Alternative titles; symbols
HGNC Approved Gene Symbol: SLAMF1
Cytogenetic location: 1q23.3 Genomic coordinates (GRCh38): 1:160,608,106-160,647,044 (from NCBI)
Cocks et al. (1995) described a novel glycoprotein of relative molecular mass 70,000, designated SLAM (signaling lymphocyte activation molecule), that belongs to the immunoglobulin gene superfamily and is involved in T-cell stimulation.
Although the Edmonston strain of measles virus (MV) and the vaccine strains derived from it use CD46 (120920), which is expressed on all nucleated cells, as a cellular receptor, most clinical isolates do not. By analysis of cDNA pools from the MV-susceptible B95a cell line, Tatsuo et al. (2000) identified a cDNA encoding SLAM, also called CDw150, and showed that it is a cellular receptor for both clinical and vaccine MV strains.
Cocks et al. (1995) 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.
Punnonen et al. (1997) found that activated B cells express the membrane-bound form of SLAM and the soluble and cytoplasmic isoforms of SLAM, and that the expression levels of membrane-bound SLAM on B cells are rapidly regulated after activation in vitro. They presented data suggesting that signaling through homophilic SLAM-SLAM binding during B-B and B-T cell interactions enhances the expansion and differentiation of activated B cells.
The expression of SLAM in rheumatoid arthritis (180300) was studied by Isomaki et al. (1997) and in acute multiple sclerosis (126200) by Ferrante et al. (1998).
Tatsuo et al. (2000) found that in MV-resistant cell lines infection with clinical MV and expression of SLAM, but not CD46, caused cytopathic effects (CPE). Likewise, anti-SLAM antibody protected cells from CPE when challenged with MV. Lymphoid cell lines expressing SLAM, but not lymphoid and myelomonocytic cell lines devoid of SLAM, were shown to be susceptible to MV. Tatsuo et al. (2000) noted that 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. They proposed that 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.
Latour et al. (2001) reported that antibody-mediated ligation of SLAM on thymocytes triggered a protein tyrosine phosphorylation signal in T cells in a SAP (300490)-dependent manner. This signal also involved SHIP (601582); the adaptor molecules DOK2 (604997), DOK1 (602919), and SHC (600560); and RASGAP (see 139150). SAP was crucial for this pathway because it selectively recruited and activated the T-cell isoform of FYN (137025).
Using yeast 2-hybrid, immunoblot, and structural analyses, Chan et al. (2003) showed that the SH2 domain of SAP bound to the SH3 domain of FYN in a noncanonical manner and directly coupled FYN to SLAM.
Chan, B., Lanyi, A., Song, H. K., Griesbach, J., Simarro-Grande, M., Poy, F., Howie, D., Sumegi, J., Terhorst, C., Eck, M. J. SAP couples Fyn to SLAM immune receptors. Nature Cell Biol. 5: 155-160, 2003. [PubMed: 12545174] [Full Text: https://doi.org/10.1038/ncb920]
Cocks, B. G., Chang, C.-C. J., Carballido, J. M., Yssel, H., de Vries, J. E., Aversa, G. A novel receptor involved in T-cell activation. Nature 376: 260-263, 1995. [PubMed: 7617038] [Full Text: https://doi.org/10.1038/376260a0]
Ferrante, P., Fusi, M. L., Saresella, M., Caputo, D., Biasin, M., Trabattoni, D., Salvaggio, A., Clerici, E., de Vries, J. E., Aversa, G., Cazzullo, C. L., Clerici, M. Cytokine production and surface marker expression in acute and stable multiple sclerosis: altered IL-12 production and augmented signaling lymphocytic activation molecule (SLAM)-expressing lymphocytes in acute multiple sclerosis. J. Immun. 160: 1514-1521, 1998. [PubMed: 9570575]
Isomaki, P., Aversa, G., Cocks, B. G., Luukkainen, R., Saario, R., Toivanen, P., de Vries, J. E., Punnonen, J. Increased expression of signaling lymphocytic activation molecule in patients with rheumatoid arthritis and its role in the regulation of cytokine production in rheumatoid synovium. J. Immun. 159: 2986-2993, 1997. [PubMed: 9300723]
Latour, S., Gish, G., Helgason, C. D., Humphries, R. K., Pawson, T., Veillette, A. Regulation of SLAM-mediated signal transduction by SAP, the X-linked lymphoproliferative gene product. Nature Immun. 2: 681-690, 2001. [PubMed: 11477403] [Full Text: https://doi.org/10.1038/90615]
Punnonen, J., Cocks, B. G., Carballido, J. M., Bennett, B., Peterson, D., Aversa, G., de Vries, J. E. Soluble and membrane-bound forms of signaling lymphocytic activation molecule (SLAM) induce proliferation and Ig synthesis by activated human B lymphocytes. J. Exp. Med. 185: 993-1004, 1997. [PubMed: 9091591] [Full Text: https://doi.org/10.1084/jem.185.6.993]
Tatsuo, H., Ono, N., Tanaka, K., Yanagi, Y. SLAM (CDw150) is a cellular receptor for measles virus. Nature 406: 893-897, 2000. [PubMed: 10972291] [Full Text: https://doi.org/10.1038/35022579]