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Identification of a cell protein (FIP-3) as a modulator of NF-kappaB activity and as a target of an adenovirus inhibitor of tumor necrosis factor alpha-induced apoptosis.

FIP-3 (14.7K interacting protein) was discovered during a search for cell proteins that could interact with an adenovirus protein (Ad E3-14.7K) that had been shown to prevent tumor necrosis factor (TNF)-alpha-induced cytolysis. FIP-3, which contains leucine zippers and a zinc finger domain, inhibits both basal and induced transcriptional activity of NF-kappaB and causes a late-appearing apoptosis with unique morphologic manifestations. Ad E3-14.7K can partially reverse apoptotic death induced by FIP-3. FIP-3 also was shown to bind to other cell proteins, RIP and NIK, which previously had been described as essential components of TNF-alpha-induced NF-kappaB activation. In addition, FIP-3 inhibited activation of NF-kappaB induced by TNF-alpha, the TNFR-1 receptor, RIP, NIK, and IKKbeta, as well as basal levels of endogenous NF-kappaB in 293 cells. Because the activation of NF-kappaB has been shown to inhibit apoptosis, FIP-3 appears both to activate a cell-death pathway and to inhibit an NF-kappaB-dependent survival mechanism.

Pubmed ID: 9927690


  • Li Y
  • Kang J
  • Friedman J
  • Tarassishin L
  • Ye J
  • Kovalenko A
  • Wallach D
  • Horwitz MS


Proceedings of the National Academy of Sciences of the United States of America

Publication Data

February 2, 1999

Associated Grants

  • Agency: NCI NIH HHS, Id: 5T32CA 09060
  • Agency: NCI NIH HHS, Id: CA13330
  • Agency: NCI NIH HHS, Id: R01 CA72963

Mesh Terms

  • Adenoviridae
  • Adenovirus E3 Proteins
  • Amino Acid Sequence
  • Apoptosis
  • Carrier Proteins
  • Cell Line
  • Cell Survival
  • Glutathione Transferase
  • Humans
  • I-kappa B Kinase
  • Leucine Zippers
  • Molecular Sequence Data
  • Molecular Weight
  • NF-kappa B
  • Protein Kinases
  • Protein-Serine-Threonine Kinases
  • Proteins
  • Receptor-Interacting Protein Serine-Threonine Kinases
  • Recombinant Fusion Proteins
  • Recombinant Proteins
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Transcriptional Activation
  • Tumor Necrosis Factor-alpha
  • Zinc Fingers