Regulation of MDA5-MAVS antiviral signaling axis by TRIM25 through TRAF6-mediated NF-κB activation

Na Rae Lee, Hye In Kim, Myung Soo Choi, Chae Min Yi, Kyung Soo Inn

Research output: Contribution to journalArticlepeer-review

43 Citations (Scopus)

Abstract

Tripartite motif protein 25 (TRIM25), mediates K63-linked polyubiquitination of Retinoic acid inducible gene I (RIG-I) that is crucial for downstream antiviral interferon signaling. Here, we demonstrate that TRIM25 is required for melanoma differentiation-associated gene 5 (MDA5) and MAVS mediated activation of NF-κB and interferon production. TRIM25 is required for the full activation of NF-κB at the downstream of MAVS, while it is not involved in IRF3 nuclear translocation. Mechanical studies showed that TRIM25 is involved in TRAF6-mediated NF-κB activation. These collectively indicate that TRIM25 plays an additional role in RIG-I/MDA5 signaling other than RIG-I ubiquitination via activation of NF-κB.

Original languageEnglish
Pages (from-to)756-764
Number of pages9
JournalMolecules and Cells
Volume38
Issue number9
DOIs
Publication statusPublished - 2015

Bibliographical note

Publisher Copyright:
© The Korean Society for Molecular and Cellular Biology.

Keywords

  • MAVS
  • MDA5
  • NF-κB
  • TRAF6
  • TRIM25

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