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A systematic survey of PRMT interactomes reveals key roles of arginine methylation in the global control of RNA splicing and translation

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Homo sapiens

PROVIDER: GSE153144 | GEO | 2022/06/30

REPOSITORIES: GEO

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A systematic survey of PRMT interactomes reveals key roles of arginine methylation in the global control of RNA splicing and translation [RNA-seq]

Project description:Since many proteins involved in splicing regulation were identified as PRMT substrates, we examined the impact of PRMT inhibition on alternative RNA splicing. We achieved effective gene silence with shRNAs in six different PRMTs and examined their effect on splicing using RNA-seq.

2022-06-30 | GSE153143 | GEO

A systematic survey of PRMT interactomes reveals key roles of arginine methylation in the global control of RNA splicing and translation [Ribo-Seq]

Project description:We used Ribo-seq to determine how PRMT inhibition affects translation of different mRNAs, This analysis can generate a “snapshot” of all mRNAs that are occupied by active ribosomes (i.e., undergoing active translation) in a cell at a particular condition.

2022-06-30 | GSE153142 | GEO

A systematic survey of PRMT interactomes reveals key roles of arginine methylation in the global control of RNA splicing and translation [Poly-Seq]

Project description:To examine how PRMT inhibitions affect the translation of different mRNAs, we sequenced the mRNA population associated with different ribosomal fractions after treatment of PRMT1 and PRMT4 inhibitors

2022-06-30 | GSE153141 | GEO

A systematic survey of PRMT interactomes reveals key roles of arginine methylation in the global control of RNA splicing and translation

Project description:A systematic survey of PRMT interactomes reveals key roles of arginine methylation in the global control of RNA splicing and translation

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A systematic survey of PRMT interactomes reveals key roles of arginine methylation in the global control of RNA splicing and translation [RNA-seq]

Project description:A systematic survey of PRMT interactomes reveals key roles of arginine methylation in the global control of RNA splicing and translation [RNA-seq]

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A systematic survey of PRMT interactomes reveals key roles of arginine methylation in the global control of RNA splicing and translation [Poly-Seq]

Project description:A systematic survey of PRMT interactomes reveals key roles of arginine methylation in the global control of RNA splicing and translation [Poly-Seq]

| PRJNA641623 | ENA

A systematic survey of PRMT interactomes reveals key roles of arginine methylation in the global control of RNA splicing and translation [Ribo-Seq]

Project description:A systematic survey of PRMT interactomes reveals key roles of arginine methylation in the global control of RNA splicing and translation [Ribo-Seq]

| PRJNA641624 | ENA

Profiling PRMT methylome reveals roles of hnRNPA1 arginine methylation in RNA splicing and cell growth.

Project description:Numerous substrates have been identified for Type I and II arginine methyltransferases (PRMTs). However, the full substrate spectrum of the only type III PRMT, PRMT7, and its connection to type I and II PRMT substrates remains unknown. Here, we use mass spectrometry to reveal features of PRMT7-regulated methylation. We find that PRMT7 predominantly methylates a glycine and arginine motif; multiple PRMT7-regulated arginine methylation sites are close to phosphorylations sites; methylation sites and proximal sequences are vulnerable to cancer mutations; and methylation is enriched in proteins associated with spliceosome and RNA-related pathways. We show that PRMT4/5/7-mediated arginine methylation regulates hnRNPA1 binding to RNA and several alternative splicing events. In breast, colorectal and prostate cancer cells, PRMT4/5/7 are upregulated and associated with high levels of hnRNPA1 arginine methylation and aberrant alternative splicing. Pharmacological inhibition of PRMT4/5/7 suppresses cancer cell growth and their co-inhibition shows synergistic effects, suggesting them as targets for cancer therapy.

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Caenorhabditis elegans PRMT-7 and PRMT-9 Are Evolutionarily Conserved Protein Arginine Methyltransferases with Distinct Substrate Specificities.

Project description:Caenorhabditis elegans protein arginine methyltransferases PRMT-7 and PRMT-9 are two evolutionarily conserved enzymes, with distinct orthologs in plants, invertebrates, and vertebrates. Biochemical characterization of these two enzymes reveals that they share much in common with their mammalian orthologs. C. elegans PRMT-7 produces only monomethylarginine (MMA) and preferentially methylates R-X-R motifs in a broad collection of substrates, including human histone peptides and RG-rich peptides. In addition, the activity of the PRMT-7 enzyme is dependent on temperature, the presence of metal ions, and the reducing agent dithiothreitol. C. elegans PRMT-7 has a substrate specificity and a substrate preference different from those of mammalian PRMT7, and the available X-ray crystal structures of the PRMT7 orthologs show differences in active site architecture. C. elegans PRMT-9, on the other hand, produces symmetric dimethylarginine and MMA on SFTB-2, the conserved C. elegans ortholog of human RNA splicing factor SF3B2, indicating a possible role in the regulation of nematode splicing. In contrast to PRMT-7, C. elegans PRMT-9 appears to be biochemically indistinguishable from its human ortholog.

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Project description:A decade of high-throughput screenings for intraviral and virus-host protein-protein interactions led to the accumulation of data and to the development of theories on laws governing interactome organization for many viruses. We present here a computational analysis of intraviral protein networks (EBV, FLUAV, HCV, HSV-1, KSHV, SARS-CoV, VACV, and VZV) and virus-host protein networks (DENV, EBV, FLUAV, HCV, and VACV) from up-to-date interaction data, using various mathematical approaches. If intraviral networks seem to behave similarly, they are clearly different from the human interactome. Viral proteins target highly central human proteins, which are precisely the Achilles' heel of the human interactome. The intrinsic structural disorder is a distinctive feature of viral hubs in virus-host interactomes. Overlaps between virus-host data sets identify a core of human proteins involved in the cellular response to viral infection and in the viral capacity to hijack the cell machinery for viral replication. Host proteins that are strongly targeted by a virus seem to be particularly attractive for other viruses. Such protein-protein interaction networks and their analysis represent a powerful resource from a therapeutic perspective.

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