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Signaling lymphocytic activation molecule 1 is aprotein that in humans is encoded by theSLAMF1gene.[5][6] Recently SLAMF1 has also been designatedCD150 (cluster of differentiation 150).
Thegene encoding SLAMF1receptor is located on the humanchromosome 1. It consists of eightexons and sevenintrons.Alternative splicing of SLAMF1 transcripts results in severalisoforms of theprotein, including the conventional transmembrane isoform (mCD150), secreted isoform (sCD150) cytoplasmic isoform (cCD150), and the novel transmembrane isoform (nCD150).[7]
SLAMF1 is a type Itransmembrane protein belonging to theimmunoglobulin superfamily.[8] Its molecular weight is between 70 kDa and 95 kDa. The extracellular region of thereceptor is composed of one Ig variable-likedomain and one Ig constant 2-likedomain. The intracellular region of thereceptor contains two intracellular tyrosine-based switch motives (ITSMs) that interact withSH2 domain-containingproteins. However, nCD150 intracellular region differs from otherisoforms of thisprotein, it lacks ITSMs. sCD150 isoform lacks thetransmembrane domain and therefore, it can not be anchored to thecell membrane.[7]
SH2 domain-containingproteins, specificallyadaptor proteinsSAP andEAT-2, andphosphatasesSHP-1,SHP-2 andSHIP, interact with ITSMs in the intracellular region of SLAMF1.[7][10] Binding ofSAP to ITSMs leads to the activation of thekinaseFyn that phosphorylatestyrosines of SLAMF1 and recruits downstreamsignalingproteins. Because of the high affinity ofSAP totyrosine phosphorylated ITSMs, it outcompetes thephosphatases which are the mediators of the inhibitory signal. Therefore, the expression and availability ofSAP play a crucial role in the determination of the type of the signal.[11][12]
The development ofNKT cells is dependent on a signal mediated bySAP. It was found out that the homophilic interaction of SLAMF1 or SLAMF6 is required forSAP recruitment inNKT cells. This interaction mediates a secondary signal crucial forNKT celldifferentiation and expansion in thethymus.[13]
SLAMF1 expression inmacrophages is associated with killing ofGram-negative bacteria. SLAMF1 acts as a bacterial sensor. It is internalized after the recognition ofGram-negative bacteria, and it plays a role in the regulation ofphagosome maturation,ROS andNO production. The absence of SLAMF1 inphagocytes leads, among other things, to the disruption ofcytokine production.[13]
^Schwartz AM, Putlyaeva LV, Covich M, Klepikova AV, Akulich KA, Vorontsov IE, et al. (October 2016). "Early B-cell factor 1 (EBF1) is critical for transcriptional control of SLAMF1 gene in human B cells".Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms.1859 (10):1259–1268.doi:10.1016/j.bbagrm.2016.07.004.PMID27424222.
^Wu N, Veillette A (February 2016). "SLAM family receptors in normal immunity and immune pathologies".Current Opinion in Immunology.38:45–51.doi:10.1016/j.coi.2015.11.003.PMID26682762.
Sayos J, Wu C, Morra M, Wang N, Zhang X, Allen D, et al. (October 1998). "The X-linked lymphoproliferative-disease gene product SAP regulates signals induced through the co-receptor SLAM".Nature.395 (6701):462–469.Bibcode:1998Natur.395..462S.doi:10.1038/26683.PMID9774102.S2CID4324402.
Rogge L, Bianchi E, Biffi M, Bono E, Chang SY, Alexander H, et al. (May 2000). "Transcript imaging of the development of human T helper cells using oligonucleotide arrays".Nature Genetics.25 (1):96–101.doi:10.1038/75671.PMID10802665.S2CID5449948.
Murabayashi N, Kurita-Taniguchi M, Ayata M, Matsumoto M, Ogura H, Seya T (July 2002). "Susceptibility of human dendritic cells (DCs) to measles virus (MV) depends on their activation stages in conjunction with the level of CDw150: role of Toll stimulators in DC maturation and MV amplification".Microbes and Infection.4 (8):785–794.doi:10.1016/S1286-4579(02)01598-8.PMID12270725.
Ferrand V, Li C, Romeo G, Yin L (May 2003). "Absence of SLAM mutations in EBV-associated lymphoproliferative disease patients".Journal of Medical Virology.70 (1):131–136.doi:10.1002/jmv.10373.PMID12629654.S2CID44309832.
