Signaling lymphocytic activation molecule family member 1 (SLAMF1)

Signaling lymphocytic activation molecule family member 1 (SLAMF1, also known as CD150) is a type I transmembrane glycoprotein belonging to the immunoglobulin superfamily and is primarily expressed on hematopoietic cells such as T cells, B cells, NK cells, dendritic cells, and macrophages. Structurally, it has an extracellular domain featuring Ig variable-like and constant 2-like motifs, and a cytoplasmic tail containing immunoreceptor tyrosine-based switch motifs (ITSMs) that mediate intracellular signaling via interactions with SH2-domain containing proteins (such as SAP and EAT-2). SLAMF1 functions in cell signaling involved in immune cell activation, differentiation (notably NKT cell development), co-stimulation, and phagocytic regulation. It also participates as a bacterial sensor in macrophages and serves as the cellular entry receptor for the measles virus, highlighting its role in infectious disease susceptibility and host-pathogen interactions. While not widely targeted by drugs, its manipulation offers potential in immunotherapeutic research.

Other names

CD150SLAMIPO-3CRACCSFTA1Ly9 (note: Ly9 is often considered SLAMF3 but may be used in some contexts; most commonly, CD150 is the main alias for SLAMF1)

Modulation of immune cell signaling—through ITSM motifs, interacts with SH2 domain-containing adaptors (SAP, EAT-2), kinases (Fyn), and phosphatases (SHP-1, SHP-2), leading to activating or inhibitory signals depending on cellular and contextual factors