Leukemia inhibitory factor receptor beta (LIFRβ)

Leukemia inhibitory factor receptor beta (LIFRβ, commonly called LIFR or CD118) is a transmembrane protein that functions as a core receptor component for leukemia inhibitory factor (LIF) and several other cytokines, including oncostatin M (OSM), ciliary neurotrophic factor (CNTF), cardiotrophin-1 (CT-1), and cardiotrophin-like cytokine (CLC)[1][4][8]. LIFRβ forms a high-affinity receptor complex with glycoprotein 130 (gp130), and in some contexts with additional coreceptors, to mediate signal transduction. The receptor's extracellular domain has a complex structure with cytokine-binding and immunoglobulin-like domains, facilitating ligand-induced receptor dimerization and activation of downstream signaling pathways such as JAK/STAT, AKT, and ERK1/2[1][6][7]. LIFRβ plays critical physiological roles in cell differentiation, survival, neurodevelopment, embryogenesis, inflammatory responses, and stem cell maintenance. In pathology, it acts both as a metastasis suppressor (notably in breast cancer) and as a contributor to inflammatory and degenerative conditions[5][8]. Loss or dysfunction of LIFRβ can correlate with increased metastatic potential, while aberrant activation can promote tumor progression or resistance to therapy[5][8]. No approved drugs directly target LIFRβ, but the pathway is under investigation as a therapeutic target and as a biomarker for disease progression and patient stratification.

Other names

LIFRCD118Leukemia inhibitory factor receptorLIF receptor beta

Agonists or antagonists of LIFRβ would modulate cytokine-initiated signal transduction, particularly through the JAK/STAT, AKT, ERK1/2, and mTOR pathways[7]. Inhibition or activation can affect cell differentiation, survival, proliferation, or stemness, depending on cellular context[1][5].