Lys63/Met1-hybrid ubiquitin chains are commonly formed during the activation of innate immune signalling.

Christoph Emmerich, Siddharth Bakshi, Ian Kelsall, Juan Ortiz-Guerrero, Natalia Shpiro, Philip Cohen (Lead / Corresponding author)

Research output: Contribution to journalArticlepeer-review

42 Citations (Scopus)
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Abstract

We have reported previously that activation of the MyD88-signaling network rapidly induces the formation of hybrid ubiquitin chains containing both Lys63-linked and Met1-linked ubiquitin (Ub) oligomers, some of which are attached covalently to Interleukin Receptor Associated kinase 1. Here we show that Lys63/Met1-Ub hybrids are also formed rapidly when the TNFα, TLR3/TRIF- and NOD1/RIP2-signaling networks are activated, some of which are attached covalently to Receptor-Interacting Protein 1 (TNFα pathway) or Receptor-Interacting Protein 2 (NOD1 pathway). These observations suggest that the formation of Lys63/Met1-Ub hybrids are of general significance for the regulation of innate immune signaling systems, and their potential roles in vivo are discussed. We also report that TNFα induces the attachment of Met1-linked Ub chains directly to TNF receptor 1, which do not seem to be attached covalently to Lys63-linked or other types of ubiquitin chain.
Original languageEnglish
Pages (from-to)452-461
Number of pages10
JournalBiochemical and Biophysical Research Communications
Volume474
Issue number3
Early online date28 Apr 2016
DOIs
Publication statusPublished - 3 Jun 2016

Keywords

  • Ubiquitin
  • innate
  • immunity
  • TNF
  • TLR3
  • NOD1
  • LUBAC

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