Interleukin-10 receptor complex (IL-10R complex)

The Interleukin-10 receptor complex is a cell surface, tetrameric protein assembly composed of two IL-10 receptor alpha (IL-10R1) chains and two IL-10 receptor beta (IL-10R2) chains[2][4][7][8]. IL-10R1 is primarily expressed in hematopoietic cells, serving as the ligand-binding subunit, while IL-10R2 is ubiquitously expressed and acts as the signaling subunit, also shared with other cytokines from the IL-10 family[1][2][4][5]. IL-10 binding to its receptor triggers JAK1 and TYK2 kinase activation, leading to phosphorylation and dimerization of STAT3, which translocates to the nucleus and modulates transcription of anti-inflammatory and immunoregulatory genes[4][7][9]. The IL-10 receptor complex is central to limiting excessive immune responses and is critical for mucosal immunity and tissue homeostasis. Genetic deficiencies or dysfunction in either subunit result in very early-onset inflammatory and autoimmune diseases, especially severe forms of IBD and lymphoma[3][4][7]. Modulating the receptor is a focus for therapeutic development in autoimmune disease, chronic inflammation, and cancer. However, its use is limited by complexity of immune regulation and risk of immune suppression, requiring careful biomarker and genetic patient stratification[3][7][9].

Other names

IL-10 receptor complexIL-10R complexIL-10 receptorType II cytokine receptorIL-10R1/IL-10R2 complex

Agonism: Recombinant or pegylated IL-10 binds the receptor complex, activating anti-inflammatory and immunomodulatory signaling. Inhibition (investigational): Potential anti-receptor antibodies or small molecules would block IL-10 binding and downstream signaling, though none are approved.