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

First Author  Matsumura T Year  2004
Journal  Biochem Biophys Res Commun Volume  317
Issue  1 Pages  230-4
PubMed ID  15047173 Mgi Jnum  J:304571
Mgi Id  MGI:6695670 Doi  10.1016/j.bbrc.2004.03.030
Citation  Matsumura T, et al. (2004) TIFAB inhibits TIFA, TRAF-interacting protein with a forkhead-associated domain. Biochem Biophys Res Commun 317(1):230-4
abstractText  Tumor necrosis factor receptor-associated factor 6 (TRAF6) transduces signals that lead to activation of NFkappaB 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 NFkappaB. 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.
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