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

被引：14

作者：

Ikeda, Osamu

Miyasaka, Yuto

Yoshida, Ryuji

Mizushima, Akihiro

Oritani, Kenji ^{[2
]}

Sekine, Yuichi

Kuroda, Makoto

Yasui, Teruhito ^{[3
]}

Fujimuro, Masahiro ^{[4
]}

Muromoto, Ryuta

Nanbo, Asuka

Matsuda, Tadashi ^{[1
]}

机构：

[1] Hokkaido Univ, Grad Sch Pharmaceut Sci, Dept Immunol, Kita Ku, Sapporo, Hokkaido 0600812, Japan

[2] Osaka Univ, Grad Sch Med, Dept Hematol & Oncol, Suita, Osaka 5650871, Japan

[3] Osaka Univ, Microbial Dis Res Inst, Dept Mol Immunol, Suita, Osaka 5650871, Japan

[4] Univ Yamanashi, Interdisciplinary Grad Sch Med & Engn, Dept Mol Cell Biol, Chuo 4093898, Japan

来源：

FEBS LETTERS | 2010年 / 584卷 / 05期

关键词：

BS69; EBV; LMP1; TRAF3; NF-kappa B; Transcription; LATENT MEMBRANE-PROTEIN; TRANSFORMING PROTEIN; BINDING-SITE; ENGAGES; LMP1; MEMBRANE-PROTEIN-1; DOMAIN; LYMPHOCYTES; NF-KAPPA-B2; PATHWAY;

D O I：

10.1016/j.febslet.2010.01.060

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Epstein-Barr virus latent membrane protein 1 (LMP1) activates NF-kappa B 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-kappa B 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-kappa B activation and subsequent IL-6 production. Regarding the mechanisms involved, we found that BS69 directly interacted with TRAF3, a negative regulator of NF-kappa B activation. Furthermore, small-interfering RNA-mediated knockdown experiments revealed that TRAF3 was involved in the BS69-mediated suppression of LMP1/CTAR1-induced NF-kappa B activation. Structured summary: MINT-7556591: lmp1 (uniprotkb: P03230) physically interacts (MI:0915) with BS69 (uniprotkb:Q15326) by anti tag coimmunoprecipitation (MI: 0007) MINT-7556646: TRAF6 (uniprotkb:Q9Y4K3) physically interacts (MI: 0915) with BS69 (uniprotkb: Q15326) by anti tag coimmunoprecipitation (MI: 0007) MINT-7556658, MINT-7556670: TRAF3 (uniprotkb:Q13114) physically interacts (MI: 0915) with BS69 (uniprotkb: Q15326) by anti tag coimmunoprecipitation (MI: 0007) MINT-7556607: TRAF1 (uniprotkb:Q13077) physically interacts (MI: 0915) with BS69 (uniprotkb: Q15326) by anti tag coimmunoprecipitation (MI: 0007) MINT-7556634: TRAF5 (uniprotkb:O00463) physically interacts (MI: 0915) with BS69 (uniprotkb: Q15326) by anti tag coimmunoprecipitation (MI: 0007) MINT-7556622: TRAF2 (uniprotkb:Q12933) physically interacts (MI: 0915) with BS69 (uniprotkb: Q15326) by anti tag coimmunoprecipitation (MI: 0007) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：865 / 872

页数：8

共 26 条

[1] The conserved Mynd domain of BS69 binds cellular and oncoviral proteins through a common PXLXP motif [J].