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OTU takes the chains OUT

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A20 protein, a regulator of inflammation and cell survival, modulates cellular signaling via two apparently opposite enzyme activities. Recent studies elucidate the unusual structural organization of the A20 protease domain and provide new mechanistic insights into its biological function.

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Figure 1: Model of A20 function showing the low catalytic activity of the OTU domain, its high affinity toward polyubiquitin chains and differential chain cleavage.

Katie Ris-Vicari

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Authors and Affiliations

  1. Maxim Y. Balakirev is in the Institut de Recherches en Technologies et Sciences pour le Vivant, CEA, 17 rue des Martyrs, Grenoble 38054, France. balakirev@dsvgre.cea.fr,

    Maxim Y Balakirev

  2. Keith D. Wilkinson is in the Department of Biochemistry, Emory University, 1510 Clifton Road, Atlanta, Georgia 30322, USA. genekdw@emory.edu,

    Keith D Wilkinson

Authors
  1. Maxim Y Balakirev
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  2. Keith D Wilkinson
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Balakirev, M., Wilkinson, K. OTU takes the chains OUT. Nat Chem Biol 4, 227–228 (2008). https://doi.org/10.1038/nchembio0408-227

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  • DOI: https://doi.org/10.1038/nchembio0408-227

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