K63-linked polyubiquitination of transcription factor IRF1 is essential for IL-1-induced production of chemokines CXCL10 and CCL5

  • Kuzhuvelil B. Harikumar
  • , Jessie W. Yester
  • , Michael J. Surace
  • , Clement Oyeniran
  • , Megan M. Price
  • , Wei Ching Huang
  • , Nitai C. Hait
  • , Jeremy C. Allegood
  • , Akimitsu Yamada
  • , Xiangqian Kong
  • , Helen M. Lazear
  • , Reetika Bhardwaj
  • , Kazuaki Takabe
  • , Michael S. Diamond
  • , Cheng Luo
  • , Sheldon Milstien
  • , Sarah Spiegel
  • , Tomasz Kordula

Research output: Contribution to journalArticlepeer-review

110 Scopus citations

Abstract

Although interleukin 1 (IL-1) induces expression of the transcription factor IRF1 (interferon-regulatory factor 1), the roles of IRF1 in immune and inflammatory responses and mechanisms of its activation remain elusive. Here we found that IRF1 was essential for IL-1-induced expression of the chemokines CXCL10 and CCL5, which recruit mononuclear cells into sites of sterile inflammation. Newly synthesized IRF1 acquired Lys63 (K63)-linked polyubiquitination mediated by the apoptosis inhibitor cIAP2 that was enhanced by the bioactive lipid S1P. In response to IL-1, cIAP2 and the sphingosine kinase SphK1 (the enzyme that generates S1P) formed a complex with IRF1, which led to its activation. Thus, IL-1 triggered a hitherto unknown signaling cascade that controlled the induction of IRF1-dependent genes that encode molecules important for sterile inflammation.

Original languageEnglish
Pages (from-to)231-238
Number of pages8
JournalNature immunology
Volume15
Issue number3
DOIs
StatePublished - Mar 2014

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