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METTL3-dependent m6A RNA methylation regulates activation of the NLRP3 inflammasome

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Homo sapiens

PROVIDER: GSE216483 | GEO | 2025/05/28

REPOSITORIES: GEO

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METTL3-dependent m6A RNA methylation regulates activation of the NLRP3 inflammasome [RIP-Seq]

Project description:Inflammasomes are signalling complexes that are activated in response to infection, cellular stress and other cues to initiate an inflammatory response. The NLRP3 (NOD-, LRR- and pyrin domain-containing protein 3) inflammasome is a cytosolic sensor that mediates caspase-1-dependent maturation and release of the pro-inflammatory cytokines IL-1β and IL-18, and Gasdermin D-induced pyroptotic cell death. While a broad range of pathogens can activate the NLRP3 inflammasome, in most cases, it appears to be dispensable to fight infection. In recent work, m6A has emerged as a key regulator of the immune response. However, the specific role played by METTL3 and RNA m6A methylation during inflammasome activation is still unknown. Using genetic manipulation and pharmacological inhibition, we demonstrate that METTL3 is essential for activation of the NLRP3 inflammasome in vitro and in vivo. We show that pharmacological inhibition of METTL3 attenuates NLRP3 hyperactivation in PBMCs isolated from patients affected by Cryopyrin Associated Periodic Syndrome (CAPS).

2025-05-28 | GSE216482 | GEO

METTL3-dependent m6A RNA methylation regulates activation of the NLRP3 inflammasome [RNA-Seq]

2025-05-28 | GSE216441 | GEO

METTL3-dependent m6A RNA methylation regulates activation of the NLRP3 inflammasome

Project description:METTL3-dependent m6A RNA methylation regulates activation of the NLRP3 inflammasome

| PRJNA893677 | ENA

METTL3-dependent m6A RNA methylation regulates activation of the NLRP3 inflammasome [RIP-Seq]

Project description:METTL3-dependent m6A RNA methylation regulates activation of the NLRP3 inflammasome [RIP-Seq]

| PRJNA893686 | ENA

METTL3-dependent m6A RNA methylation regulates activation of the NLRP3 inflammasome [RNA-Seq]

Project description:METTL3-dependent m6A RNA methylation regulates activation of the NLRP3 inflammasome [RNA-Seq]

| PRJNA893624 | ENA

mTORC1-Induced HK1-Dependent Glycolysis Regulates NLRP3 Inflammasome Activation.

Project description:The mammalian target of rapamycin complex 1 (mTORC1) regulates activation of immune cells and cellular energy metabolism. Although glycolysis has been linked to immune functions, the mechanisms by which glycolysis regulates NLRP3 inflammasome activation remain unclear. Here, we demonstrate that mTORC1-induced glycolysis provides an essential mechanism for NLRP3 inflammasome activation. Moreover, we demonstrate that hexokinase 1 (HK1)-dependent glycolysis, under the regulation of mTORC1, represents a critical metabolic pathway for NLRP3 inflammasome activation. Downregulation of glycolysis by inhibition of Raptor/mTORC1 or HK1 suppressed both pro-IL-1β maturation and caspase-1 activation in macrophages in response to LPS and ATP. These results suggest that upregulation of HK1-dependent glycolysis by mTORC1 regulates NLRP3 inflammasome activation.

| S-EPMC4858438 | biostudies-literature

METTL3 mediated m6A mRNA methylation regulates neutrophil activation through targeting TLR4 signaling

Project description:This SuperSeries is composed of the SubSeries listed below.

2023-03-31 | GSE225143 | GEO

Mettl3-mediated mRNA m6A methylation promotes dendritic cell activation

Project description:This SuperSeries is composed of the SubSeries listed below.

2019-04-02 | GSE108333 | GEO

MARK4 regulates NLRP3 positioning and inflammasome activation through a microtubule-dependent mechanism.

Project description:Excessive activation of the NLR family pyrin domain containing 3 (NLRP3) inflammasome is involved in many chronic inflammatory diseases, including cardiovascular and Alzheimer's disease. Here we show that microtubule-affinity regulating kinase 4 (MARK4) binds to NLRP3 and drives it to the microtubule-organizing centre, enabling the formation of one large inflammasome speck complex within a single cell. MARK4 knockdown or knockout, or disruption of MARK4-NLRP3 interaction, impairs NLRP3 spatial arrangement and limits inflammasome activation. Our results demonstrate how an evolutionarily conserved protein involved in the regulation of microtubule dynamics orchestrates NLRP3 inflammasome activation by controlling its transport to optimal activation sites, and identify a targetable function for MARK4 in the control of innate immunity.

| S-EPMC5493753 | biostudies-literature

Inhibition of METTL3 Alleviates NLRP3 Inflammasome Activation via Increasing Ubiquitination of NEK7.

Project description:N6-methyladenosine (m6A) modification, installed by METTL3-METTL14 complex, is abundant and critical in eukaryotic mRNA. However, its role in oral mucosal immunity remains ambiguous. Periodontitis is a special but prevalent infectious disease characterized as hyperinflammation of oral mucosa and bone resorption. Here, it is reported that genetic deletion of Mettl3 alleviates periodontal destruction via suppressing NLRP3 inflammasome activation. Mechanistically, the stability of TNFAIP3 (also known as A20) transcript is significantly attenuated upon m6A modification. When silencing METTL3, accumulated TNFAIP3 functioning as a ubiquitin-editing enzyme facilitates the ubiquitination of NEK7 [NIMA (never in mitosis gene a)-related kinase 7], and subsequently impairs NLRP3 inflammasome assembly. Furtherly, Coptisine chloride, a natural small-molecule, is discovered as a novel METTL3 inhibitor and performs therapeutic effect on periodontitis. The study unveils a previously unknown pathogenic mechanism of METTL3-mediated m6A modifications in periodontitis and indicates METTL3 as a potential therapeutic target.

| S-EPMC11234428 | biostudies-literature

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