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Portland Press, Biochemical Journal, 3(357), p. 617-623, 2001

DOI: 10.1042/bj3570617

Portland Press, Biochemical Journal, 3(357), p. 617

DOI: 10.1042/0264-6021:3570617

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Isolation and characterization of two novel A20-like proteins.

Journal article published in 2001 by Pc C. Evans ORCID, Er R. Taylor, John Coadwell, Karen Heyninck, Rudi Beyaert ORCID, Pj J. Kilshaw
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

The transcription factor nuclear factor kappa B (NF-kappa B) 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-kappa B. 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-kappa B) 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-kappa B. It is likely, therefore, that Cezanne participates in the regulation of inflammatory processes.