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J Biol Chem, Vol. 274, Issue 7, 4045-4052, February 12, 1999

The Proximal Tyrosines of the Cytoplasmic Domain of the beta  Chain of the Type I Interferon Receptor Are Essential for Signal Transducer and Activator of Transcription (Stat) 2 Activation
EVIDENCE THAT TWO Stat2 SITES ARE REQUIRED TO REACH A THRESHOLD OF INTERFERON alpha -INDUCED Stat2 TYROSINE PHOSPHORYLATION THAT ALLOWS NORMAL FORMATION OF INTERFERON-STIMULATED GENE FACTOR 3

Owen W. Nadeaua, Paul Domanskia, Anna Usachevaac, Shahab Uddind, Leonidas C. Plataniasd, Paula Pithae, Regina Razf, David Levyf, Beata Majchrzakg, Eleanor Fishg, and Oscar R. Colamonicia

From the a Department of Pathology, University of Tennessee, Memphis, Tennessee 38163, the c Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, Russia, d Section of Hematology/Oncology, University of Illinois, Chicago, Illinois 60606, g Department of Medical Genetics and Microbiology, University of Toronto, Toronto, Ontario M5S 3E2, Canada, f Department of Pathology, New York University School of Medicine, New York, New York 10016, and the e Oncology Center, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21231

The precise role of the different subunits (alpha /IFNAR1 and beta L/IFNAR2) of the type I interferon receptor (IFN-R) in the activation of signal transducer and activator of transcription (Stat) 1, Stat2, and Stat3 has not yet been established. In this report we demonstrate that there are functionally redundant phosphotyrosine-dependent and -independent binding sites for Stat2 in the alpha  and beta  subunits of the type I IFN-R. Expression of a type I IFN-R containing only the constitutive Stat2 site or the proximal tyrosines of beta L, but not the docking site on the alpha  chain (Tyr466 and Tyr481), supported low levels of Stat2 activation. However, the presence of only one intact Stat2 site did not lead to induction of interferon-stimulated gene factor 3 (ISGF3) or an antiviral state. Normal levels of Stat2 tyrosine phosphorylation, induction of ISGF3, and an antiviral effect always required the proximal tyrosines of beta L and at least one of the other Stat2 sites (Tyralpha 466, 481 or beta L404-462). These data suggest that a threshold of Stat2 tyrosine phosphorylation is required for complete activation of ISGF3. Interestingly, a receptor in which all tyrosines were mutated to phenylalanine shows normal Stat3 phosphorylation and low levels of activation of Stat1.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.


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