Interleukin-10 receptor 1 (IL-10R1)

Interleukin-10 receptor 1 is a cell surface receptor that serves as the primary binding site for the anti-inflammatory cytokine interleukin-10 (IL-10)[1][3][4]. Structurally, it is a transmembrane glycoprotein composed of extracellular, transmembrane, and intracellular domains, and belongs to the class II cytokine receptor family[1][3]. Signal transduction occurs upon assembly of a heterodimeric receptor complex including IL-10R1 and the accessory protein IL-10R2 (IL-10RB); binding of IL-10 to IL-10R1 initiates intracellular signaling cascades—primarily JAK1/TYK2 kinases which phosphorylate STAT3—leading to suppression of inflammatory responses and promotion of regulatory and anti-apoptotic pathways[1][3][4]. The receptor is widely expressed on hematopoietic and immune cells, and its activity is essential for limiting the extent and duration of immune and inflammatory

Other names

IL-10RAIL10R1CD210Interleukin-10 receptor subunit alpha

Activation of Janus kinase 1 (JAK1) and Tyrosine kinase 2 (TYK2) following ligand binding leads to phosphorylation of STAT transcription factors, predominantly STAT3, driving anti-inflammatory gene expression and inhibition of pro-inflammatory cytokine signaling[1][3].