Correction: SIRT2 regulates NF-κB-dependent gene expression through deacetylation of p65 Lys310 (doi:10.1242/jcs.073783)

Rothgiesser, Karin; Erener, Süheda; Waibel, Susanne; Lüscher, Bernhard; Hottiger, Michael O.

doi:10.1242/jcs.232801

Cited by 10 publications

(4 citation statements)

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“…Sirtuin 2 (SIRT2) depletion results in a decrease in cellular iron levels; mechanistically, SIRT2 deacetylates nuclear factor erythroid-derived 2-related factor 2 (NRF2) on K506 and K508 to reduce FPN1 expression, leading to the decreased cellular iron export ( 113 ). After TNF-α stimulation, Sirt2 -/- mouse embryonic fibroblasts (MEFs) cells become highly acetylated, resulting in increased expression of NF-κB target genes, including Mpa2l , Cxcl5 , Ip10 , and Il6 ( 114 ). Reciprocally, whether iron status shapes M1 polarization as an outcome of the effect of SIRT2/NRF2 is still unknown.…”

Section: Mechanisms Whereby Iron Mediates Macrophage Polarizationmentioning

confidence: 99%

Ironing Out the Details: How Iron Orchestrates Macrophage Polarization

Xia

et al. 2021

Front. Immunol.

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Iron fine-tunes innate immune responses, including macrophage inflammation. In this review, we summarize the current understanding about the iron in dictating macrophage polarization. Mechanistically, iron orchestrates macrophage polarization through several aspects, including cellular signaling, cellular metabolism, and epigenetic regulation. Therefore, iron modulates the development and progression of multiple macrophage-associated diseases, such as cancer, atherosclerosis, and liver diseases. Collectively, this review highlights the crucial role of iron for macrophage polarization, and indicates the potential application of iron supplementation as an adjuvant therapy in different inflammatory disorders relative to the balance of macrophage polarization.

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Section: Mechanisms Whereby Iron Mediates Macrophage Polarizationmentioning

confidence: 99%

Ironing Out the Details: How Iron Orchestrates Macrophage Polarization

Xia

et al. 2021

Front. Immunol.

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“…Similarly, cytoplasmic SIRT2 induces the deacetylate of p65 Lys310 and regulates NF-κB–dependent gene expression viz . reduces transcription of pro-inflammation genes ( Rothgiesser et al, 2019 ). These finding showing that acetylation status of NF-κB is an important driver of rates of inflammation in cells and tissues.…”

Section: Do Epigenetics Mechanisms Contribute To Vascular Aging?mentioning

confidence: 99%

Epigenetics and Vascular Senescence–Potential New Therapeutic Targets?

et al. 2020

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Epigenetics is defined as the heritable alterations of gene expression without changes to the coding sequence of DNA. These alterations are mediated by processes including DNA methylation, histone modifications, and non-coding RNAs mechanisms. Vascular aging consists of both structural and functional changes in the vasculature including pathological processes that drive progression such as vascular cell senescence, inflammation, oxidation stress, and calcification. As humans age, these pathological conditions gradually accumulate, driven by epigenetic alterations, and are linked to various aging-related diseases. The development of drugs targeting a spectrum of epigenetic processes therefore offers novel treatment strategies for the targeting of age-related diseases. In our previous studies, we identified HDAC4, JMJD3, Fra-1, and GATA4 as potential pharmacological targets for regulating vascular inflammation, injury, and senescence.

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“…SIRT2 translocates to the chromatin and deacetylates histone H3 at lysine 18 after Listeria infection, modulating the expression of a set of genes necessary for bacterial replication (Eskandarian et al , 2013; Pereira et al , 2018). SIRT2 directly binds to and deacetylates p65, the subunit of NF‐κB, inhibiting the activation of NF‐κB as well as the transcription of numerous pro‐inflammatory cytokines (Zhang & Chi, 2018; Rothgiesser et al , 2019). SIRT2 also negatively regulates the NLRP3 inflammasome assemble by deacetylating NLRP3, leading to the reduced production of IL‐1β and cleaved caspase 1 (He et al , 2020).…”

Section: Introductionmentioning

confidence: 99%

SIRT2 negatively regulates the cGAS‐STING pathway by deacetylating G3BP1

Li,

Bie,

Song

et al. 2023

EMBO Reports

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SIRT2, a cytoplasmic member of the Sirtuin family, has important roles in immunity and inflammation. However, its function in regulating the response to DNA virus infection remains elusive. Here, we find that SIRT2 is a unique regulator among the Sirtuin family that negatively modulates the cGAS‐STING‐signaling pathway. SIRT2 is down‐regulated after Herpes simplex virus‐1 (HSV‐1) infection, and SIRT2 deficiency markedly elevates the expression levels of type I interferon (IFN). SIRT2 inhibits the DNA binding ability and droplet formation of cGAS by interacting with and deacetylating G3BP1 at K257, K276, and K376, leading to the disassembly of the cGAS‐G3BP1 complex, which is critical for cGAS activation. Administration of AGK2, a selective SIRT2 inhibitor, protects mice from HSV‐1 infection and increases the expression of IFN and IFN‐stimulated genes. Our study shows that SIRT2 negatively regulates cGAS activation through G3BP1 deacetylation, suggesting a potential antiviral strategy by modulating SIRT2 activity.

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Correction: SIRT2 regulates NF-κB-dependent gene expression through deacetylation of p65 Lys310 (doi:10.1242/jcs.073783)

Cited by 10 publications

References 0 publications

Ironing Out the Details: How Iron Orchestrates Macrophage Polarization

Ironing Out the Details: How Iron Orchestrates Macrophage Polarization

Epigenetics and Vascular Senescence–Potential New Therapeutic Targets?

SIRT2 negatively regulates the cGAS‐STING pathway by deacetylating G3BP1

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