BS69 negatively regulates the canonical NF-kappaB activation induced by Epstein-Barr virus-derived LMP1

FEBS Lett. 2009 May 19;583(10):1567-74. doi: 10.1016/j.febslet.2009.04.022. Epub 2009 Apr 18.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carrier Proteins / analysis
  • Carrier Proteins / metabolism*
  • Cell Cycle Proteins
  • Cells, Cultured
  • Co-Repressor Proteins
  • DNA-Binding Proteins
  • Gene Expression Regulation
  • HeLa Cells
  • Humans
  • Interleukin-6 / genetics
  • Interleukin-6 / metabolism
  • Microscopy, Fluorescence
  • Models, Biological
  • NF-kappa B / analysis
  • NF-kappa B / metabolism*
  • Signal Transduction
  • TNF Receptor-Associated Death Domain Protein / metabolism
  • Viral Matrix Proteins / analysis
  • Viral Matrix Proteins / metabolism*

Substances

  • Carrier Proteins
  • Cell Cycle Proteins
  • Co-Repressor Proteins
  • DNA-Binding Proteins
  • EBV-associated membrane antigen, Epstein-Barr virus
  • Interleukin-6
  • NF-kappa B
  • TNF Receptor-Associated Death Domain Protein
  • Viral Matrix Proteins
  • ZMYND11 protein, human