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. 2018 Feb 15;10(1):e2018014. doi: 10.4084/MJHID.2018.014

Figure 2. Structure and function of SLAMF receptor in an immune synapse.

Figure 2

The SLAMF receptors are structurally characterized by IgV and IgC2 domains within an extracellular portion and one or more ITSMs, depicted as a closed rectangle, within the cytoplasmic portion. The mostly homophilic interactions between SLAMF receptors result in their costimulatory effects on TCR/CD3 complex signaling pathway. When the SLAMF receptor is engaged by its ligand, cytoplasmic domain ITSMs with tyrosine-based motifs undergo phosphorylation, recruiting adaptors proteins, SAP or EAT-2. SAP can then recruit the Src family protein tyrosine kinase Fyn or Lck, which is important for activation via SLAM family receptors. The coupling of EAT-2 carboxyl-terminal tail to the PLC-γ SH2 domains leads to an additional activation pathway. ITSM-like motif (non-ITSM) depicted as an unfilled rectangle does not bind SAP or EAT-2. SAP is mostly expressed in T cells, while EAT-2 is primarily expressed in antigen-presenting cells.