Oncostatin M receptor-mediated signal transduction is negatively regulated by suppressor of cytokine signaling (SOCS) 3 through a receptor tyrosine-independent mechanism

doi:10.1074/jbc.M511212200

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Papers In Press, published online ahead of print February 2, 2006
J. Biol. Chem, 10.1074/jbc.M511212200
Submitted on October 14, 2005
Accepted on February 2, 2006

Oncostatin M receptor-mediated signal transduction is negatively regulated by suppressor of cytokine signaling (SOCS) 3 through a receptor tyrosine-independent mechanism

Claudia Stross, Simone Radtke, Thomas Clahsen, Christa Gerlach, Rudolf Volkmer-Engert, Fred Schaper, Peter C. Heinrich, and Heike M. Hermanns

Institut für Biochemie, Universitätsklinikum RWTH Aachen, Aachen, NRW 52074

Corresponding Author: hermanns{at}rwth-aachen.de

Downregulation of interleukin (IL)-6-type cytokine signaling has been shown to occur, among other mechanisms, via induction of the feedback inhibitor suppressor of cytokine signaling 3 (SOCS3). Binding of SOCS3 to the phosphorylated Y759 in the cytoplasmic region of gp130, the common signal transducing receptor chain of all IL-6-type cytokines, is necessary for inhibition of Janus kinase (JAK)-mediated signaling. In the present study, we analyzed the effect of SOCS3 on signal transduction by the pro-inflammatory cytokine oncostatin M (OSM), which signals through a receptor complex of gp130 and the OSMR. OSM leads to a much stronger and prolonged induction of SOCS3 in HepG2 hepatoma cells and murine embryonal fibroblasts (MEF) compared to IL-6. A negative effect of SOCS3 on OSM signaling was confirmed using MEF cells lacking SOCS3. We can show that the OSMR-mediated signaling is inhibited by SOCS3 to a similar extent as previously described for gp130. However, the inhibition occurs independent of tyrosine motifs within the OSMR. Instead SOCS3 interacts directly with JAK1 in a stimulation-dependent manner, a mechanism so far only known for SOCS1.

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