This is a preview of subscription content, access via your institution
Access options
Access Nature and 54 other Nature Portfolio journals
Get Nature+, our best-value online-access subscription
$29.99 / 30 days
cancel any time
Subscribe to this journal
Receive 12 digital issues and online access to articles
$119.00 per year
only $9.92 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Data availability
All data are available from the corresponding author on reasonable request.
References
Guo, T. et al. ADP-ribosyltransferase PARP11 modulates the interferon antiviral response by mono-ADP-ribosylating the ubiquitin E3 ligase β-TrCP. Nat. Microbiol. https://doi.org/10.1038/s41564-019-0428-3 (2019).
Ling, L. E. et al. Human type I interferon receptor, IFNAR, is a heavily glycosylated 120-130 kD membrane protein. J. Interf. Cytok. Res. 15, 55–61 (1995).
Constantinescu, S. N. et al. Expression and signaling specificity of the IFNAR chain of the type I interferon receptor complex. Proc. Natl Acad. Sci. USA 92, 10487–10491 (1995).
Wang, C. et al. Enterovirus 71 suppresses interferon responses by blocking Janus kinase (JAK)/signal transducer and activator of transcription (STAT) signaling through inducing karyopherin-α1 degradation. J. Biol. Chem. 292, 10262–10274 (2017).
Xia, C. et al. Hemagglutinin of influenza A virus antagonizes type I interferon (IFN) responses by inducing degradation of type I IFN receptor 1. J. Virol. 90, 2403–2417 (2015).
Teijaro, J. R. et al. S1PR1-mediated IFNAR1 degradation modulates plasmacytoid dendritic cell interferon-α autoamplification. Proc. Natl Acad. Sci. USA 113, 1351–1356 (2016).
Walters, D. K. & Jelinek, D. F. A role for Janus kinases in crosstalk between ErbB3 and the interferon-alpha signaling complex in myeloma cells. Oncogene 23, 1197–1205 (2004).
Sen, A., Sharma, A. & Greenberg, H. B. Rotavirus degrades multiple interferon (IFN) type receptors to inhibit IFN signaling and protects against mortality from endotoxin in suckling mice. J. Virol. 92, e01394-17 (2017).
Shah, K. M. et al. The EBV-encoded latent membrane proteins, LMP2A and LMP2B, limit the actions of interferon by targeting interferon receptors for degradation. Oncogene 28, 3903–3914 (2009).
Lubick, K. J. et al. Flavivirus antagonism of type I interferon signaling reveals prolidase as a regulator of IFNAR1 surface expression. Cell Host Microbe 18, 61–74 (2015).
Kumar, K. G., Krolewski, J. J. & Fuchs, S. Y. Phosphorylation and specific ubiquitin acceptor sites are required for ubiquitination and degradation of the IFNAR1 subunit of type I interferon receptor. J. Biol. Chem. 279, 46614–46620 (2004).
Kurt, R. et al. Chaperone-mediated autophagy targets IFNAR1 for lysosomal degradation in free fatty acid treated HCV cell culture. PLoS ONE 10, e0125962 (2015).
Ragimbeau, J. et al. The tyrosine kinase Tyk2 controls IFNAR1 cell surface expression. EMBO J. 22, 537–547 (2003).
Acknowledgements
We thank X. Zhu for the numerical analysis of the original FACS data.
Author information
Authors and Affiliations
Contributions
T.G. and H.Z. further analysed previous data. T.G. and J.L. conducted experiments to analyse all three types of glycosylated IFNAR1. T.G., X.C., L.J. and F.H. performed the FACS experiments. T.G. and H.Z. wrote the paper.
Corresponding author
Ethics declarations
Competing interests
The authors declare no competing interests.
Additional information
Publisher’s note Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Source data
Rights and permissions
About this article
Cite this article
Guo, T., Liu, J., Chen, X. et al. PARP11 regulates total levels of type-I interferon receptor IFNAR1. Nat Microbiol 4, 1771–1773 (2019). https://doi.org/10.1038/s41564-019-0582-7
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1038/s41564-019-0582-7
