Signaling lymphocytic activation molecule F7 (SLAMF7)

Signaling lymphocytic activation molecule F7 (SLAMF7) is a type I transmembrane receptor belonging to the immunoglobulin superfamily. It contains an extracellular domain with two immunoglobulin-like domains (C2 and V) and a cytoplasmic region with immune receptor tyrosine-based switch motifs (ITSMs), which mediate intracellular signaling via interactions with adaptor proteins such as EAT-2 and SAP[1]. SLAMF7 is expressed on natural killer (NK) cells, some T cells, macrophages, and especially plasma cells, both normal and malignant[1][3][5][7][8]. Engagement of SLAMF7 initiates signaling pathways that activate NK cells and enhance their cytotoxicity, facilitate cytokine secretion (such as IFN-γ), and regulate antibody-dependent cellular cytotoxicity (ADCC). This property makes SLAMF7 a central target for cancer immunotherapy—in particular, the approved drug Elotuzumab targets SLAMF7 in multiple myeloma to boost immune-mediated elimination of tumor cells[4][5]. SLAMF7 also contributes to the coordination of immune responses within the tumor microenvironment and is implicated in the regulation of macrophage phagocytosis and monocyte function, with roles in inflammation and infection[1][9]. It is considered a robust biomarker for malignant plasma cells, facilitating disease diagnosis and therapeutic monitoring[5]. Therapeutic challenges involve managing immune-related adverse effects and avoiding off-target immunosuppression due to SLAMF7's presence on normal immune cells[3][4].

Other names

CD319CRACCCS1Membrane protein FOAP-9CD2 subset 1

Antibody-dependent cellular cytotoxicity (ADCC) enhancement (Elotuzumab and similar antibodies bind SLAMF7 on plasma cells and NK cells to stimulate immune attack against target cells)\nDirect activation of NK cells and cytotoxic pathways\nImmune modulation (shaping tumor microenvironment and overcoming immune evasion)