Title: Differential tyrosine phosphorylation of the IFNAR chain of the type I interferon receptor and of an associated surface protein in response to IFN-alpha and IFN-beta.
Abstract: Research Article15 December 1994free access Differential tyrosine phosphorylation of the IFNAR chain of the type I interferon receptor and of an associated surface protein in response to IFN-alpha and IFN-beta. C. Abramovich C. Abramovich Department of Molecular Genetics and Virology, Weizmann Institute of Science, Rehovot, Israel. Search for more papers by this author L.M. Shulman L.M. Shulman Department of Molecular Genetics and Virology, Weizmann Institute of Science, Rehovot, Israel. Search for more papers by this author E. Ratovitski E. Ratovitski Department of Molecular Genetics and Virology, Weizmann Institute of Science, Rehovot, Israel. Search for more papers by this author S. Harroch S. Harroch Department of Molecular Genetics and Virology, Weizmann Institute of Science, Rehovot, Israel. Search for more papers by this author M. Tovey M. Tovey Department of Molecular Genetics and Virology, Weizmann Institute of Science, Rehovot, Israel. Search for more papers by this author P. Eid P. Eid Department of Molecular Genetics and Virology, Weizmann Institute of Science, Rehovot, Israel. Search for more papers by this author M. Revel M. Revel Department of Molecular Genetics and Virology, Weizmann Institute of Science, Rehovot, Israel. Search for more papers by this author C. Abramovich C. Abramovich Department of Molecular Genetics and Virology, Weizmann Institute of Science, Rehovot, Israel. Search for more papers by this author L.M. Shulman L.M. Shulman Department of Molecular Genetics and Virology, Weizmann Institute of Science, Rehovot, Israel. Search for more papers by this author E. Ratovitski E. Ratovitski Department of Molecular Genetics and Virology, Weizmann Institute of Science, Rehovot, Israel. Search for more papers by this author S. Harroch S. Harroch Department of Molecular Genetics and Virology, Weizmann Institute of Science, Rehovot, Israel. Search for more papers by this author M. Tovey M. Tovey Department of Molecular Genetics and Virology, Weizmann Institute of Science, Rehovot, Israel. Search for more papers by this author P. Eid P. Eid Department of Molecular Genetics and Virology, Weizmann Institute of Science, Rehovot, Israel. Search for more papers by this author M. Revel M. Revel Department of Molecular Genetics and Virology, Weizmann Institute of Science, Rehovot, Israel. Search for more papers by this author Author Information C. Abramovich1, L.M. Shulman1, E. Ratovitski1, S. Harroch1, M. Tovey1, P. Eid1 and M. Revel1 1Department of Molecular Genetics and Virology, Weizmann Institute of Science, Rehovot, Israel. The EMBO Journal (1994)13:5871-5877https://doi.org/10.1002/j.1460-2075.1994.tb06932.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info The human interferon alpha-receptor (IFNAR gene product) is a transmembranal protein of 557 amino acids with an intracytoplasmic domain of 100 amino acids containing four tyrosines. Antibodies to a C-terminal peptide (residues 521-536) were developed which efficiently immunoprecipitate the 105 kDa IFNAR protein from detergent extracts of human cells. We show that the IFNAR protein becomes tyrosine phosphorylated within 5 min after treatment of human myeloma U266 cells with IFN-alpha 2, IFN-alpha 8 or IFN-beta. The IFNAR chain interacts with both IFN-alpha 2 and IFN-beta, as demonstrated by cross-linking. Among elements involved in signal transduction by type I IFNs, the tyrosine kinase Tyk2 but not Jak1, and the ISGF3 transcription factor subunit Stat2 (p113) but not Stat1 (p91), are found associated with the IFNAR protein. After IFN-beta treatment for 5 min, a tyrosine-phosphorylated protein of approximately 95 kDa (beta-PTyr) is found bound to IFNAR, but can be dissociated by denaturation. The beta-PTyr protein is present on the cell surface, like IFNAR, as shown by extracellular biotin tagging. The ratio of beta-PTyr to IFNAR tyrosine phosphorylation is much higher with IFN-beta than with IFN-alpha 2 or 8. Both are IFN dependent and abrogated by a monoclonal antibody which blocks IFNAR action. The beta-PTyr component may represent an important difference in the action of IFN-beta as compared with IFN-alpha in their shared receptor system. Previous ArticleNext Article Volume 13Issue 241 December 1994In this issue RelatedDetailsLoading ...