SLAM family member 6; also known as Activating NK receptor; NK-T-B-antigen; NTB-A; SLAMF6; KALI and Ly108; is a single-pass type I membrane protein which belongs to the CD2 subfamily of the immunoglobulin superfamily. SLAMF6 / Ly108 contains one Ig-like (immunoglobulin-like) domain. It is expressed by all (resting and activated) natural killer cells (NK); T- and B-lymphocytes. SLAMF6 / Ly108 triggers cytolytic activity only in natural killer cells (NK) expressing high surface densities of natural cytotoxicity receptors. SLAMF6 / Ly108 is a homodimer. It interacts with PTN6 and; upon phosphorylation; with PTN11 and SH2D1A/SAP. SLAMF6 / Ly108 undergoes tyrosine phosphorylation and associates with the Src homology 2 domain-containing protein (SH2D1A) as well as with SH2 domain-containing phosphatases (SHPs). It may function as a coreceptor in the process of NK cell activation. SLAMF6 / Ly108 can also mediate inhibitory signals in NK cells from X-linked lymphoproliferative patients.
SLAM Family Member 6 (SLAMF6) is a single-pass type I membrane protein that belongs to the SLAM subgroup of the CD2 family. Human SLAMF6/ NTB-A contains a 205 amino acid extracellular domain (ECD) with one Ig-like V-set and one Ig-like C2-set domain; a 21 amino acid transmembrane segment and an 84 amino acid cytoplasmic domain; with two immunoreceptor tyrosine-based switch motifs. SLAMF6 is a homodimer. SLAMF6 can interact with PTN6 and; upon phosphorylation; with PTN11 and SH2D1A/SAP. Phosphorylation-dependent NTB-A association with SAP is required for full production of IFN-γ by NK cells and independent of EAT-2 binding. It Triggers cytolytic activity only in natural killer cells (NK) expressing high surface densities of natural cytotoxicity receptors. On B cells; NTB-A modulates immunoglobulin class switching and the balance between tolerance and autoimmunity.
SLAM Family Member 6 (SLAMF6) is a 60 kD single-pass type I membrane protein that belongs to the SLAM subgroup of the CD2 family. Human SLAMF6/ NTB-A contains a 205 amino acid extracellular domain (ECD) with one Ig-like V-set and one Ig-like C2-set domain; a 21 amino acid transmembrane segment and an 84 amino acid cytoplasmic domain; with two immunoreceptor tyrosine-based switch motifs. SLAMF6 is a homodimer. SLAMF6 can interact with PTN6 and; upon phosphorylation; with PTN11 and SH2D1A/SAP. Phosphorylation-dependent NTB-A association with SAP is required for full production of IFN-γ by NK cells and independent of EAT-2 binding. It Triggers cytolytic activity only in natural killer cells (NK) expressing high surface densities of natural cytotoxicity receptors. On B cells; NTB-A modulates immunoglobulin class switching and the balance between tolerance and autoimmunity.
SLAM family member 7 (SLAMF7), also known as CRACC, CD319, CD2-like receptor-activating cytotoxic cells, and CS1, is a single-pass type I membrane protein and a member of the CD2 family of cell surface receptors. SLAMF7 is expressed in NK cells, activated B-cells, NK-cell line but not in promyelocytic, B-cell lines, or T-cell lines. Although the cytoplasmic domain of CS1 contains immunoreceptor tyrosine-based switch motifs (ITSM), which enables to recruite signaling lymphocyte activation molecule (SLAM)-associated protein (SAP/SH2D1A), it activates NK cells in the absence of a functional SAP. CS1 is a self ligand and homophilic interaction of CS1 regulates NK cell cytolytic activity. CRACC positively regulated natural killer cell functions by a mechanism dependent on the adaptor EAT-2 but not the related adaptor SAP. However, in the absence of EAT-2, CRACC potently inhibited natural killer cell function. It was also inhibitory in T cells, which are typically devoid of EAT-2. Thus, CRACC can exert activating or inhibitory influences on cells of the immune system depending on cellular context and the availability of effector proteins.
SLAMF7 is a single-pass type I membrane protein and contains 1 Ig-like C2-type (immunoglobulin-like) domain. SLAMF7 is expressed in NK cells, activated B-cells, NK-cell line but not in promyelocytic, B-cell lines, or T-cell lines. Although the cytoplasmic domain of CS1 contains immunoreceptor tyrosine-based switch motifs (ITSM), which enables to recruite signaling lymphocyte activation molecule (SLAM)-associated protein (SAP/SH2D1A), it activates NK cells in the absence of a functional SAP. SLAMF7 positively regulated natural killer cell functions by a mechanism dependent on the adaptor EAT-2 but not the related adaptor SAP. However, in the absence of EAT-2, CRACC potently inhibited natural killer cell function. It was also inhibitory in T cells, which are typically devoid of EAT-2. Thus, SLAMF7 can exert activating or inhibitory influences on cells of the immune system depending on cellular context and the availability of effector proteins.
SLAM family member 8 (SLAMF8) is a single-pass type I membrane protein and contains 1 Ig-like C2-type domain. SLAMF8 is a member of the CD2 family of cell surface proteins involved in lymphocyte activation. These proteins are characterized by Ig domains and studies of a similar protein in mouse suggest that it may function during B cell lineage commitment. SLAMF8 is expressed in lymph node, spleen, thymus and bone marrow. It may play a role in B-lineage commitment and/or modulation of signaling through the B-cell receptor.
SLAM-induced signal-transduction events in T-lymphocytes are different from those in B-cells. Two modes of SLAM signaling are likely to exist: one in which the inhibitor SH2D1A acts as a negative regulator and another in which protein-tyrosine phosphatase 2C (PTPN11)-dependent signal transduction operates.
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