ArticleScience signaling2023
Membrane-proximal motifs encode differences in signaling strength between type I and III interferon receptors.
Article in Science signaling, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 12 citations in OpenAlex.
- A versatile fluorescent reporter for Usutu virus drug screening and infection tracking.PNAS nexus · 2026Article
- Triple IFN pathway deficiency sensitizes mice to human respiratory virus infection independent of human viral receptor expression.Nature communications · 2026Article
- Interferon lambda signaling to maternal dendritic cells protects against congenital Zika virus infection.bioRxiv : the preprint server for biology · 2026Article
- Mechanisms of Differential Signal Transduction by Interferon Lambda Receptor 1 Variants.Journal of innate immunity · 2026Article
- Mechanisms of Differential Signal Transduction by IFNLR1 Variants.bioRxiv : the preprint server for biology · 2025Article
- Receptor transporter protein 4 (RTP4)-mediated repression of hepatitis C virus replication in mouse cells.PLoS pathogens · 2025Article
- Interferons in health and disease.Cell · 2025Review
- Amino acid changes in two viral proteins drive attenuation of the yellow fever 17D vaccine.Nature microbiology · 2025Article
- Engineered chimeric receptors for dissecting interferon signaling.Journal of virology · 2024Review
- Liver-specific Mettl14 deletion induces nuclear heterotypia and dysregulates RNA export machinery.bioRxiv : the preprint server for biology · 2024Article
- Structure-function of type I and III interferons.Current opinion in immunology · 2024Review
- Synthetic Heterodimers of Type III Interferon Receptors Require TYK2 for STAT Activation.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2023Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Interferons (IFNs) play crucial roles in antiviral defenses. Despite using the same Janus-activated kinase (JAK)-signal transducer and activator of transcription (STAT) signaling cascade, type I and III IFN receptors differ in the magnitude and dynamics of their signaling in terms of STAT phosphorylation, gene transcription, and antiviral responses. These differences are not due to ligand-binding affinity and receptor abundance. Here, we investigated the ability of the intracellular domains (ICDs) of IFN receptors to differentiate between type I and III IFN signaling. We engineered synthetic, heterodimeric type I and III IFN receptors that were stably expressed at similar amounts in human cells and responded to a common ligand. We found that our synthetic type I IFN receptors stimulated STAT phosphorylation and gene expression to greater extents than did the corresponding type III IFN receptors. Furthermore, we identified short "box motifs" within ICDs that bind to JAK1 that were sufficient to encode differences between the type I and III IFN receptors. Together, our results indicate that specific regions within the ICDs of IFN receptor subunits encode different downstream signaling strengths that enable type I and III IFN receptors to produce distinct signaling outcomes.
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