Signaling Steps Involving the Cytoplasmic Domain of the Interferon-Gamma Receptor Alpha-Subunit Are Not Species-Specific

The ligand binding chain of the interferon-gamma receptor (IFN-gamma R) is a unique cell surface protein which has no similarities to other cytokine receptors. Expression of this receptor chain (alpha-subunit) is not sufficient to mediate responsiveness to IFN-gamma. We and others have shown that IFN-gamma-mediated signal transduction requires a species-specific interaction of the extracellular portion of the known IFN-gamma receptor alpha-chain with an additional receptor subunit that was cloned recently and designated IFN-gamma R beta-chain or accessory factor 1. Here, we investigated whether this tight species barrier also ap plies to signaling events mediated by the cytoplasmic receptor domain. A cell line derived from embryos that lack the IFN-gamma R alpha-subunit was reconstituted with a hybrid mouse-human alpha-subunit that consisted of an extracellular murine and transmembrane and cytoplasmic human domains. The experiments reported herein showed that in mouse cells, the human intracellular domain of the hybrid IFN-gamma R alpha-subunit was fully functional and that, therefore, signaling steps involving this domain are not species-specific.

Published in:
Journal of Biological Chemistry, 269, 20, 14541-14545
Univ Zurich,Inst Molec Biol 1,Ch-8093 Zurich,Switzerland

 Record created 2007-12-12, last modified 2020-07-30

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