Differences in interferon α and β signaling: Interferon β selectively induces the interaction of the α and β(L) subunits of the type I interferon receptor

Leonidas C. Platanias*, Shahab Uddin, Paul Domanski, Oscar R. Colamonici

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

102 Scopus citations

Abstract

All Type I interferons (IFNα, IFNβ, IFNω) bind to the Type I IFN receptor (IFNR) and elicit a common set of signaling events, including activation of the Jak/Stat and IRS pathways. However, IFNβ selectively induces the association of the α subunit of the Type I IFNR with p100, a tyrosyl phosphoprotein, to transduce IFNβ-specific signals. Using antibodies raised against the different components of the Type I IFNR, we identified p100 as the long form of the β subunit (β(L) subunit) of the Type I IFNR. This was also confirmed in experiments with mouse L-929 cells transfected with truncated forms of β(L). Thus, IFNβ stimulation of human cells or mouse L-929 transfectants expressing the human α and β(L) subunits, selectively induces the formation of a signaling complex containing the α and β(L) subunits of the receptor. The IFNβ-regulated interaction of the α and β(L) chains is rapid and transient and follows a similar time course with the tyrosine phosphorylation of these receptor components. These data demonstrate that the signaling specificity for different Type I IFNs is established early in the signaling cascade, at the receptor level, and results from distinct interactions between components of the Type I IFNR.

Original languageEnglish (US)
Pages (from-to)23630-23633
Number of pages4
JournalJournal of Biological Chemistry
Volume271
Issue number39
DOIs
StatePublished - 1996

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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