MIP-T3 associates with IL-13Rα1 and suppresses STAT6 activation in response to IL-13 stimulation

Yamei Niu, Takashi Murata, Ken Watanabe, Koji Kawakami, Akihiko Yoshimura, Jun ichiro Inoue, Raj K. Puri, Nobuyuki Kobayashi

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

To unravel the mechanism of interleukin-13 (IL-13)-specific functions, we sought to identify IL-13 receptor (IL-13R) binding molecules. A novel human IL-13Rα1 binding protein (IL13RBP1) has been identified using yeast tri-hybrid system, which was found to encode the same protein as MIP-T3 (microtubule interacting protein that associates with tumor necrosis factor (TNF) receptor associating factor-3 (TRAF3)). It constitutively associates with IL-13Rα1 and suppresses IL-4/13-induced signal transducer and activator of transcription-6 (STAT6) phosphorylation. IL-13-induced STAT6 activation was also inhibited as determined by dual luciferase assay and electrophoretic mobility shift assay (EMSA). These results suggest that MIP-T3 is a novel inhibitor of IL-13 signaling and may be a useful molecule in ameliorating various conditions in which IL-13 plays a central role.

Original languageEnglish
Pages (from-to)139-143
Number of pages5
JournalFEBS Letters
Volume550
Issue number1-3
DOIs
Publication statusPublished - 2003 Aug 28

Keywords

  • Interleukin-13
  • Interleukin-13 receptor-α1 binding protein-1
  • Interleukin-4
  • Microtubule interacting protein that associates with tumor necrosis factor receptor associating factor-3
  • Signal transducer and activator of transcription-6

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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