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Originally published In Press as doi:10.1074/jbc.M005408200 on October 2, 2000

J. Biol. Chem., Vol. 275, Issue 52, 40742-40748, December 29, 2000
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Non-redundant Signal Transduction of Interleukin-6-type Cytokines
THE ADAPTER PROTEIN Shc IS SPECIFICALLY RECRUITED TO THE ONCOSTATIN M RECEPTOR*

Heike M. Hermanns, Simone Radtke, Fred Schaper, Peter C. Heinrich, and Iris BehrmannDagger

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 alpha 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.

Dagger 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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