Two distinct ubiquitin-binding motifs in A20 mediate its anti-inflammatory and cell-protective activities
Author:
Funder
Universiteit Gent
Stichting Tegen Kanker
Fonds Wetenschappelijk Onderzoek
Publisher
Springer Science and Business Media LLC
Subject
Immunology,Immunology and Allergy
Link
http://www.nature.com/articles/s41590-020-0621-9.pdf
Reference30 articles.
1. Catrysse, L., Vereecke, L., Beyaert, R. & van Loo, G. A20 in inflammation and autoimmunity. Trends Immunol. 35, 22–31 (2014).
2. Martens, A. & van Loo, G. A20 at the crossroads of cell death, inflammation, and autoimmunity. Cold Spring Harb. Perspect. Biol. 12, a036418 (2020).
3. Wertz, I. E. et al. De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling. Nature 430, 694–699 (2004).
4. Lu, T. T. et al. Dimerization and ubiquitin mediated recruitment of A20, a complex deubiquitinating enzyme. Immunity 38, 896–905 (2013).
5. De, A., Dainichi, T., Rathinam, C. V. & Ghosh, S. The deubiquitinase activity of A20 is dispensable for NF-κB signaling. EMBO Rep. 15, 775–783 (2014).
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