Abstract
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).
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Carrier Proteins / analysis
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Carrier Proteins / metabolism*
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Cell Cycle Proteins
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Cells, Cultured
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Co-Repressor Proteins
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DNA-Binding Proteins
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Gene Expression Regulation
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HeLa Cells
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Humans
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Interleukin-6 / genetics
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Interleukin-6 / metabolism
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Microscopy, Fluorescence
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Models, Biological
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NF-kappa B / analysis
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NF-kappa B / metabolism*
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Signal Transduction
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TNF Receptor-Associated Death Domain Protein / metabolism
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Viral Matrix Proteins / analysis
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Viral Matrix Proteins / metabolism*
Substances
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Carrier Proteins
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Cell Cycle Proteins
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Co-Repressor Proteins
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DNA-Binding Proteins
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EBV-associated membrane antigen, Epstein-Barr virus
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Interleukin-6
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NF-kappa B
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TNF Receptor-Associated Death Domain Protein
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Viral Matrix Proteins
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ZMYND11 protein, human