SLP-76 is a direct substrate of SHP-1 recruited to killer cell inhibitory receptors

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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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Binstadt, B. A., Billadeau, D. D., Jevremović, D., Williams, B. L., Fang, N., Yi, T., … Leibson, P. J. (1998). SLP-76 is a direct substrate of SHP-1 recruited to killer cell inhibitory receptors. Journal of Biological Chemistry, 273(42), 27518–27523. https://doi.org/10.1074/jbc.273.42.27518

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