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c-Cbl Is Tyrosine-Phosphorylated by Interleukin-4 and Enhances
Mitogenic and Survival Signals of Interleukin-4 Receptor by
Linking With the Phosphatidylinositol 3 -Kinase Pathway
Hiroo Ueno,
Ko Sasaki,
Hiroaki Honda,
Tetsuya Nakamoto,
Tetsuya Yamagata,
Kiyoshi Miyagawa,
Kinuko Mitani,
Yoshio Yazaki, and
Hisamaru Hirai
From the Third Department of Internal Medicine, Faculty of Medicine,
University of Tokyo, Tokyo, Japan.
Interleukin-4 (IL-4) is a cytokine that induces both proliferation
and differentiation and suppresses apoptosis of B cells. Although IL-4
has been shown to activate the phosphatidylinositol 3
(PI3)-kinase pathway, the role of PI3 kinase in the IL-4 receptor (IL-4R) signaling remains unclear. In this study, we demonstrated that
c-Cbl proto-oncogene product is inducibly phosphorylated on tyrosine
residues and is associated with the p85 subunit of PI3-kinase by IL-4
stimulation. Overexpression of c-Cbl enhances the PI3-kinase activity
and, at the same time, mitogenic activity and survival of cells in the
presence of IL-4. However, these effects of c-Cbl were abolished by
wortmannin, a specific inhibitor for the PI3 kinase pathway, or by a
point mutation at tyrosine 731 of c-Cbl, which is a major binding site
for p85. These results indicate that c-Cbl plays a role in linking
IL-4R with the PI3 kinase pathway and thus enhancing the mitogenic and
survival signals.
Blood, Vol. 91 No. 1 (January 1), 1998:
pp. 46-53
© 1998 by The American Society of Hematology.
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