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Wiley, FEBS Letters, 5(584), p. 865-872, 2010

DOI: 10.1016/j.febslet.2010.01.060

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BS69 cooperates with TRAF3 in the regulation of Epstein-Barr virus-derived LMP1/CTAR1-induced NF-κB activation

Journal article published in 2010 by Osamu Ikeda, Yuto Miyasaka, Ryuji Yoshida, Akihiro Mizushima, Kenji Oritani, Yuichi Sekine ORCID, Makoto Kuroda, Teruhito Yasui, Masahiro Fujimuro, Ryuta Muromoto, Asuka Nanbo, Tadashi Matsuda
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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Abstract

Epstein-Barr virus latent membrane protein 1 (LMP1) activates NF-kappaB signaling pathways through two C-terminal regions, CTAR1 and CTAR2. Previous studies have demonstrated that BS69, a multidomain cellular protein, regulates LMP1/CTAR2-mediated NF-kappaB activation by interfering with the complex formation between TRADD and LMP1/CTAR2. Here, we found that BS69 directly interacted with the LMP1/CTAR1 domain and regulated LMP1/CTAR1-mediated NF-kappaB activation and subsequent IL-6 production. Regarding the mechanisms involved, we found that BS69 directly interacted with TRAF3, a negative regulator of NF-kappaB activation. Furthermore, small-interfering RNA-mediated knockdown experiments revealed that TRAF3 was involved in the BS69-mediated suppression of LMP1/CTAR1-induced NF-kappaB activation.