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JBC, Vol. 270, Issue 19, 11037-11039, May, 1995
T Matsuda, T Fukada, M Takahashi-Tezuka, Y Okuyama, Y Fujitani, Y Hanazono, H Hirai and T Hirano
gp130 is a signal-transducing subunit of receptors for the interleukin- 6
(IL-6)-related cytokine subfamily including IL-6, leukemia inhibitory
factor, oncostatin M, IL-11, and ciliary neurotrophic factor, indicating
that gp130-mediated signals are involved in the immune response,
hematopoiesis, inflammation, and endocrine and nervous system activity. We
previously showed that gp130 stimulation rapidly activates Jak, Btk, and
Tec tyrosine kinases, all of which constitutively associate with gp130. To
further elucidate intracellular signal transduction through gp130, we
examined the possible involvement of another nonreceptor tyrosine kinase,
p92c-fes (Fes). We showed that gp130 stimulation rapidly induced tyrosine
phosphorylation of Fes and actually activated its kinase activity in
hematopoietic lineage cells. Furthermore, Fes associated with gp130
independently of ligand stimulation like Jak, Btk, and Tec tyrosine
kinases. These results indicate that multiple nonreceptor tyrosine kinases
are involved in the gp130-mediated signal transduction pathway. Because
both gp130 and Fes are expressed not only in hematopoietic lineage cells
but also in heart and nerve cells, Fes may play a role in signal
transduction through gp130 in these tissues.
Activation of Fes tyrosine kinase by gp130, an interleukin-6 family cytokine signal transducer, and their association
Division of Molecular Oncology, Osaka University Medical School, Japan.
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