, exerts its effects through binding to its cognate receptor, IL-11RA. This interaction triggers a cascade of events that ultimately lead to the activation of downstream signaling pathways, primarily the JAK-STAT pathway. The binding of IL-11 to IL-11RA initiates receptor dimerization, bringing together two IL-11RA molecules. This dimerization event then recruits the Janus kinase (JAK) family members, JAK1 and JAK2, which are associated with the cytoplasmic tails of IL-11RA. Upon receptor dimerization, JAK1 and JAK2 become activated through transphosphorylation, a process where each kinase phosphorylates the other. Activated JAKs then phosphorylate tyrosine residues on the cytoplasmic tail of IL-11RA, creating docking sites for signal transducer and activator of transcription (STAT) proteins, particularly STAT3. STAT3 binds to the phosphorylated IL-11RA and is subsequently phosphorylated by JAKs. Once phosphorylated, STAT3 dimerizes and translocates to the nucleus, where it binds to specific DNA sequences known as STAT3-binding elements. This binding event triggers the transcription of target genes that are involved in diverse cellular processes such as proliferation, differentiation, survival, and inflammation. The molecular function of IL-11 binding, therefore, involves a complex interplay of receptor dimerization, JAK activation, STAT3 phosphorylation, nuclear translocation, and gene transcription, ultimately mediating the pleiotropic effects of IL-11.'
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Proteins (1)

Compounds (2)