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The deubiquitinase OTUD1 attenuates periodontal inflammation by restricting neutrophil protein transport

ABSTRACT: We report that OTUD1 acts as an immune regulator in periodontitis. OTUD1 inhibits neutrophils migration to inflammatory site via blocking surface protein presentation. Our data reveals that activation of OTUD1 may be a potential strategy for periodontitis treatment.

ORGANISM(S): Mus musculus

PROVIDER: GSE216573 | GEO | 2024/10/31

REPOSITORIES: GEO

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The deubiquitinase OTUD1 attenuates periodontal inflammation by restricting neutrophil protein transport

Project description:The deubiquitinase OTUD1 attenuates periodontal inflammation by restricting neutrophil protein transport

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The deubiquitinase OTUD1 enhances iron transport and potentiates host antitumor immunity.

Project description:Although iron is required for cell proliferation, iron-dependent programmed cell death serves as a critical barrier to tumor growth and metastasis. Emerging evidence suggests that iron-mediated lipid oxidation also facilitates immune eradication of cancer. However, the regulatory mechanisms of iron metabolism in cancer remain unclear. Here we identify OTUD1 as the deubiquitinase of iron-responsive element-binding protein 2 (IREB2), selectively reduced in colorectal cancer. Clinically, downregulation of OTUD1 is highly correlated with poor outcome of cancer. Mechanistically, OTUD1 promotes transferrin receptor protein 1 (TFRC)-mediated iron transportation through deubiquitinating and stabilizing IREB2, leading to increased ROS generation and ferroptosis. Moreover, the presence of OTUD1 promotes the release of damage-associated molecular patterns (DAMPs), which in turn recruits the leukocytes and strengthens host immune response. Reciprocally, depletion of OTUD1 limits tumor-reactive T-cell accumulation and exacerbates colon cancer progression. Our data demonstrate that OTUD1 plays a stimulatory role in iron transportation and highlight the importance of OTUD1-IREB2-TFRC signaling axis in host antitumor immunity.

| S-EPMC7857436 | biostudies-literature

Transcriptome analysis of control and OTUD1 knockout T24 Cells

Project description:We have confirmed that OTUD1 interacted directly with Akt and inhibited Akt phosphorylation. To investigate the exact mechanism of OTUD1 in the regulation of Akt signaling pathway, we established T24 cells with stable OTUD1 depletion by using sgRNA.

2022-12-23 | GSE217570 | GEO

Endothelial OTUD1 promotes Ang II-induced vascular remodeling by deubiquitinating SMAD3

Project description:Understanding the molecular mechanisms of pathological vascular remodeling is important for treating cardiovascular diseases and complications. Recent studies have highlighted a role of deubiquitinases in vascular pathophysiology. In this study, we investigated the role of a deubiquitinase, OTUD1, in angiotensin II (Ang II)-induced vascular remodeling. We identified upregulated OTUD1 in the vascular endothelium of Ang II-challenged mice and showed OTUD1 deletion attenuated vascular remodeling, collagen deposition, and EndMT. Conversely, OTUD1 overexpression aggravated these pathological changes both in vivo and in vitro. Mechanistically, SMAD3 was identified as a substrate of OTUD1 using co-immunoprecipitation followed with LC-MS/MS. We found OTUD1 stabilizes SMAD3 and facilitates SMAD3/SMAD4 complex formation and subsequent nuclear translocation through both K48- and K63-linked deubiquitination. OTUD1-mediated SMAD3 activation regulate the transcription of genes involved in vascular EndMT and remodeling in HUVECs. Finally, SMAD3 inhibition reversed OTUD1-promoted vascular remodeling. Our findings demonstrate endothelial OTUD1 promoted Ang II-induced vascular remodeling by deubiquitinating SMAD3. This study identified SMAD3 as a target of OTUD1 and indicates OTUD1 as a potential therapeutic target for the diseases related to vascular remodeling.

2022-12-24 | GSE217304 | GEO

Transcriptome analysis of control and OTUD1 knockout SKOV3 Cells

Project description:We have confirmed that high level of OTUD1 is important for retaining ovarian cancer stem cells (OCSCs) property. To investigate the exact mechanism of OTUD1 in the regulation of stemness maintain, we established SKOV3 cells with stable OTUD1 depletion by using sgRNA.

