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DNA methylation data for VPS39-silenced human muscle cells and controls

ABSTRACT: DNA methylation data for VPS39-silenced human muscle cells and controls

PROVIDER: PRJNA701306 | ENA |

REPOSITORIES: ENA

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mRNA expression data for VPS39-silenced human muscle cells and controls

Project description:mRNA expression data for VPS39-silenced human muscle cells and controls (n=6 per group) were obtained using GeneChip™ Human Gene 2.0 ST Assay (Applied Biosystems)

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DNA methylation data for VPS39-silenced human muscle cells and controls

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mRNA expression data for VPS39-silenced human muscle cells and controls

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Insights into the role of VPS39 and its interaction with CP204L and A137R in ASFV infection

Project description:The African swine fever virus (ASFV) is a large and complex DNA virus that causes a highly le-thal disease in swine, for which no antiviral drugs or vaccines are currently available. Studying viral–host protein-protein interactions advances our understanding of the molecular mecha-nisms underlying viral replication and pathogenesis and can facilitate the discovery of antiviral therapeutics. In this study, we employed affinity tagging and purification mass spectrometry to characterize the interactome of VPS39, an important cellular factor during the early phase of ASFV replication. The interaction network of VPS39 revealed associations with mitochondrial proteins involved in membrane contact sites formation and cellular respiration. We show that ASFV proteins CP204L and A137R target VPS39 by interacting with its clathrin heavy chain func-tional domain. Furthermore, we elaborate on the potential mechanisms by which VPS39 may contribute to ASFV replication and prioritize interactions for further investigation into mito-chondrial protein function in the context of ASFV infection.

2024-09-17 | PXD054169 | Pride

expression data for the mouse skeletal muscle from VPS39 ko and WT

Project description:mRNA expression data for the mouse muscle (n=6 per sex and genotype, for a total of 24 mice) were obtained using Clariom™ S Assay Mouse (Applied Biosystems) according to the manufacturer’s recommendations.

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African swine fever virus protein CP204L is involved in endosomal trafficking and interacts with the VPS39 subunit of the HOPS complex

Project description:African swine fever virus (ASFV) is a large DNA virus causing a highly contagious disease in domestic and wild boar, for which no treatment is available. ASFV vaccine development is hindered by large gaps in knowledge considering virus protein function and virus-host interaction. This study shows that the ASFV CP204L is a multifunctional protein engaged in endosomal trafficking and localizes to virus replication sites. Moreover, VPS39, a component of the HOPS complex, is a direct host interactor of CP204L. The virus CP204L binds the VPS39 domain responsible for its recruitment to the endosomal membrane, prevents its integration into the HOPS complex, and promotes the clustering of lysosomes. Additionally, we show that VPS39 is an important factor in the early phase of infection, as virus replication and protein synthesis in VPS39 knockout cells are delayed. These results uncover a novel function of viral protein CP204L and extend our understanding of complex interaction between virus and host, providing insights for developing a vaccine to prevent and control ASFV.

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The HOPS complex subunit VPS39 controls ciliogenesis through autophagy.

Project description:Primary cilia are microtubule-based organelles that assemble and protrude from the surface of most mammalian cells during quiescence. The biomedical relevance of cilia is indicated by disorders ascribed to cilia dysfunction, known as ciliopathies, that display distinctive features including renal cystic disease. In this report, we demonstrate that vacuolar protein sorting 39 (VPS39), a component of the homotypic fusion and vacuole protein sorting (HOPS) complex, acts as a negative regulator of ciliogenesis in human renal cells, by controlling the localization of the intraflagellar transport 20 protein at the base of cilia through autophagy. Moreover, we show that VPS39 controls ciliogenesis through autophagy also in vivo in renal tubules of medaka fish. These observations suggest a direct involvement of the HOPS complex in the regulation of autophagy-mediated ciliogenesis and eventually in target selection. Interestingly, we show that the impact of autophagy modulation on ciliogenesis is cell-type dependent and strictly related to environmental stimuli. This report adds a further tile to the cilia-autophagy connection and suggests that VPS39 could represent a new biological target for the recovery of the cilia-related phenotypes observed in the kidneys of patients affected by ciliopathies.

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