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J. Biol. Chem., Vol. 269, Issue 15, 11648-11655, 04, 1994
TG Boulton, N Stahl and GD Yancopoulos
Ciliary neurotrophic factor (CNTF), leukemia inhibitory factor (LIF),
oncostatin M (OSM), and interleukin-6 (IL6) compose a family of distantly
related cytokines that initiate signaling by inducing either
homodimerization of the "beta" signal transducing receptor component gp130
(in the case of IL6) or heterodimerization between gp130 and the
gp130-related LIFR beta (in the case of CNTF, LIF, and OSM); dimerization
of beta receptor components in turn activates members of the Jak/Tyk family
of receptor-associated tyrosine kinases. Here we report that CNTF, LIF,
OSM, and IL6 induce most of the same protein tyrosine phosphorylations,
regardless of the cell type assayed or whether they initiate signaling by
inducing homo- or heterodimerization of beta components. Although several
of the protein tyrosine phosphorylations induced by the CNTF/LIF/OSM/IL6
family of factors may correspond to novel tyrosine kinase targets, we have
been able to demonstrate the involvement of known signaling molecules, such
as phospholipase C gamma, phosphoinositol 3-kinase, phosphotyrosine
phosphatase (PTP1D), pp120, SHC, GRB2, STAT91, Raf-1, and the mitogen-
activated protein kinases ERK1 and ERK2, revealing substantial convergence
not only between the pathways activated by this cytokine family and other
cytokines, but with pathways previously known to be activated only by
factors that utilize receptor tyrosine kinases. Our data suggest the beta
receptor components can form complexes with some of the signaling proteins
identified and may play some role in their recruitment.
Ciliary neurotrophic factor/leukemia inhibitory factor/interleukin 6/oncostatin M family of cytokines induces tyrosine phosphorylation of a common set of proteins overlapping those induced by other cytokines and growth factors
Regeneron Pharmaceuticals, Inc., Tarrytown, New York 10591.
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