| Literature DB >> 20138174 |
Osamu Ikeda1, Yuto Miyasaka, Ryuji Yoshida, Akihiro Mizushima, Kenji Oritani, Yuichi Sekine, Makoto Kuroda, Teruhito Yasui, Masahiro Fujimuro, Ryuta Muromoto, Asuka Nanbo, Tadashi Matsuda.
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. Copyright (c) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.Entities:
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Year: 2010 PMID： 20138174 DOI： 10.1016/j.febslet.2010.01.060
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124