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Papers In Press, published online ahead of print January 10, 2002
Institute for Biochemistry, Aachen 52074
Corresponding Author: behrmann{at}rwth-aachen.de
The oncostatin M receptor (OSMR) is part of a heterodimeric receptor complex which mediates signal transduction of the pleiotropic cytokine OSM via a signalling pathway involving Janus kinases (Jaks) and transcription factors of the signal transducers and activators of transcription (STAT) family. Upon heterologous expression of the OSMR in several cell lines, we observed that its surface expression was significantly enhanced by coexpression of the Janus kinases Jak1, Jak2 and Tyk2 but not Jak3. Chimeric receptors consisting of the extracellular region of the IL-5Rb chain and the transmembrane and intracellular part of the OSMR were similarly upregulated on the plasma membrane when Jak1 was coexpressed. The overall expression level of these constructs did not change significantly but Jak1 coexpression increased the amount of EndoH-resistant, fully processed OSMR chimeras. Using mutated receptor and Jak1 constructs, we were able to demonstrate that association of Jak1 with the membrane proximal region of the receptor but not its kinase activity is necessary for this effect. Moreover, deletion of the OSMR-box1/2 region also resulted in an improved surface expression indicating that this region may contain a signal preventing efficient receptor surface expression in the absence of associated Jaks. Finally we demonstrate that in Jak1-deficient cells, the endogenous OSMR is significantly downregulated, an effect which can be reversed by transient expression of Jak1 in these cells.
J. Biol. Chem, 10.1074/jbc.M100822200
Submitted on January 29, 2001
Revised on December 22, 2001
Accepted on January 9, 2002
Novel role for Janus kinase 1 in the regulation of oncostatin M receptor surface expression
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