A20: attractive without showing cleavage. (30th May 2014)

• Record Type: Journal Article
• Authors: Verhelst, Kelly; van Loo, Geert; Beyaert, Rudi
• Is Part Of: EMBO reports. Volume 15:Number 7(2014:Jul.)
• Page Start: 734
• Page End: 735
• Publication Date: 2014-05-30
• Subjects: Molecular biology -- Periodicals; Molecular Biology -- Periodicals; Molecular biology; Periodicals; 572.8
• DOI: 10.15252/embr.201439014
• Languages: English
• ISSNs: 1469-221X

Abstract

<abstract abstract-type="main" id="embr201439014-abs-0001"> <title> <x xml:space="preserve">Abstract</x> </title> <p content-type="executiveSummary">A20 (also known as TNFAIP3) is a deubiquitinating enzyme (DUB) that ensures optimal immune responses in cells stimulated by cytokines, such as TNF and IL‐1, or pathogen components, such as lipopolysaccharide. Deletion of <italic>A20</italic> in mice results in multi‐organ inflammation and death within 2 weeks <xref ref-type="link" rid="embr201439014-bib-0001">1</xref>. The anti‐inflammatory functions of A20 have been attributed to its ability to negatively regulate NF‐κB signaling <xref ref-type="link" rid="embr201439014-bib-0002">2</xref>. The picture that has emerged over the last decade is that A20 attenuates NF‐κB signaling by removing polyubiquitin chains from specific NF‐κB signaling proteins. A study published in this issue of <italic>EMBO reports</italic> by Sankar Ghosh and colleagues <xref ref-type="link" rid="embr201439014-bib-0003">3</xref> now shows that A20 knockin mice expressing a catalytically inactive A20 mutant that can no longer remove ubiquitin are normal and do not have an inflammatory phenotype. These results challenge the notion that A20 exerts its NF‐κB inhibitory and anti‐inflammatory function by acting as a DUB.</p> </abstract>