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The Journal of Immunology, 1999, 163: 5753-5757.
Copyright © 1999 by The American Association of Immunologists

CUTTING EDGE

Cutting Edge: SLP-76 Cooperativity with FYB/FYN-T in the Up-Regulation of TCR-Driven IL-2 Transcription Requires SLP-76 Binding to FYB at Tyr595 and Tyr651

Liping Geng*,{dagger}, Monika Raab*,{ddagger} and Christopher E. Rudd1,*,{dagger},{ddagger}

* Division of Tumor Immunology, Department of Cancer Immunology and AIDS, {dagger} Dana Farber Cancer Institute and Departments of Medicine and {ddagger} Pathology, Harvard Medical School, Boston, MA 02115

SLP-76 (Src homology (SH) 2-domain-containing leukocyte protein of 76 kDa) and FYB/SLAP (FYN-T-binding protein/SLP-76-associated protein) are two hemopoietic cell-specific adaptor proteins downstream of TCR-activated protein tyrosine kinases. SLP-76 has been implicated as an essential component in T cell signaling. FYB is selectively phosphorylated by FYN-T, providing a template for the recruitment of FYN-T and SLP-76 SH2 domains. Coexpression of FYN-T, FYB, and SLP-76 can synergistically up-regulate IL-2 production in T cells upon TCR ligation. In this report, we show that two tyrosines, Tyr595 and Tyr651, of FYB are major sites of phosphorylation by FYN-T and mediate binding to SLP-76 in Jurkat T cells. Furthermore, the synergistic up-regulation of IL-2 promoter activity in the FYN-T-FYB-SLP-76 pathway is contingent upon the interaction between FYB and SLP-76, but not the interaction between FYB and FYN-T. These observations define a pathway by which SLP-76 interacts with downstream components in the up-regulation of T cell cytokine production.




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