COPs and POPs: modulators of inflammasome activity
Open accessAbstract
Inflammasomes represent molecular platforms for the activation of inflammatory caspases and are essential for processing and secretion of the inflammatory cytokines IL-1beta and IL-18. Multiple key proteins of inflammasomes contain caspase recruitment domains (CARDs) or pyrin domains (PYDs). Dissecting CARD- and PYD-mediated interactions substantially improved our understanding of the mechanisms by which these protein platforms are activated and emphasized their essential role during the inflammatory cytokine response. However, their precise regulation is still poorly understood. A family of small proteins that are composed of either a CARD or a PYD only emerged as important inflammasome regulators. These CARD-only proteins (COPs) and PYD-only proteins (POPs) function as endogenous dominant negative proteins that modulate the activity of inflammasomes in response to pathogen infection and tissue destruction. In this review we will summarize the most recent advances in the regulation of inflammasomes and highlight their importance for immunity and inflammatory disease.
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Caspase recruitment domain-only proteins (COPs), such as Iceberg, Pseudo-ICE, and caspase-12, and pyrin domain-only proteins (POPs), such as pyrin, POP1, and POP2, are thought to inhibit inflammasome activity by blocking inflammasome assembly and subsequent caspase-1 cleavage.
“Caspase recruitment domain–only proteins (COPs), such as Iceberg, Pseudo-ICE, and caspase-12, and pyrin domain–only proteins (POPs), such as pyrin, POP1, and POP2, are thought to inhibit inflammasome activity by blocking inflammasome assembly and subsequent caspase-1 cleavage (16,39).”
From Sustained Inflammasome Activity in Macrophages Impairs Wound Healing in Type 2 Diabetic Humans and Mice (2014) · cites this paper as [39]
Humans express a broad array of COPs and POPs, whereas rodents only express a limited subset.
“Interestingly, humans express a broad array of COPs and POPs, whereas rodents only express a limited subset (16,39).”
From Sustained Inflammasome Activity in Macrophages Impairs Wound Healing in Type 2 Diabetic Humans and Mice (2014) · cites this paper as [39]
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References 77 · Cited by 130
- Authors
- Stehlik, C., & Dorfleutner, A.
- Affiliations
- Northwestern University (US)
- Venue
- The Journal of Immunology
- Publisher
- Oxford University Press (OUP)
- Published
- 2007-12
- Volume
- 179
- Issue
- 12
- Pages
- 7993-7998
- ISSN
- 0022-1767 (ISSN-L)
- 1550-6606
- PMC
- PMC2645488
- OpenAlex
- W2170089416
- Cited by
- 130
- References
- 77
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 2 · 2023: 2 · 2022: 5 · 2021: 3 · 2020: 6 · 2019: 7 · 2018: 4 · 2017: 11 · 2016: 4 · 2015: 9 · 2014: 6 · 2013: 17 · 2012: 10
- FWCI
- 0.72
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Immunology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Concern Foundation
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM071723)
- National Institute of Allergy and Infectious Diseases (R21AI067680, R03AI067806)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Immunology and Microbiology › Immunology › IL-33, ST2, and ILC Pathways
- Keywords
- inflammasome, caspase recruitment domain, pyrin domain, dominant negative regulation, IL-1β, IL-18, caspase activation, inflammatory cytokines, inflammasome regulation, innate immunity, inflammatory diseases
- MeSH terms
- Pyrin, Animals, Cytoskeletal Proteins, Humans, Inflammation, Protein Precursors, Proteins, Protein Structure, Tertiary, Caspases, Interleukin-18, Mice, Interleukin-1beta
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