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J Biol Chem, Vol. 273, Issue 7, 3994-4000, February 13, 1998
From the Divisions of Cell Biology and Cellular Immunology, La
Jolla Institute for Allergy and Immunology,
San Diego, California 92121
In cells expressing the oncogenic Bcr-Abl
tyrosine kinase, the regulatory p85 subunit of phosphatidylinositol
3-kinase is phosphorylated on tyrosine residues. We report that this
phosphorylation event is readily catalyzed by the Abl and Lck
protein-tyrosine kinases in vitro, by Bcr-Abl or a
catalytically activated Lck-Y505F in co-transfected COS cells, and by
endogenous kinases in transfected Jurkat T cells upon triggering of
their T cell antigen receptor. Using these systems, we have mapped a
major phosphorylation site to Tyr-688 in the C-terminal SH2 domain of
p85. Tyrosine phosphorylation of p85 in vitro or in
vivo was not associated with detectable change in the enzymatic
activity of the phosphatidylinositol 3-kinase heterodimer, but
correlated with a strong reduction in the binding of some, but not all,
phosphoproteins to the SH2 domains of p85. This provides an additional
candidate to the list of SH2 domains regulated by tyrosine
phosphorylation and may explain why association of phosphatidylinositol
3-kinase with some cellular ligands is transient or of lower
stoichiometry than anticipated.
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