AIM2 Inflammasome Assembly and Signaling

Wang, Bing; Tian, Yuan; Yin, Qian

doi:10.1007/978-981-13-9367-9_7

Cited by 63 publications

(55 citation statements)

References 37 publications

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“…AIM2 is a member of the ALR family of proteins, characterized by an N-terminal PYD (pyrin) domain and a C-terminal HIN (hematopoietic, interferon-inducible, and nuclear localization) domain. 30 The HIN domain is directly responsible for binding to dsDNA in the cytosol. Structural studies have revealed that the HIN domain is comprised of two OB (oligonucleotide/oligosaccharide binding) folds, which have been shown to bind to both strands of DNA.…”

Section: B I O Chemi C Al and S Truc Tur Al Ba S Is Of Dna S En S Imentioning

confidence: 99%

“…23 The OB folds contain positively charged arginine and lysine residues that associate with the negatively charged phosphates on the ribose backbone of DNA molecules. 30,32 Additionally, minimal polar and hydrophobic interactions between the HIN domain and DNA have also been shown to contribute to AIM2 binding of DNA.…”

Section: B I O Chemi C Al and S Truc Tur Al Ba S Is Of Dna S En S Imentioning

confidence: 99%

“…Interestingly, structural analysis of the HIN domain and DNA interaction has revealed negligible contact of the HIN domain with the bases of DNA, potentially explaining sequence-independent sensing of DNA by AIM2. 30 Furthermore, multiple AIM2 molecules can bind to the same molecule of dsDNA allowing for the clustering of AIM2 molecules to initiate inflammasome formation. 33 The PYD domain of AIM2 is responsible for recruiting the adapter protein ASC during inflammasome assembly.…”

Section: B I O Chemi C Al and S Truc Tur Al Ba S Is Of Dna S En S Imentioning

confidence: 99%

“…34 Structural studies have revealed that the PYD domain contains a six-helix bundle and has a high affinity to associate with other PYD domains. 30,32,35 It was found that the AIM2 PYD domain contains a loop connecting α2 and α3 that is critical for self-association. 36 The PYD domain of AIM2 directly binds to the PYD domain of ASC.…”

Section: B I O Chemi C Al and S Truc Tur Al Ba S Is Of Dna S En S Imentioning

confidence: 99%

“…The interaction between the PYD domains of these two proteins results in the assembly of helical filaments, allowing for oligomerization of the AIM2 inflammasome. 30 In the ASC filaments, AIM2 PYD exists at only one end, while ASC PYD polymerizes to make up the remaining filament structure. 37 It is considered that AIM2 PYD functions as a nucleating platform for ASC PYD molecules to assemble and polymerize into filaments, similar to how actin nucleation factors drive actin polymerization.…”

Section: B I O Chemi C Al and S Truc Tur Al Ba S Is Of Dna S En S Imentioning

confidence: 99%

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AIM2 in health and disease: Inflammasome and beyond

Kumari

Russo

Shivcharan

et al. 2020

Immunological Reviews

157

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Nucleic acid sensing is a critical mechanism by which the immune system monitors for pathogen invasion. A set of germline‐encoded innate immune receptors detect microbial DNA in various compartments of the cell, such as endosomes, the cytosol, and the nucleus. Sensing of microbial DNA through these receptors stimulates, in most cases, interferon regulatory factor‐dependent type I IFN synthesis followed by JAK/STAT‐dependent interferon‐stimulated gene expression. In contrast, the detection of DNA in the cytosol by AIM2 assembles a macromolecular complex called the inflammasome, which unleashes the proteolytic activity of a cysteine protease caspase‐1. Caspase‐1 cleaves and activates the pro‐inflammatory cytokines such as IL‐1β and IL‐18 and a pore‐forming protein, gasdermin D, which triggers pyroptosis, an inflammatory form of cell death. Research over the past decade has revealed that AIM2 plays essential roles not only in host defense against pathogens but also in inflammatory diseases, autoimmunity, and cancer in inflammasome‐dependent and inflammasome‐independent manners. This review discusses the latest advancements in our understanding of AIM2 biology and its functions in health and disease.

