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J Biol Chem, Vol. 274, Issue 39, 27583-27589, September 24, 1999
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From the Ligation of the T cell antigen receptor (TCR)
activates the Src family tyrosine kinase p56 Lck, which, in turn,
phosphorylates a variety of intracellular substrates. The
phosphatidylinositol 3-kinase (PI3K) and the tyrosine phosphatase SHP-1
are two Lck substrates that have been implicated in TCR signaling. In
this study, we demonstrate that SHP-1 co-immunoprecipitates with the p85 regulatory subunit of PI3K in Jurkat T cells, and that this association is increased by ligation of the TCR complex. Co-expression of SHP-1 and PI3K with a constitutively activated form of Lck in COS7
cells demonstrated the carboxyl-terminal SH2 domain of PI3K to
inducibly associate with the full-length SHP-1 protein. By contrast, a
truncated SHP-1 mutant lacking the Lck phosphorylation site
(Tyr564) failed to bind p85. Wild-type but not
catalytically inactive SHP-1 induced dephosphorylation of p85.
Furthermore, expression of SHP-1 decreased PI3K enzyme activity in
anti-phosphotyrosine immunoprecipitates and phosphorylation of serine
473 in Akt, a process dependent on PI3K activity. These results
indicate the presence of a functional interaction between PI3K and
SHP-1 and suggest that PI3K signaling, which has been implicated in
cell proliferation, apoptosis, cytoskeletal reorganization, and many other biological activities, can be regulated by SHP-1 in T lymphocytes.
Division of Medicine, and the Cell Growth
Regulation Laboratory, University of Texas M. D. Anderson Cancer
Center, Houston, Texas 77030 and the § Departments of
Medicine, Immunology, and Molecular and Medical Genetics, University of
Toronto, Toronto M5G 1X5, Ontario, Canada
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