Regular ArticleDistinct Interactions of the X-Linked Lymphoproliferative Syndrome Gene Product SAP with Cytoplasmic Domains of Members of the CD2 Receptor Family
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Cited by (38)
Phenotypic differences between mice deficient in XIAP and SAP, two factors targeted in X-linked lymphoproliferative syndrome (XLP)
2009, Cellular ImmunologyCitation Excerpt :The discovery that human X-linked lymphoproliferative syndrome can be caused by mutations in the genes encoding either SAP and XIAP led us to determine whether the two proteins might interact. We have previously described a system in which the association of SAP with the cytoplasmic tails of several members of the CD2 family, including SLAM and 2B4, can be readily evaluated [7]. Using this system, the cytoplasmic signaling domain of SLAM fused in-frame with glutathione-S-transferase (SLAM–GST) was expressed with FLAG-epitope-tagged SAP (SAP–FLAG) and XIAP.
The SLAM and SAP Gene Families Control Innate and Adaptive Immune Responses
2008, Advances in ImmunologyCitation Excerpt :Thus, in principle, SAP should have the capacity to out‐compete SH2‐domain proteins that bind to the same phosphotyrosine motif with lesser affinity. Although there is a modicum of support for the concept of SAP as an inhibitor of the recruitment of the protein tyrosine phosphatase (SHP‐2) to the cytoplasmic tail of SLAM, CD244, CD84, and CD229 (Howie et al., 2002a; Lewis, 2001; Sayos et al., 1998), further experiments are required. SH2 domains are typically found in multidomain signaling enzymes or in adapter proteins, where they mediate protein–protein interactions and regulate associated catalytic subunits (Kuriyan and Cowburn, 1997; Machida and Mayer, 2005; Pawson, 2004).
Sequence specificity of SHP-1 and SHP-2 Src homology 2 domains: Critical roles of residues beyond the pY+3 position
2006, Journal of Biological ChemistryNTB-A, a New Activating Receptor in T Cells That Regulates Autoimmune Disease
2004, Journal of Biological ChemistryCitation Excerpt :A hallmark of CD2 family members is the presence of two to four SAP-binding motifs (TXYXX(V/I)) in the intracellular domain; SAP can bind to the both the phosphorylated and non-phosphorylated forms of CD150, although SAP has a higher affinity for the phosphorylated form (31, 32). In addition to binding SAP, CD150 has also been reported to bind SHP-2 (22, 24, 33–35). Both human and mouse NTB-A have two SAP-binding motifs in the intracellular domain.
CD84 expression on human hematopoietic progenitor cells
2003, Experimental HematologySLAM-associated protein deficiency causes imbalanced early signal transduction and blocks downstream activation in T cells from X-linked lymphoproliferative disease patients
2003, Journal of Biological ChemistryCitation Excerpt :Three days later, cells were harvested for scintillation counting after pulsing with 1 μCi of 3H-labeled tritiated thymidine during the last 16 h of culture. SH2D1A Retroviral Vector Generation, Transfections, and Transductions—The SH2D1A cDNA (31) and the MND-IRES-EGFP retroviral vector were generous gifts of Drs. C. S. Duckett (University of Michigan) and D. B. Kohn (Children's Hospital Los Angeles), respectively. The full-length SH2D1A cDNA was blunt-ended and ligated into the SfoI site of MND-IRES-EGFP (M-IE), upstream of the IRES sequence, thus generating MND-SH2D1A-IRES-EGFP (M-SAP-IE), a bicistronic retroviral vector expressing both SH2D1A and EGFP under the control of the myeloproliferative sarcoma virus LTR.
- 1
To whom correspondence may be addressed at the Metabolism Branch, Division of Clinical Sciences, National Cancer Institute, National Institutes of Health, 10 Center Drive, Room 6B-05, Bethesda, MD 20892-1578. E-mail: [email protected].