BS69 negatively regulates the canonical NF-kappaB activation induced by Epstein-Barr virus-derived LMP1.
Epstein-Barr virus (EBV) latent membrane protein 1 (LMP1) activates NF-kappaB signaling pathways through the two C-terminal regions, CTAR1 and CTAR2. BS69 has previously been shown to be involved in LMP1-induced c-Jun N-terminal kinase activation through CTAR2 by interacting with tumor necrosis factor (TNFR) receptor-associated factor 6. In the present study, ... our manipulation of BS69 expression clearly indicates that BS69 negatively regulates LMP1-mediated NF-kappaB activation and up-regulates IL-6 mRNA expression and IkappaB degradation. Our immunoprecipitation experiments suggest that BS69 decreases complex formation between LMP1 and TNFR-associated death domain protein (TRADD).
Mesh Terms:
Carrier Proteins, Cells, Cultured, Gene Expression Regulation, Hela Cells, Humans, Interleukin-6, Microscopy, Fluorescence, Models, Biological, NF-kappa B, Signal Transduction, TNF Receptor-Associated Death Domain Protein, Viral Matrix Proteins
Carrier Proteins, Cells, Cultured, Gene Expression Regulation, Hela Cells, Humans, Interleukin-6, Microscopy, Fluorescence, Models, Biological, NF-kappa B, Signal Transduction, TNF Receptor-Associated Death Domain Protein, Viral Matrix Proteins
FEBS Lett.
Date: May. 19, 2009
PubMed ID: 19379743
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