CD150

CD150, officially designated SLAMF1, is a cell-surface receptor of the signaling lymphocytic activation molecule (SLAM) family. It is expressed on activated T cells, B cells, natural killer cells, dendritic cells, monocytes/macrophages, and some hematopoietic progenitors. CD150 belongs to the immunoglobulin superfamily and features two extracellular Ig-like domains; its cytoplasmic tail contains ITSM motifs that recruit SH2-domain–containing adaptor proteins such as SAP (SH2D1A) and EAT-2 to transduce signals.

CD150 engages in both homophilic and heterophilic interactions, notably binding to CD48 (SLAMF2) in trans. These interactions support cell adhesion and co-stimulatory signaling that influence immune cell activation. Through ITSM motifs and associated adaptors, CD150 modulates T cell activation and differentiation, B cell responses in germinal centers, and NK cell cytotoxicity, thereby shaping cytokine production and antibody responses.

In infection, CD150 serves as a major entry receptor for measles virus on activated immune cells and dendritic cells, contributing to the virus’s tropism for lymphoid tissues. Clinically, signaling through SLAMF1 is interconnected with the SLAM-associated protein (SAP) family adaptors, and defects in this pathway underlie X-linked lymphoproliferative disease type 1 and related immune dysregulation, illustrating the receptor’s role in maintaining immune homeostasis.

CD150 remains an area of active research for understanding immune signaling networks and as a potential target for therapies aiming to modulate adaptive and innate immune responses.