Isolation and characterization of two novel A20-like proteins

• Published in: Biochemical journal Vol. 357; no. Pt 3; pp. 617 - 623
• Main Authors: Evans, P C, Taylor, E R, Coadwell, J, Heyninck, K, Beyaert, R, Kilshaw, P J
• Format: Journal Article
• Language: English
• Published: England 01.08.2001
• Subjects: Amino Acid Sequence; Animals; Cells, Cultured; Cloning, Molecular; Cysteine Endopeptidases; DNA-Binding Proteins; Endopeptidases - genetics; Endopeptidases - isolation & purification; Endopeptidases - metabolism; Gene Expression Regulation; Humans; Intracellular Signaling Peptides and Proteins; Mice; Molecular Sequence Data; NF-kappa B - metabolism; Nuclear Proteins; Proteins - genetics; Proteins - isolation & purification; Proteins - metabolism; Sequence Homology, Amino Acid; Subcellular Fractions; TNF Receptor-Associated Factor 6; Transcription, Genetic; Tumor Necrosis Factor alpha-Induced Protein 3
• ISSN: 0264-6021; 1470-8728
• DOI: 10.1042/0264-6021:3570617

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.