| Título: | Identification of a cell protein (FIP-3) as a modulator of NF-κB activity and as a target of an adenovirus inhibitor of tumor necrosis factor α-induced apoptosis |
| Autores: |
Li, Yongan Kang, Jian Friedman, Joshua Tarassishin, Leonid Ye, Jianjiang Kovalenko, Andrei Wallach, David Horwitz, Marshall S. |
| Fecha: | 1999-02-02 |
| Publicador: | The National Academy of Sciences |
| Fuente: |
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| Tipo: | Text |
| Tema: | Biological Sciences |
| Descripción: | 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)-α-induced cytolysis. FIP-3, which contains leucine zippers and a zinc finger domain, inhibits both basal and induced transcriptional activity of NF-κB 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-α-induced NF-κB activation. In addition, FIP-3 inhibited activation of NF-κB induced by TNF-α, the TNFR-1 receptor, RIP, NIK, and IKKβ, as well as basal levels of endogenous NF-κB in 293 cells. Because the activation of NF-κB has been shown to inhibit apoptosis, FIP-3 appears both to activate a cell-death pathway and to inhibit an NF-κB-dependent survival mechanism. |
| Idioma: | en |