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J. Biol. Chem., Vol. 275, Issue 52, 40742-40748, December 29, 2000
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From the Institut für Biochemie, Universitätsklinikum
der Rheinisch-Westfälischen Technischen Hochschule Aachen,
Pauwelsstr. 30, 52074 Aachen, Germany
The common use of the cytokine receptor gp130 has
served as an explanation for the extremely redundant biological
activities exerted by interleukin (IL)-6-type cytokines. Indeed, hardly
any differences in signal transduction initiated by these cytokines are
known. In the present study, we demonstrate that oncostatin M (OSM),
but not IL-6 or leukemia inhibitory factor, induces tyrosine phosphorylation of the Shc isoforms p52 and p66 and their association with Grb2. Concomitantly, OSM turns out to be a stronger activator of
ERK1/2 MAPKs. Shc is recruited to the OSM receptor (OSMR), but not to
gp130. Binding involves Tyr861 of the OSMR, located
within a consensus binding sequence for the Shc PTB domain. Moreover,
Tyr861 is essential for activation of ERK1/2 and for full
activation of the
Non-redundant Signal Transduction of Interleukin-6-type
Cytokines
THE ADAPTER PROTEIN Shc IS SPECIFICALLY RECRUITED TO THE
ONCOSTATIN M RECEPTOR*
2-macroglobulin promoter, but not for
an exclusively STAT-responsive promoter. This study therefore provides
evidence for qualitative differential signaling mechanisms exerted by
IL-6-type cytokines.
*
This work was supported by the Deutsche
Forschungsgemeinschaft (SFB 542) and by Fonds der Chemischen Industrie.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 49 241 8088838;
Fax: 49 241 8888428; E-mail: behrmann@rwth-aachen.de.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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