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Section: B I O Chemi C Al and S Truc Tur Al Ba S Is Of Dna S En S Imentioning

confidence: 99%

Section: B I O Chemi C Al and S Truc Tur Al Ba S Is Of Dna S En S Imentioning

confidence: 99%

Section: B I O Chemi C Al and S Truc Tur Al Ba S Is Of Dna S En S Imentioning

confidence: 99%

Section: B I O Chemi C Al and S Truc Tur Al Ba S Is Of Dna S En S Imentioning

confidence: 99%

Section: B I O Chemi C Al and S Truc Tur Al Ba S Is Of Dna S En S Imentioning

confidence: 99%

See 3 more Smart Citations

AIM2 in health and disease: Inflammasome and beyond

Kumari

Russo

Shivcharan

et al. 2020

Immunological Reviews

157

View full text Add to dashboard Cite

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Innate Immune Response and Epigenetic Regulation: A Closely Intertwined Tale in Inflammation

Jawale,

Khandibharad,

Singh

2024

Advanced Biology

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Maintenance of delicate homeostasis is very important in various diseases because it ensures appropriate immune surveillance against pathogens and prevents excessive inflammation. In a disturbed homeostatic condition, hyperactivation of immune cells takes place and interplay between these cells triggers a plethora of signaling pathways, releasing various pro‐inflammatory cytokines such as Tumor necrosis factor alpha (TNFα), Interferon‐gamma (IFNƴ), Interleukin‐6 (IL‐6), and Interleukin‐1 beta (IL‐1β), which marks cytokine storm formation. To be precise, dysregulated balance can impede or increase susceptibility to various pathogens. Pathogens have the ability to hijack the host immune system by interfering with the host's chromatin architecture for their survival and replication in the host cell. Cytokines, particularly IL‐6, Interleukin‐17 (IL‐17), and Interleukin‐23 (IL‐23), play a key role in orchestrating innate immune responses and shaping adaptive immunity. Understanding the interplay between immune response and the role of epigenetic modification to maintain immune homeostasis and the structural aspects of IL‐6, IL‐17, and IL‐23 can be illuminating for a novel therapeutic regimen to treat various infectious diseases. In this review, the light is shed on how the orchestration of epigenetic regulation facilitates immune homeostasis.

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Nanomaterials for Disease Treatment by Modulating the Pyroptosis Pathway

Wang

2023

Adv Healthcare Materials

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Pyroptosis differs significantly from apoptosis and cell necrosis as an alternative mode of programmed cell death. Its occurrence is mediated by the gasdermin protein, leading to characteristic outcomes including cell swelling, membrane perforation, and release of cell contents. Research underscores the role of pyroptosis in the etiology and progression of many diseases, making it a focus of research intervention as scientists explore ways to regulate pyroptosis pathways in disease management. Despite numerous reviews detailing the relationship between pyroptosis and disease mechanisms, few delve into recent advancements in nanomaterials as a mechanism for modulating the pyroptosis pathway to mitigate disease effects. Therefore, there is an urgent need to fill this gap and elucidate the path for the use of this promising technology in the field of disease treatment. This review article delves into recent developments in nanomaterials for disease management through pyroptosis modulation, details the mechanisms by which drugs interact with pyroptosis pathways, and highlights the promise that nanomaterial research holds in driving forward disease treatment.

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AIM2 Inflammasome Assembly and Signaling

Cited by 63 publications

References 37 publications

AIM2 in health and disease: Inflammasome and beyond

AIM2 in health and disease: Inflammasome and beyond

Innate Immune Response and Epigenetic Regulation: A Closely Intertwined Tale in Inflammation

Nanomaterials for Disease Treatment by Modulating the Pyroptosis Pathway

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