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J Biol Chem, Vol. 274, Issue 30, 21170-21179, July 23, 1999

FYN-T-FYB-SLP-76 Interactions Define a T-cell Receptor zeta /CD3-mediated Tyrosine Phosphorylation Pathway That Up-regulates Interleukin 2 Transcription in T-cells

Monika RaabDagger §, Hyun KangDagger §, Antonio da SilvaDagger , Xiaochun ZhuDagger §, and Christopher E. RuddDagger §

From the Dagger  Division of Tumor Immunology, Department of Cancer Immunology and AIDS, Dana Farber Cancer Institute and Departments of § Medicine and  Pathology, Harvard Medical School, Boston, Massachusetts 02115

Protein-tyrosine kinases p56Lck, SYK, and ZAP-70 and downstream adaptors LAT and SLP-76 have been implicated as essential components in T-cell activation. Another lymphoid-specific adaptor FYB/SLAP has also been identified as a predominant binding partner of SLP-76 and the Src kinase FYN-T, although its role in the activation process has been unclear. In this study, we demonstrate that FYN-T selectively phosphorylates FYB providing a template for the recruitment of FYN-T and SLP-76 SH2 domain binding. This interaction is unusual in its distinct cytoplasmic localization and its long term stable kinetics of phosphorylation. Furthermore, we demonstrate for the first time that the co-expression of all three components of the FYN-T-FYB-SLP-76 matrix can synergistically up-regulate T-cell receptor-driven interleukin 2 transcription activity. These findings document the existence of a T-cell receptor-regulated FYN-T-FYB pathway that interfaces with the adaptor SLP-76 and up-regulates lymphokine production in T-cells.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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