Claudia Gottier
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Claudia Gottier has a total of 19 co-authors. Here are the top co-authors by number of shared publications:
Andrew C. Chan
Department of Immunology, Genentech, South San Francisco, California, USA
1 shared publication- Burkhard Becher
Institute of Experimental Immunology, University of Zurich, Zurich, Switzerland
1 shared publication David J. Rawlings
Seattle Children’s Research Institute, Division of Immunology, Seattle, Washington, USA
1 shared publication- Emmanuel Contassot
Department of Biomedicine University Hospital and University of Basel Basel Switzerland
1 shared publication - Florian Mair
Flow Cytometry Core Facility, ETH Zürich, Zürich, Switzerland
1 shared publication - Gerhard Rogler
Department of Gastroenterology and Hepatology, University Hospital Zurich, University of Zurich , Zurich
1 shared publication
Latest Publications
- Open Access
- 4 April 2016
- Published by American Society for Clinical Investigation in Journal of Clinical Investigation
- Vol. 126 (5) , 1783-1800
NLRP3 tyrosine phosphorylation is controlled by protein tyrosine phosphatase PTPN22
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.
- 4 April 2016
- Published by American Society for Clinical Investigation in Journal of Clinical Investigation
- Vol. 126 (5) , 1783-1800
Open AccessNLRP3 tyrosine phosphorylation is controlled by protein tyrosine phosphatase PTPN22
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.