TIFAB inhibits TIFA, TRAF-interacting protein with a forkhead-associated domain

Takayuki Matsumura, Kentaro Semba, Sakura Azuma, Shuntaro Ikawa, Jin Gohda, Taishin Akiyama, Jun Ichiro Inoue

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Tumor necrosis factor receptor-associated factor 6 (TRAF6) transduces signals that lead to activation of NFκB and AP-1, which is essential for cell differentiation and establishment of the immune and inflammatory systems. TRAF-interacting protein with a forkhead-associated domain (TIFA) was identified as a TRAF6-binding protein that could link IRAK-1 to TRAF6 and then activate TRAF6 upon stimulation. We report identification of a TIFA-related protein, TIFAB, that inhibits TIFA-mediated activation of NFκB. TIFAB does not associate with members of the TRAF family but does bind TIFA. We analyzed the effect of TIFAB expression on the TRAF6/TIFA interaction by immunoprecipitation of TRAF6 and found that TIFA coprecipitated with TRAF6 was not changed. However, when we analyzed this interaction by immunoprecipitation of TIFA, we found that TIFAB significantly increased the amount of TRAF6 coprecipitated with TIFA. These findings suggest that TIFAB inhibits the TIFA-mediated TRAF6 activation possibly by inducing a conformational change in TIFA.

Original languageEnglish
Pages (from-to)230-234
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume317
Issue number1
DOIs
Publication statusPublished - 2004 Apr 23
Externally publishedYes

Keywords

  • IL-1
  • IRAK-1
  • NFκB
  • Negative regulator
  • TIFA
  • TLR
  • TRAF

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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