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Corrigendum Open Access | 10.1172/JCI169304

NLRP3 tyrosine phosphorylation is controlled by protein tyrosine phosphatase PTPN22

Marianne R. Spalinger, Stephanie Kasper, Claudia Gottier, Silvia Lang, Kirstin Atrott, Stephan R. Vavricka, Sylvie Scharl, Petrus M. Gutte, Markus G. Grütter, Hans-Dietmar Beer, Emmanuel Contassot, Andrew C. Chan, Xuezhi Dai, David J. Rawlings, Florian Mair, Burkhard Becher, Werner Falk, Michael Fried, Gerhard Rogler, and Michael Scharl

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Published February 15, 2023 - More info

Published in Volume 133, Issue 4 on February 15, 2023
J Clin Invest. 2023;133(4):e169304. https://doi.org/10.1172/JCI169304.
© 2023 Spalinger et al. This work is licensed under the Creative Commons Attribution 4.0 International License. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
Published February 15, 2023 - Version history
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Related article:

NLRP3 tyrosine phosphorylation is controlled by protein tyrosine phosphatase PTPN22
Marianne R. Spalinger, … , Gerhard Rogler, Michael Scharl
Marianne R. Spalinger, … , Gerhard Rogler, Michael Scharl
Research Article Gastroenterology Immunology

NLRP3 tyrosine phosphorylation is controlled by protein tyrosine phosphatase PTPN22

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Abstract

Inflammasomes form as the result of the intracellular presence of danger-associated molecular patterns and mediate the release of active IL-1β, which influences a variety of inflammatory responses. Excessive inflammasome activation results in severe inflammatory conditions, but physiological IL-1β secretion is necessary for intestinal homeostasis. Here, we have described a mechanism of NLRP3 inflammasome regulation by tyrosine phosphorylation of NLRP3 at Tyr861. We demonstrated that protein tyrosine phosphatase non-receptor 22 (PTPN22), variants in which are associated with chronic inflammatory disorders, dephosphorylates NLRP3 upon inflammasome induction, allowing efficient NLRP3 activation and subsequent IL-1β release. In murine models, PTPN22 deficiency resulted in pronounced colitis, increased NLRP3 phosphorylation, but reduced levels of mature IL-1β. Conversely, patients with inflammatory bowel disease (IBD) that carried an autoimmunity-associated PTPN22 variant had increased IL-1β levels. Together, our results identify tyrosine phosphorylation as an important regulatory mechanism for NLRP3 that prevents aberrant inflammasome activation.

Authors

Marianne R. Spalinger, Stephanie Kasper, Claudia Gottier, Silvia Lang, Kirstin Atrott, Stephan R. Vavricka, Sylvie Scharl, Petrus M. Gutte, Markus G. Grütter, Hans-Dietmar Beer, Emmanuel Contassot, Andrew C. Chan, Xuezhi Dai, David J. Rawlings, Florian Mair, Burkhard Becher, Werner Falk, Michael Fried, Gerhard Rogler, Michael Scharl

×

Original citation: J Clin Invest. 2016;126(5):1783–1800. https://doi.org/10.1172/JCI83669

Citation for this corrigendum: J Clin Invest. 2023;133(4):e169304. https://doi.org/10.1172/JCI169304

The authors recently became aware of errors in Figure 8, A and B. In Figure 8A, the WT/H2O and WT/DSS pictures were inadvertently switched. In Figure 8B, the incorrect image was shown for the Ptpn22–/–/DSS sample. The correct figure is shown below.

The authors regret the errors.

Footnotes

See the related article at NLRP3 tyrosine phosphorylation is controlled by protein tyrosine phosphatase N22.

Version history
  • Version 1 (February 15, 2023): Electronic publication

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