2024-01-15 | GSE232786 | GEO

OTUD1 aggravates pathological cardiac hypertrophy through activation of PGAM5-ASK1 signaling pathways

Project description:Deubiquitinating enzymes have gained more and more attention in the field of pathological cardiac hypertrophy. In this study, we explored the role of a deubiquitinase, OTUD1, in the transverse aortic constriction (TAC) induced cardiac hypertrophy. We found the upregulation of OTUD1 in heart tissues of TAC mice. OTUD1 overexpression promoted cardiac hypertrophy, cardiac fibrosis and apoptosis. Conversely, OTUD1 depletion alleviated these pathological changes both in vivo and in vitro. Mechanistically, ASK1 was identified as one substrate of OTUD1 using co-immunoprecipitation followed with LC-MS/MS. Interestingly, OTUD1 didn’t deubiquitinate ASK1, but increased the phosphorylation level of ASK1 during the process of cardiac hypertrophy. We found that PGAM5, the upper stream regulator of ASK1, was stabilized by OTUD1 in a K63 ubiquitin chain dependent way, which reminded us OTUD1 increased the phosphorylation level of ASK1 by deubiquitinating PGAM5. This study identified the OTUD1-ASK1 axis as a potential therapeutic target for pathological cardiac hypertrophy.

2023-09-05 | GSE241809 | GEO

The deubiquitinase OTUD1 regulates immunoglobulin production and proteasome inhibitor sensitivity in multiple myeloma

Project description:Serum monoclonal immunoglobulin (Ig) is the main diagnostic factor for patients with multiple myeloma (MM), however its prognostic potential remains unclear. On a large MM patient cohort (n=4146), we observe no correlation between serum Ig levels and patient survival, while amount of intracellular Ig has a strong predictive effect. Focused CRISPR screen, transcriptional and proteomic analysis identify deubiquitinase OTUD1 as a critical mediator of Ig synthesis, proteasome inhibitor sensitivity and tumour burden in MM. Mechanistically, OTUD1 deubiquitinates peroxiredoxin 4 (PRDX4), protecting it from endoplasmic reticulum (ER)-associated degradation. In turn, PRDX4 facilitates the synthesis of Ig which coincides with the accumulation of unfolded proteins and higher ER stress. The elevated load on proteasome ultimately potentiates myeloma response to proteasome inhibitors providing a window for a rational therapy. Collectively, our findings support the significance of the Ig production machinery as a yet unappreciated biomarker and target in the combinatory treatment of MM patients.

2023-03-11 | PXD037309 | Pride

The deubiquitinase OTUD1 enhances iron transport and potentiates host antitumor immunity

Project description:Although iron is required for cell proliferation, iron-dependent programmed cell death serves as a critical barrier to tumor growth and metastasis. Emerging evidence suggests that iron-mediated lipid oxidation also facilitates immune eradication of cancer. However, the regulatory mechanisms of iron metabolism in cancer remain unclear. Here we identify OTUD1 as the deubiquitinase of Iron-responsive element-binding protein 2 (IREB2), selectively reduced in colorectal cancer. Clinically, downregulation of OTUD1 is highly correlated with poor outcome of cancer. Mechanistically, OTUD1 promotes Transferrin receptor protein 1 (TFRC)-mediated iron transportation through deubiquitinating and stabilizing IREB2, leading to increased ROS generation and ferroptosis. Moreover, presence of OTUD1 promotes the release of damage associated molecular patterns (DAMPs), which in turn recruits the leukocytes and strengthens host immune response. Reciprocally, depletion of OTUD1 limits tumor-reactive T cell accumulation and exacerbates colon cancer progression. Our data demonstrate that OTUD1 plays a stimulatory role in iron transportation and highlight the importance of OTUD1-IREB2-TFRC signaling axis in host antitumor immunity.

| S-SCDT-EMBOR-2020-51162V1P | biostudies-other

Endothelial OTUD1 promotes Ang II-induced vascular remodeling by deubiquitinating SMAD3

2022-12-24 | PXD037926 | Pride

Analysis of activated CD4T cells and OTUD1-deficient CD4T cells reveals novel target proteins and related signaling pathway affected by OTUD1

Project description:The goals of the study are to compare differently expressed proteins in activated CD4T and OTUD1-deficient CD4T cells. Proteomics was performed with activated CD4T and OTUD1-deficient CD4T cells (n = 3 for each group) to identify the differently expressed proteins and related signaling pathway affected by OTUD1.

2023-01-18 | PXD036217 | Pride

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