A region of the β subunit of the interferon α receptor different from Box 1 interacts with Jak1 and is sufficient to activate the Jak-Stat pathway and induce an antiviral state

Paul Domanski, Eleanor Fish, Owen W. Nadeau, Michael Witte, Leonidas C. Platanias, Hai Yan, John Krolewski, Paula Pitha, Oscar R. Colamonici*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

65 Scopus citations

Abstract

Coexpression of the α and β(L) subunits of the human interferon α (IFNα) receptor is required for the induction of an antiviral state by human IFNα. To explore the role of the different domains of the β(L) subunit in IFNα signaling, we coexpressed wild-type α subunit and truncated forms of the β(L) chain in L-929 cells. Our results demonstrated that the first 82 amino acids (AAs) (AAs 265-346) of the cytoplasmic domain of the β(L) chain are sufficient to activate the Jak-Stat pathway and trigger an antiviral state after IFNα2 binding to the receptor. This region of the β(L) chain, required for Jak1 binding and activation, contains the Box 1 motif that is important for the interaction of some cytokine receptors with Jak kinases. However, using glutathione S-transferase fusion proteins containing amino- and carboxyl-terminal deletions of the β(L) cytoplasmic domain, we demonstrate that the main Jak1-binding region (corresponding to AAs 300-346 on the β subunit) is distinct from the Box 1 domain (AAs 287-295).

Original languageEnglish (US)
Pages (from-to)26388-26393
Number of pages6
JournalJournal of Biological Chemistry
Volume272
Issue number42
DOIs
StatePublished - Oct 17 1997

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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