Pathogen recognition receptor signaling accelerates phosphorylation-dependent degradation of IFNAR1

Juan Qian, Hui Zheng, Wei Chun HuangFu, Jianghuai Liu, Christopher J. Carbone, N. Adrian Leu, Darren P. Baker, Serge Y. Fuchs

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

An ability to sense pathogens by a number of specialized cell types including the dendritic cells plays a central role in host's defenses. Activation of these cells through the stimulation of the pathogen-recognition receptors induces the production of a number of cytokines including Type I interferons (IFNs) that mediate the diverse mechanisms of innate immunity. Type I IFNs interact with the Type I IFN receptor, composed of IFNAR1 and IFNAR2 chains, to mount the host defense responses. However, at the same time, Type I IFNs elicit potent anti-proliferative and pro-apoptotic effects that could be detrimental for IFN-producing cells. Here, we report that the activation of p38 kinase in response to pathogen-recognition receptors stimulation results in a series of phosphorylation events within the IFNAR1 chain of the Type I IFN receptor. This phosphorylation promotes IFNAR1 ubiquitination and acceleing and the protection of activated dendritic cells from the cytotoxic effects of autocrine or paracrine Type I IFN. In this paper we discuss a potential role of this mechanism in regulating the processes of innate immunity.

Original languageEnglish
Article numbere1002065
JournalPLoS Pathogens
Volume7
Issue number6
DOIs
Publication statusPublished - Jun 2011

ASJC Scopus subject areas

  • Parasitology
  • Microbiology
  • Immunology
  • Molecular Biology
  • Genetics
  • Virology

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    Qian, J., Zheng, H., HuangFu, W. C., Liu, J., Carbone, C. J., Leu, N. A., Baker, D. P., & Fuchs, S. Y. (2011). Pathogen recognition receptor signaling accelerates phosphorylation-dependent degradation of IFNAR1. PLoS Pathogens, 7(6), [e1002065]. https://doi.org/10.1371/journal.ppat.1002065