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J Biol Chem, Vol. 274, Issue 9, 5333-5338, February 26, 1999
From the Centre de Recherche en Rhumatologie et Immunologie, Centre
de Recherche du CHUL, and the Department of Medicine, Faculty of
Medicine, Laval University, Sainte Foy,
Québec G1V 4G2, Canada
Granulocyte-macrophage colony-stimulating factor
(GM-CSF) regulates many of the biological activities of human
neutrophils. The signaling pathways via which these effects are
mediated are not fully understood. We have shown previously that GM-CSF
treatment of human neutrophils activates the Janus kinase/signal
transducers and activators of transcription (Jak/STAT) pathway and,
more specifically, Jak2, STAT3, and STAT5B in neutrophils. GM-CSF also
stimulates the activity of the phosphatidylinositol 3-kinase
(PI3-kinase) in a tyrosine kinase-dependent manner. Here we
report that pretreating the cells with a Jak2 inhibitor (AG-490)
abolishes tyrosine phosphorylation of the p85 subunit of PI3-kinase
induced by GM-CSF. Furthermore, p85 was found to associate with Jak2,
but not with Lyn, in stimulated cells in situ and with its
autophosphorylated form in vitro; however, Jak2 did not
bind to either of the two Src homology 2 (SH2) domains of the p85
subunit of PI3-kinase. Although STAT5B bound to the carboxyl-terminal
SH2 domain of p85, it was absent from the complex containing PI3-kinase
and Jak2. These results suggest that stimulation of the activity of
PI3-kinase induced by GM-CSF is mediated by Jak2 and that the
association between Jak2 and p85 depends on an adaptor protein yet to
be identified.
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