Reference : A completely foreign receptor can mediate an interferon-gamma-like response
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
A completely foreign receptor can mediate an interferon-gamma-like response
Strobl, B. [> >]
Arulampalam, V. [> >]
Isharc, H. [> >]
Newman, S. J. [> >]
Schlaak, J. F. [> >]
Watling, D. [> >]
Costa-Pereira, A. P. [> >]
Schaper, F. [> >]
Behrmann, Iris mailto [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. [> >]
EMBO Journal
Oxford University Press
Yes (verified by ORBilu)
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.

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