protein_function: High-affinity self-ligand important in bidirectional T-cell to B-cell stimulation. SLAM-induced signal-transductionevents in T-lymphocytes are different from those in B-cells. Twomodes of SLAM signaling are likely to exist: one in which theinhibitor SH2D1A acts as a negative regulator and another in whichprotein-tyrosine phosphatase 2C (PTPN11)-dependent signaltransduction operates.
Signaling lymphocytic activation molecule is a protein that in humans is encoded by the SLAMF1 gene. It belongs to the immunoglobulin gene superfamily. This gene is mapped to 1q23.3. It has found that SLAM is constitutively expressed on peripheral blood memory T cells, T-cell clones, immature thymocytes and a proportion of B cells, and is rapidly induced on naive T cells after activation. In MV-resistant cell lines, infection with clinical MV and expression of SLAM, but not CD46, caused cytopathic effects (CPE). The expression of SLAM on activated B and T lymphocytes correlates with the pathology of MV infection in humans and monkeys, in which lymphoid organs are the chief sites of MV replication and the binding of MV to SLAM may impair the signaling functions of SLAM in lymphocyte activation and inhibit Th0,Th1 cytokine production, thereby promoting Th2 cytokine production. It has reported that antibody-mediated ligation of SLAM on thymocytes triggered a protein tyrosine phosphorylation signal in T cells in a SAP-dependent manner. This signal also involved SHIP, the adaptor molecules DOK2, DOK1, and SHC and RASGAP.
