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Cited by 226

The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.

NLRP3 tyrosine phosphorylation is controlled by protein tyrosine phosphatase PTPN22

Open access
Spalinger, Marianne R., Kasper, Stephanie, Gottier, Claudia, Lang, Silvia, Atrott, Kirstin, Vavricka, Stephan R., Scharl, Sylvie, Gutte, Petrus M., Grütter, Markus G., Beer, Hans-Dietmar, Contassot, Emmanuel, Chan, Andrew C., Dai, Xuezhi, Rawlings, David J., Mair, Florian, Becher, Burkhard, Falk, Werner, Fried, Michael, Rogler, Gerhard, Scharl, Michael·2016·Journal of Clinical Investigation

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.

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Metadata

Authors
Spalinger, M. R., Kasper, S., Gottier, C., Lang, S., Atrott, K., Vavricka, S. R., Scharl, S., Gutte, P. M., Grütter, M. G., Beer, H.-D., Contassot, E., Chan, A. C., Dai, X., Rawlings, D. J., Mair, F., Becher, B., Falk, W., Fried, M., Rogler, G., & Scharl, M.
Venue
Journal of Clinical Investigation
Published
2016-04-04
Volume
126
Issue
5
Pages
1783-1800
ISSN
  • 0021-9738 (ISSN-L)
  • 1558-8238
OpenAlex
W2320348279
Cited by
226
References
9
FWCI
11.29
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: NLRP3 tyrosine phosphorylation is controlled by protein tyrosine phosphatase PTPN22. https://app.cochat.ai/papers/10.1172/jci83669
The paper
Spalinger, M. R., Kasper, S., Gottier, C., Lang, S., Atrott, K., Vavricka, S. R., Scharl, S., Gutte, P. M., Grütter, M. G., Beer, H.-D., Contassot, E., Chan, A. C., Dai, X., Rawlings, D. J., Mair, F., Becher, B., Falk, W., Fried, M., Rogler, G., & Scharl, M. (2016). NLRP3 tyrosine phosphorylation is controlled by protein tyrosine phosphatase PTPN22. Journal of Clinical Investigation. https://doi.org/10.1172/jci83669

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.