Cited by 3,080Inflammasome and immune disordersImmune Response and InflammationAutoimmune and Inflammatory Disorders Research

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Cryopyrin activates the inflammasome in response to toxins and ATP

Mariathasan, Sanjeev, Weiss, David S., Newton, Kim, McBride, Jacqueline, O'Rourke, Karen, Roose-Girma, Meron, Lee, Wyne P., Weinrauch, Yvette, Monack, Denise M., Dixit, Vishva M.·2006·Nature

DOI 10.1038/nature04515

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Abstract

A crucial part of the innate immune response is the assembly of the inflammasome, a cytosolic complex of proteins that activates caspase-1 to process the proinflammatory cytokines interleukin (IL)-1beta and IL-18. The adaptor protein ASC is essential for inflammasome function, binding directly to caspase-1 (refs 3, 4), but the triggers of this interaction are less clear. ASC also interacts with the adaptor cryopyrin (also known as NALP3 or CIAS1). Activating mutations in cryopyrin are associated with familial cold autoinflammatory syndrome, Muckle-Wells syndrome and neonatal onset multisystem inflammatory disease, diseases that are characterized by excessive production of IL-1beta. Here we show that cryopyrin-deficient macrophages cannot activate caspase-1 in response to Toll-like receptor agonists plus ATP, the latter activating the P2X7 receptor to decrease intracellular K+ levels. The release of IL-1beta in response to nigericin, a potassium ionophore, and maitotoxin, a potent marine toxin, was also found to be dependent on cryopyrin. In contrast to Asc-/- macrophages, cells deficient in the gene encoding cryopyrin (Cias1-/-) activated caspase-1 and secreted normal levels of IL-1beta and IL-18 when infected with Gram-negative Salmonella typhimurium or Francisella tularensis. Macrophages exposed to Gram-positive Staphylococcus aureus or Listeria monocytogenes, however, required both ASC and cryopyrin to activate caspase-1 and secrete IL-1beta. Therefore, cryopyrin is essential for inflammasome activation in response to signalling pathways triggered specifically by ATP, nigericin, maitotoxin, S. aureus or L. monocytogenes.

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Authors: Mariathasan, S., Weiss, D. S., Newton, K., McBride, J., O'Rourke, K., Roose-Girma, M., Lee, W. P., Weinrauch, Y., Monack, D. M., & Dixit, V. M.
Affiliations: Genentech (US)
Stanford Medicine (US)
New York University (US)
Corresponding author: Dixit, Vishva M.
ORCID: Mariathasan, Sanjeev
Weiss, David S.
Newton, Kim
McBride, Jacqueline
Roose-Girma, Meron
Lee, Wyne P.
Monack, Denise M.
Dixit, Vishva M.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2006-01-11
Volume: 440
Issue: 7081
Pages: 228-232
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature04515
OpenAlex: W2090859543
Cited by: 3,080
References: 26
Citations by year: 2026: 90 · 2025: 101 · 2024: 129 · 2023: 121 · 2022: 150 · 2021: 152 · 2020: 160 · 2019: 161 · 2018: 155 · 2017: 164 · 2016: 184 · 2015: 179 · 2014: 180 · 2013: 189 · 2012: 173
FWCI: 62.33
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Funders: National Institutes of Health
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Health Sciences › Medicine › Hematology › Autoimmune and Inflammatory Disorders Research
Keywords: NLRP3, inflammasome, caspase-1, IL-1β, IL-18, ATP, P2X7 receptor, bacterial toxins, maitotoxin, nigericin, bacterial RNA, R837, R848, urate crystals, autoinflammatory disease, innate immunity
MeSH terms: NLR Family, Pyrin Domain-Containing 3 Protein, Polyether Toxins, Adenosine Triphosphate, Animals, Carrier Proteins, Cytoskeletal Proteins, Enzyme Activation, Inflammation, Interleukin-1, Listeria monocytogenes, Macrophages, Marine Toxins, Nigericin, Staphylococcus aureus, Toxins, Biological, Signal Transduction, NF-kappa B, Caspase 1, Oxocins, Multiprotein Complexes, Intracellular Signaling Peptides and Proteins, Extracellular Signal-Regulated MAP Kinases, Apoptosis Regulatory Proteins, Toll-Like Receptors, Mice, CARD Signaling Adaptor Proteins, Nod2 Signaling Adaptor Protein

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