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The role of Matrin 3 (MATR3) in innate immune response to double-stranded RNAs (MinION RNA-Seq)

ABSTRACT: To investigate the role of Matrin 3 (MATR3) in the innate immune response we analyzed and compared MATR3 KO Clones versus Wild Type HAP1 cells.

ORGANISM(S): Homo sapiens

PROVIDER: GSE216826 | GEO | 2024/05/15

REPOSITORIES: GEO

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The role of Matrin 3 (MATR3) in innate immune response to double-stranded RNAs (NanoString)

Project description:To investigate the role of Matrin 3 (MATR3) in the innate immune response we analyzed and compared MATR3 KO Clones versus Wild Type HAP1 cells.

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The role of Matrin 3 (MATR3) in innate immune response to double-stranded RNAs (Illumina RNA-Seq)

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The role of Matrin 3 (MATR3) in innate immune response to double-stranded RNAs

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

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ALS Associated Mutations in Matrin 3 Alter Protein-Protein Interactions and Impede mRNA Nuclear Export

Project description:Mutations in Matrin 3 have recently been linked to ALS, though the mechanism of disease in these patients is still unknown. To define the protein interactome of wild-type and ALS-linked MATR3 mutations, we performed immunoprecipitation followed by mass spectrometry experiments in NSC-34 cells expressing human wild-type or mutant Matrin 3. Gene ontology analysis identified a novel role for Matrin in mRNA transport centered around proteins in the TRanscription and EXport (TREX) complex, known to function in mRNA biogenesis and nuclear export. ALS-linked mutations in Matrin 3 led to its re-distribution within the nucleus, decreased co-localization with endogenous Matrin 3 and increased co-localization with TREX components. Expression of disease-causing Matrin 3 mutations led to nuclear mRNA export defects of both global mRNA and the mRNA of ALS linked proteins TDP-43 and FUS. Our findings demonstrate the first pathogenic mechanism attributable to MATR3 mutations and further link cellular transport defects to ALS.

2017-11-15 | PXD007710 | Pride

Protein interaction networks for Matrin 3 encoding mutations

Project description:To understand how mutations in Matrin 3 (MATR3) cause amyotrophic lateral sclerosis (ALS) and distal myopathy, we used transcriptome and interactome analysis. We found over-expression of wild-type (WT) or F115C mutant MATR3 had little impact on gene expression in neuroglia cells. We identified ~123 proteins that bound MATR3, with proteins associated with stress granules and RNA processing/splicing being prominent. The interactome of myopathic S85C and ALS-variant F115C MATR3 were virtually identical to WT protein. Deletion of RNA recognition motif (RRM1) or Zn finger motifs (ZnF1 or ZnF2) diminished the binding of a subset of MATR3 interacting proteins. Remarkably, deletion of the RRM2 motif caused enhanced binding of >100 hundred proteins. In live cells, MATR3 lacking RRM2 (ΔRRM2) formed intranuclear spherical structures that fused over time into large structures. Our findings in the cell models used here suggest that MATR3 with disease-causing mutations is not dramatically different from WT protein in modulating gene regulation or in binding to normal interacting partners. The intra-nuclear localization and interaction network of MATR3 is strongly modulated by its RRM2 domain.

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MATR3-binding RNAs in ES cells [RIP-Seq]

Project description:We performed RNA binding protein immunoprecipitation (RIP) assay with anti-IgG/anti-MATR3 antibody. The RNA libraries were constructed using rib-off and strand-specific kits. Next-generation sequencing (NGS) were performed to analyze MATR3-binding RNAs.

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Project description:Precise control of gene expression during differentiation relies on the interplay of chromatin and nuclear structure. Despite an established contribution of nuclear membrane proteins to developmental gene regulation, little is known regarding the role of inner nuclear proteins. Here we demonstrate that loss of the nuclear scaffolding protein Matrin-3 (Matr3) in erythroid cells leads to morphological and gene expression changes characteristic of accelerated maturation, as well as broad alterations in chromatin organization similar to those accompanying differentiation. Matr3 protein interacts with CTCF and the cohesin complex, and its loss perturbs their occupancy at a subset of sites. Destabilization of CTCF and cohesin binding correlates with altered transcription and accelerated differentiation. This association is conserved in embryonic stem cells. Our findings indicate Matr3 negatively affects cell fate transitions and demonstrate that a critical inner nuclear protein impacts occupancy of architectural factors, culminating in broad effects on chromatin organization and cell differentiation.

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