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J Biol Chem, Vol. 274, Issue 30, 21170-21179, July 23, 1999
From the 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.
FYN-T-FYB-SLP-76 Interactions Define a T-cell Receptor
/CD3-mediated Tyrosine Phosphorylation Pathway That Up-regulates
Interleukin 2 Transcription in T-cells
§,§,¶,§, and§¶
Division of Tumor Immunology,
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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