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Fc-gamma receptor II (FcγRII, CD32) is a family of low-affinity cell surface receptors for the Fc region of immunoglobulin G (IgG), consisting primarily of three isoforms: FcγRIIa, FcγRIIb, and FcγRIIc, encoded by the FCGR2A, FCGR2B, and FCGR2C genes, respectively. They are widely expressed on immune cells such as B cells, dendritic cells, neutrophils, monocytes, platelets, and natural killer cells. FcγRII receptors have two Ig-like extracellular domains and cytoplasmic tails containing either an immunoreceptor tyrosine-based activation motif (ITAM, in FcγRIIa/c) or an immunoreceptor tyrosine inhibitory motif (ITIM, in FcγRIIb). This structure allows FcγRII to play both activating and inhibitory roles in immune cell signaling. Their primary functions are clearance of IgG-coated pathogens (phagocytosis), regulation of antibody-mediated effector activity, and modulation of inflammation. Genetically determined polymorphisms are relevant to individual variation in disease susceptibility and response to antibody-based therapies.
Engagement by the Fc portion of IgG in immune complexes can trigger intracellular signaling via ITAM (activating, FcγRIIa/c) or ITIM (inhibitory, FcγRIIb) motifs. Activates or suppresses effector functions such as phagocytosis, cytokine release, or inhibition of cell activation based on subtype. Modifies the efficacy and safety profile of IgG1/IgG3 therapeutic antibodies by modulating effector cell recruitment and function.
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