Isolation and characterization of two novel A20-like proteins

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Abstract

The transcription factor nuclear factor κB (NF-κB) plays a pivotal role in inflammatory processes through induction of adhesion molecules and chemokines. The zinc finger molecule A20 is an important negative regulator of NF-κB. The mechanism utilized by A20 is not fully understood, but A20 has been shown to bind to tumour-necrosis-factor-receptor-associated factor (TRAF) molecules, which are necessary for pro-inflammatory cytokine signalling. We report two novel genes, Cezanne (cellular zinc finger anti-NF-κB) and TRABID (TRAF-binding domain), with sequence similarity to A20. Co-immunoprecipitation studies indicated that TRAF6 was able to interact with both Cezanne and TRABID. In contrast, reporter gene experiments revealed a specific ability of Cezanne to down-regulate NF-κB. It is likely, therefore, that Cezanne participates in the regulation of inflammatory processes.

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Evans, P. C., Taylor, E. R., Coadwell, J., Heyninck, K., Beyaert, R., & Kilshaw, P. J. (2001). Isolation and characterization of two novel A20-like proteins. Biochemical Journal, 357(3), 617–623. https://doi.org/10.1042/0264-6021:3570617

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