The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
NLRP3 inflammasome assembly is regulated by phosphorylation of the pyrin domain
Open accessAbstract
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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Self-citationActivation and regulation of the inflammasomes
Latz, E., Xiao, T. S., & Stutz, A. (2013) · Nature Reviews Immunology · doi:10.1038/nri3452 · Cited by 2,884
Self-citationAIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
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Self-citationInflammasomes in health and disease
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Bile Acids Control Inflammation and Metabolic Disorder through Inhibition of NLRP3 Inflammasome
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“Furthermore, in situations in which PKA is triggered, NLRP3 can be phosphorylated at position 295, leading to its inhibition (Guo et al., 2016; Mortimer et al., 2016).”
BackgroundMishra, B. B., Rathinam, V. A. K., Martens, G. W., Martinot, A. J., Kornfeld, H., Fitzgerald, K. A., & Sassetti, C. M. (2013) · Nature Immunology · doi:10.1038/ni.2474 · Cited by 571
Cited by
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The NLRP3 Inflammasome: an overview of mechanisms of activation and regulation
Kelley, N., Jeltema, D., Duan, Y., & He, Y. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20133328 · Cited by 3,539
Targeting the NLRP3 inflammasome in inflammatory diseases
Mangan, M. S. J., Olhava, E. J., Roush, W. R., Seidel, H. M., Glick, G. D., & Latz, E. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.97 · Cited by 1,885
Self-citationFundamental Mechanisms of Regulated Cell Death and Implications for Heart Disease
Del Re, D. P., Amgalan, D., Linkermann, A., Liu, Q., & Kitsis, R. N. (2019) · Physiological Reviews · doi:10.1152/physrev.00022.2018 · Cited by 961
NLRP3 Inflammasome and the IL-1 Pathway in Atherosclerosis
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Metadata
- Authors
- Stutz, A., Kolbe, C.-C., Stahl, R., Horvath, G. L., Franklin, B. S., van Ray, O., Brinkschulte, R., Geyer, M., Meissner, F., & Latz, E.
- Venue
- Journal of Experimental Medicine
- Publisher
- Rockefeller University Press
- Published
- 2017-05-02
- Volume
- 214
- Issue
- 6
- Pages
- 1725-1736
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- OpenAlex
- W2611482243
- Cited by
- 317
- References
- 9
- FWCI
- 11.55
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Stutz, A., Kolbe, C.-C., Stahl, R., Horvath, G. L., Franklin, B. S., van Ray, O., Brinkschulte, R., Geyer, M., Meissner, F., & Latz, E. (2017). NLRP3 inflammasome assembly is regulated by phosphorylation of the pyrin domain. Journal of Experimental Medicine. https://doi.org/10.1084/jem.20160933
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