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Ed. by Lopez-Castejón, Gloria

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Regulation of NLRP3 activation by the ubiquitin system

Gloria López-Castejón
  • Manchester Collaborative Centre for Inflammation Research (MCCIR), Faculty of Life Sciences, The University of Manchester, Manchester (UK)
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2013-11-29 | DOI: https://doi.org/10.2478/infl-2013-0003


Inflammasomes, molecular complexes activated in response to pathogens or injury, are involved in the activation and release of the proinflammatory cytokine interleukin-1β. Inflammasome activation is tightly controlled and its dysregulation is associated with the development of inflammatory disorders. Ubiquitination, the conjugation of ubiquitin to a protein, is a post-translational protein modification essential for a wide variety of cellular processes. What was initially considered to be just a signal for protein degradation has become a major regulator for signalling pathways that is also involved in the regulation of NLRP3 inflammasome activation. Similarly to the inflammasome, dysregulation of ubiquitin signalling is associated with the initiation and development of pathologies including immune disorders such as arthritis or lupus erythematous, highlighting the relevance of these systems in the inflammatory processes. How the ubiquitin system regulates the NLRP3 inflammasome is discussed here

Keywords: Inflammasome; Interleukin-1β; NLRP3; ubiquitin; inflammation


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About the article

Received: 2013-08-30

Accepted: 2013-10-02

Published Online: 2013-11-29

Published in Print: 2014-01-01

Citation Information: Inflammasome, ISSN (Online) 2300-102X, DOI: https://doi.org/10.2478/infl-2013-0003.

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©2013 Gloria López-Castejón. This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License. BY-NC-ND 3.0

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