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  NLRP3 inflammasome assembly is regulated by phosphorylation of the pyrin domain

Stutz, A., Kolbe, C., Stahl, R., Franklin, B. S., van Ray, O., Brinkschulte, R., et al. (2017). NLRP3 inflammasome assembly is regulated by phosphorylation of the pyrin domain. Journal of Experimental Medicine, 214(6), 1725-1736. doi:10.1084/jem.20160933.

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Datensatz-Permalink: https://hdl.handle.net/11858/00-001M-0000-002D-DE79-0 Versions-Permalink: https://hdl.handle.net/11858/00-001M-0000-002D-DE7A-E
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© 2017 Stutz et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).
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 Urheber:
Stutz, A., Autor
Kolbe, C.C., Autor
Stahl, R., Autor
Franklin, B. S., Autor
van Ray, O., Autor
Brinkschulte, R., Autor
Geyer, Matthias, Autor
Meissner, Felix1, Autor           
Latz, E., Autor
Affiliations:
1Meissner, Felix / Experimental Systems Immunology, Max Planck Institute of Biochemistry, Max Planck Society, ou_2149678              

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 Zusammenfassung: NLRP3 is a cytosolic pattern recognition receptor that senses microbes and endogenous danger signals. Upon activation, NLRP3 forms an inflammasome with the adapter ASC, resulting in caspase-1 activation, release of proinflammatory cytokines and cell death. How NLRP3 activation is regulated by transcriptional and posttranslational mechanisms to prevent aberrant activation remains incompletely understood. Here, we identify three conserved phosphorylation sites in NLRP3 and demonstrate that NLRP3 activation is controlled by phosphorylation of its pyrin domain (PYD). Phosphomimetic residues in NLRP3 PYD abrogate inflammasome activation and structural modeling indicates that phosphorylation of the PYD regulates charge–charge interaction between two PYDs that are essential for NLRP3 activation. Phosphatase 2A (PP2A) inhibition or knock-down drastically reduces NLRP3 activation, showing that PP2A can license inflammasome assembly via dephosphorylating NLRP3 PYD. These results propose that the balance between kinases and phosphatases acting on the NLRP3 PYD is critical for NLRP3 activation.

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 Datum: 2017-05-022017-06
 Publikationsstatus: Erschienen
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 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1084/jem.20160933
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Titel: Journal of Experimental Medicine
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Baltimore, Md. : Rockefeller Institute for Medical Research
Seiten: - Band / Heft: 214 (6) Artikelnummer: - Start- / Endseite: 1725 - 1736 Identifikator: ISSN: 0022-1007
CoNE: https://pure.mpg.de/cone/journals/resource/954925413886