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Mirc11 selectively regulates inflammatory responses of NK cells by targeting ubiquitin modifiers and TRAF6-dependent NF-kB and AP1 activation (RNA-seq: Listeria_challenge)

ABSTRACT: Lack of Mirc11 significantly reduces NK cell-mediated cytokine production in vivo Mirc11 cluster targets NF-kB and AP-1-mediated gene transcriptions

ORGANISM(S): Mus musculus

PROVIDER: GSE136013 | GEO | 2019/08/20

REPOSITORIES: GEO

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Mirc11 selectively regulates inflammatory responses of NK cells by targeting ubiquitin modifiers and TRAF6-dependent NF-kB and AP1 activation (RNA-seq: IL-2_expanded_NKG2D_stimulation)

Project description:Lack of Mirc11 significantly reduces NK cell-mediated cytokine production in vivo Mirc11 cluster targets NF-kB and AP-1-mediated gene transcriptions

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Mirc11 selectively regulates inflammatory responses of NK cells by targeting ubiquitin modifiers and TRAF6-dependent NF-kB and AP1 activation

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

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Mirc11 selectively regulates inflammatory responses of NK cells by targeting ubiquitin modifiers and TRAF6-dependent NF-kB and AP1 activation

Project description:Mirc11 selectively regulates inflammatory responses of NK cells by targeting ubiquitin modifiers and TRAF6-dependent NF-kB and AP1 activation

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Mirc11 selectively regulates inflammatory responses of NK cells by targeting ubiquitin modifiers and TRAF6-dependent NF-kB and AP1 activation (RNA-seq: Listeria_challenge)

Project description:Mirc11 selectively regulates inflammatory responses of NK cells by targeting ubiquitin modifiers and TRAF6-dependent NF-kB and AP1 activation (RNA-seq: Listeria_challenge)

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Mirc11 selectively regulates inflammatory responses of NK cells by targeting ubiquitin modifiers and TRAF6-dependent NF-kB and AP1 activation (RNA-seq: IL-2_expanded_NKG2D_stimulation)

Project description:Mirc11 selectively regulates inflammatory responses of NK cells by targeting ubiquitin modifiers and TRAF6-dependent NF-kB and AP1 activation (RNA-seq: IL-2_expanded_NKG2D_stimulation)

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<i>Mirc11</i> Disrupts Inflammatory but Not Cytotoxic Responses of NK Cells.

Project description:Natural killer (NK) cells generate proinflammatory cytokines that are required to contain infections and tumor growth. However, the posttranscriptional mechanisms that regulate NK cell functions are not fully understood. Here, we define the role of the microRNA cluster known as Mirc11 (which includes miRNA-23a, miRNA-24a, and miRNA-27a) in NK cell-mediated proinflammatory responses. Absence of Mirc11 did not alter the development or the antitumor cytotoxicity of NK cells. However, loss of Mirc11 reduced generation of proinflammatory factors in vitro and interferon-γ-dependent clearance of Listeria monocytogenes or B16F10 melanoma in vivo by NK cells. These functional changes resulted from Mirc11 silencing ubiquitin modifiers A20, Cbl-b, and Itch, allowing TRAF6-dependent activation of NF-κB and AP-1. Lack of Mirc11 caused increased translation of A20, Cbl-b, and Itch proteins, resulting in deubiquitylation of scaffolding K63 and addition of degradative K48 moieties on TRAF6. Collectively, our results describe a function of Mirc11 that regulates generation of proinflammatory cytokines from effector lymphocytes.

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Regulation of ubiquitin and ubiquitin-like modifiers by phosphorylation.

Project description:The regulatory influence of ubiquitin is vast, encompassing all cellular processes, by virtue of its central roles in protein degradation, membrane trafficking, and cell signaling. But how does ubiquitin, a 76 amino acid peptide, carry out such diverse, complex functions in eukaryotic cells? Part of the answer is rooted in the high degree of complexity associated with ubiquitin polymers, which can be 'read' and processed differently depending on topology and cellular context. However, recent evidence indicates that post-translational modifications on ubiquitin itself enhance the complexity of the ubiquitin code. Here, we review recent discoveries related to the regulation of the ubiquitin code by phosphorylation. We summarize what is currently known about phosphorylation of ubiquitin at Ser65, Ser57, and Thr12, and we discuss the potential for phosphoregulation of ubiquitin at other sites. We also discuss accumulating evidence that ubiquitin-like modifiers, such as SUMO, are likewise regulated by phosphorylation. A complete understanding of these regulatory codes and their complex lexicon will require dissection of mechanisms that govern phosphorylation of ubiquitin and ubiquitin-like proteins, particularly in the context of cellular stress and disease.

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Mechanism of ubiquitin transfer promoted by TRAF6.

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2-O-Methylhonokiol Suppresses HCV Replication via TRAF6-Mediated NF-kB Activation.

Project description:Hepatitis C virus (HCV) is associated with various liver diseases. Chronic HCV infection is characterized by an abnormal host immune response. Therefore, it is speculated that to suppress HCV, a well-regulated host immune response is necessary. 2-O-methylhonokiol was identified by the screening of anti-HCV compounds using Renilla luciferase assay in Huh 7.5/Con 1 genotype 1b replicon cells. Here, we investigated the mechanism by which 2-O-methylhonokiol treatment inhibits HCV replication using real-time PCR. Our data shows that treatment with 2-O-methylhonokiol activated innate immune responses via nuclear factor kappa-light-chain-enhancer of activated B cells (NF-kB) pathway. Additionally, the immunoprecipitation result shows that treatment with 2-O-methylhonokiol augmented tumor necrosis factor receptor (TNFR)-associated factor 6 (TRAF6) by preventing p62 from binding to TRAF6, resulting in reduced autophagy caused by HCV. Finally, we reproduced our data with the conditioned media from 2-O-methylhonokiol-treated cells. These findings strongly suggest that 2-O-methylhonokiol enhances the host immune response and suppresses HCV replication via TRAF6-mediated NF-kB activation.

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Misfolded SOD1 binds the ubiquitin ligase TRAF6

Project description:Amyotrophic lateral sclerosis (ALS) is a fatal disease, characterized by the selective loss of motor neurons. Mutations in Cu/Zn superoxide dismutase (SOD1) are the second most common cause of ALS and it is now well accepted that they result in a gain of toxicity due to protein misfolding. We previously demonstrated in the SOD1G93A rat model that misfolded SOD1 exists as distinct conformers and deposits on mitochondrial subpopulations. Here, using SOD1G93A rats coupled with conformation-restricted antibodies for misfolded SOD1 (AMF7-63 and B8H10), we identified the interactomes of the mitochondrial pools of misfolded SOD1. This strategy identified binding partners that uniquely interacted with either AMF7-63- or B8H10-reactive SOD1 conformers as well as a high proportion of interactors common to both conformers. Of this latter set, we identified the E3 ubiquitin ligase TNF receptor-associated factor 6 (TRAF6) and determined that exposure of the SOD1 functional loops facilitates this interaction. However, this conformational criterion is not universally fulfilled by all SOD1 mutants and differentiates TRAF6-interacting from non-interacting SOD1 mutants. Functionally, TRAF6 stimulates mutant SOD1 polyubiquitination and aggregation. While TRAF6 E3 ubiquitin ligase activity is required for the former, it is dispensable for the latter, indicating that the polyubiquitination and aggregation of mutant SOD1 mediated by TRAF6 are independent events. We propose that misfolded SOD1 binding to TRAF6 may be relevant to ALS disease.

2020-02-24 | PXD015279 | Pride

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