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Abstract

Activation of immune system cells via antigen-, Fc-, or natural killer cell-triggering-receptor stimulation is aborted by co-engagement of inhibitory receptors. Negative signaling by killer cell inhibitory receptors and related receptors depends on the Src homology 2 (SH2)-containing protein tyrosine phosphatase SHP-1. Using a combination of direct binding and functional assays, we demonstrated that the SH2 domain-containing leukocyte protein 76 (SLP-76) is a specific target for dephosphorylation by SHP-1 in T cells and natural killer cells. Furthermore, we showed that tyrosine-phosphorylated SLP-76 is required for optimal activation of cytotoxic lymphocytes, suggesting that the targeted dephosphorylation of SLP-76 by SHP-1 is an important mechanism for the negative regulation of immune cell activation by inhibitory receptors.

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PubMed ID:: 9765283

DOI:: 10.1074/jbc.273.42.27518

ScienceOpen disciplines: Chemistry

Keywords: Adaptor Proteins, Signal Transducing,Catalytic Domain,Cytotoxicity Tests, Immunologic,Cytotoxicity, Immunologic,Humans,Intracellular Signaling Peptides and Proteins,Killer Cells, Natural,immunology,Phosphopeptides,metabolism,Phosphoproteins,Protein Tyrosine Phosphatase, Non-Receptor Type 11,Protein Tyrosine Phosphatase, Non-Receptor Type 6,Protein Tyrosine Phosphatases,Receptors, Immunologic,Receptors, KIR,SH2 Domain-Containing Protein Tyrosine Phosphatases,Signal Transduction,Substrate Specificity,T-Lymphocytes, Cytotoxic,Vaccinia virus

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