| Reference : A completely foreign receptor can mediate an interferon-gamma-like response |
| Scientific journals : Article | |||
| Life sciences : Biochemistry, biophysics & molecular biology | |||
| http://hdl.handle.net/10993/6241 | |||
| A completely foreign receptor can mediate an interferon-gamma-like response | |
| English | |
| Strobl, B. [> >] | |
| Arulampalam, V. [> >] | |
| Isharc, H. [> >] | |
| Newman, S. J. [> >] | |
| Schlaak, J. F. [> >] | |
| Watling, D. [> >] | |
| Costa-Pereira, A. P. [> >] | |
| Schaper, F. [> >] | |
Behrmann, Iris  [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit >] | |
| Sheehan, K. C. [> >] | |
| Schreiber, R. D. [> >] | |
| Horn, F. [> >] | |
| Heinrich, P. C. [> >] | |
| Kerr, I. M. [> >] | |
| 2001 | |
| EMBO Journal | |
| Oxford University Press | |
| 20 | |
| 19 | |
| 5431-42 | |
| Yes (verified by ORBilu) | |
| International | |
| 0261-4189 | |
| 1460-2075 | |
| Oxford | |
| United Kingdom | |
| [en] Trans-Activators ; Gene Expression Regulation ; Histocompatibility Antigens Class II ; Humans ; Interferon Type II ; Nuclear Proteins ; Receptor, Interferon alpha-beta ; Receptors, Erythropoietin ; Receptors, Immunologic ; Receptors, Interferon ; Receptors, Interleukin-6 ; Recombinant Fusion Proteins ; STAT1 Transcription Factor ; Signal Transduction ; DNA-Binding Proteins | |
| [en] A tripartite receptor comprising the external region of the erythropoietin (Epo) receptor, the transmembrane and JAK-binding domains of the gp130 subunit of the interleukin-6 (IL-6) receptor, and a seven amino acid STAT1 recruitment motif (Y440) from the interferon (IFN)-gamma receptor, efficiently mediates an IFN-gamma-like response. An analogous completely foreign chimeric receptor in which the Y440 motif is replaced with the Y905 motif from gp130 also mediates an IFN-gamma-like response, but less efficiently. The IFNGR1 signal-transducing subunit of the IFN-gamma receptor is tyrosine phosphorylated through the chimeric receptors and the endogenous IL-6 and OSM receptors. Cross phosphorylation of IFNGR1 is not, however, required for the IFN-gamma-like response through the chimeric receptors, nor does it mediate an IFN-gamma-like response to IL-6 or OSM. The data argue strongly for modular JAK/STAT signalling and against any rigid structural organization for the "pathways" involved. They emphasize the likely high degree of overlap between the signals generated from disparate JAK-receptor complexes and show that relatively minor changes in such complexes can profoundly affect the response. | |
| http://hdl.handle.net/10993/6241 | |
| 10.1093/emboj/20.19.5431 |
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