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A20 attenuate oxidized self-DNA mediated inflammasome activation through promoting NEK7 ubiquitination in AKI

ABSTRACT: A20 attenuate oxidized self-DNA mediated inflammasome activation through promoting NEK7 ubiquitination in AKI

PROVIDER: PRJNA907366 | ENA |

REPOSITORIES: ENA

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A20 attenuate oxidized self-DNA mediated inflammasome activation in AKI [AA-DNA]

Project description:A20 attenuate oxidized self-DNA mediated inflammasome activation in AKI [AA-DNA]

| PRJNA907368 | ENA

A20 attenuate oxidized self-DNA mediated inflammasome activation through promoting NEK7 ubiquitination in AKI [ox-dsDNA90]

Project description:A20 attenuate oxidized self-DNA mediated inflammasome activation through promoting NEK7 ubiquitination in AKI [ox-dsDNA90]

| PRJNA907369 | ENA

A20 attenuate oxidized self-DNA mediated inflammasome activation through promoting NEK7 ubiquitination in AKI

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

2022-12-20 | GSE219189 | GEO

A20 attenuate oxidized self-DNA mediated inflammasome activation through promoting NEK7 ubiquitination in AKI [ox-dsDNA90]

Project description:To seek out the target of restricting the exaggerated inflammation results from ox-dsDNA90, we treated BMDMs with ox-dsDNA90 from kidney of acute kidney injury mice model. We then performed gene expression profiling analysis using data obtained from RNA-seq of 2 different groups of BMDMs.

2022-12-20 | GSE219188 | GEO

A20 attenuate oxidized self-DNA mediated inflammasome activation in AKI [AA-DNA]

Project description:To seek out the target of restricting the exaggerated inflammation results from ox-self-DNA, we treated BMDMs with self-dsDNA from kidney of acute kidney injury mice model. We then performed gene expression profiling analysis using data obtained from RNA-seq of 2 different groups of BMDMs.

2022-12-20 | GSE219187 | GEO

Inhibition of NLRP3 Inflammasome Activation by A20 through Modulation of NEK7

Project description:The NLRP3 inflammasome, a pivotal component of innate immunity, has been implicated in various inflammatory disorders. The ubiquitin-editing enzyme A20 is well known to regulate inflammation and maintain homeostasis. However, the precise molecular mechanisms by which A20 modulates the NLRP3 inflammasome remain poorly understood. Here our study revealed that macrophages deficient in A20 exhibit increased protein abundance and elevated mRNA level of NIMA-related kinase 7 (NEK7). Importantly, A20 directly binds with NEK7, mediating its K48-linked ubiquitination, thereby targeting NEK7 for proteasomal degradation. Our results demonstrate that A20 enhance the ubiquitination of NEK7 at K189 and K293 ubiquitinated sites, with K189 playing a crucial role in the binding of NEK7 to A20, albeit not significantly influencing the interaction between NEK7 and NLRP3. Furthermore, A20 disrupts the association of NEK7 with the NLRP3 complex, potentially through the OTU domain and/or synergistic effect of ZnF4 and ZnF7 motifs. Significantly, NEK7 deletion markedly attenuates the activation of the NLRP3 inflammasome in A20-deficient conditions, both in vitro and in vivo. This study uncovers a new mechanism by which A20 inhibits the NLRP3 inflammasome.

2024-07-03 | GSE253265 | GEO

The contribution of RNA oxidation to acute kidney injury: evidence from ISG20-mediated oxidized RNA degradation

Project description:RNA is more vulnerable to oxidation than other cellular components, which is linked to a range of diseases and pathological conditions, such as AKI. To identify the contribution of RNA oxidation to AKI, the mechanisms of how cells handle oxidized RNA should be elucidated. By RNA sequencing analysis in ischemia/reperfusion-induced AKI, we observed the significant changes of genes important in degradingting oxidative RNA.

2023-03-03 | GSE226275 | GEO

Oxidized thioredoxin-1 restrains the NLRP1 inflammasome.

Project description:Oxidized thioredoxin-1 restrains the NLRP1 inflammasome.

| PRJNA888111 | ENA

Oxidized thioredoxin-1 restrains the NLRP1 inflammasome [mBMDM]

Project description:The danger signals that activate the NLRP1 inflammasome have yet to be firmly established. NLRP1 undergoes autoproteolysis to generate N-terminal (NT) and C-terminal (CT) fragment, which importantly, is a necessary step for its check-point regulation by the DPP9 ternary complex and the mechanistic activation of NLRP1 through functional degradation. Here, we report an added layer of regulatory complexity to NLRP1 activity, in the form of a repressive interaction that NLRP1 forms with the oxidized, but not reduced, form of thioredoxin-1 (TRX1). Loss of TRX1 destabilizes the NT fragment of NLRP1 and promotes enhanced inflammasome activation. The TRX1 interaction occurs through the NACHT-LRR of NLRP1 and requires nucleotide binding in its ATPase domain. In addition, we found that several patient-derived and ATPase-inactivating mutations in the NACHT-LRR region hyperactive the inflammasome by destabilize protein folding and are also shown to abrogate TRX1 binding. Thus, NLRP1 appears to detect intracellular reductive stress through a decrease in the fraction of intracellular oxidized TRX1, which enhances protein disorder, leading to inflammasome signaling. These findings link the cellular redox environment to NLRP1-mediated innate immunity.

2022-11-04 | GSE215035 | GEO

Mouse WT vs. A20 KO BMDM differential proteomics

Project description:A20 is a negative regulator of NF-κB signaling, crucial to control inflammatory responses and ensure tissue homeostasis. A20 is thought to restrict NF-κB activation both by its ubiquitin-editing activity as by non-enzymatic activities. Besides its role in NF-κB signaling, A20 also acts as a protective factor inhibiting apoptosis and necroptosis. Because of the ability of A20 to both ubiquitinate and deubiquitinate substrates and its involvement in many cellular processes, we hypothesized that deletion of A20 might generally impact on protein levels, thereby disrupting cellular processes. We performed a differential proteomics study of bone marrow derived macrophages (BMDMs) from control and myeloid-specific A20 knockout mice, both in untreated conditions and after LPS and TNF treatment, and demonstrate proteome-wide changes in protein expression upon A20 deletion. Several inflammatory proteins are up-regulated in the absence of A20, even without an inflammatory stimulus. Depending on the treatment and the time, more proteins are regulated. Together these changes may affect multiple signaling pathways disturbing tissue homeostasis and inducing (autoimmune) inflammation, as suggested by genetic studies in patients.

2018-05-15 | PXD008726 | Pride

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