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The protein arginine methyl transferase 5 (PRMT5) emerges as a therapeutic target in S-methyl-5'-thioadenosine phosphorylase (MTAP)-deleted cancers, where MTA accumulation partially inhibits its activity. However, It remains unclear whether other genetic alterations can dictate PRMT5 activity in can...
2026-04-30 | MTBLS14411 | MetaboLights
The goal of this study was to compare the transcriptional profile (RNA-seq) of prmt5 and prmt4a;4b Arabidopsis mutants with their respective wild type plants grown under continous light conditions WT, prmt5 and prmt4a;4b mutant plants were grown together with their respective wild type plants for tw...
ORGANISM(S): Arabidopsis thaliana 
Identification of arginine methylation sites in human HEK293 cells, yielding a total of >8.000 high-confident modification sites on >3.300 proteins
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-31 | MSV000080836 | MassIVE
Protein Arginine MethylTransferase 5 (PRMT5) is known to mediate epigenetic control on chromatin and to functionally regulate components of the splicing machinery. In this study we show that selective deletion of PRMT5 in different organs leads to cell cycle arrest and apoptosis. At the molecular le...
ORGANISM(S): Mus musculus 
The C-terminal domain (CTD) of the RNA polymerase II (RNAPII) subunit POLR2A is a platform for modifications specifying the recruitment of factors that regulate transcription, mRNA processing, and chromatin remodeling. Here, we show that a CTD arginine residue (R1810 in human) that is conserved acr...
ORGANISM(S): Homo sapiens 
Glutathionylation is an important posttranslational modification that protects proteins from further oxidative damage as well as influencing protein structure and activity. In the present study, we demonstrate that the cysteine-42 residue in protein arginine N-methyltransferase 5 (PRMT5) is glutathi...
ORGANISM(S): Homo sapiens (Human) 
2020-09-02 | PXD020428 | Pride
In this study, we analyzed the Arabidopsis homologue of PRMT5, AtPRMT5M-bM-^@M-^Ys function in RNA processing. RNA-seq analyses revealed that AtPRMT5 is involved in a subset of pre-mRNA splicing. Several RNA processing factors involved in regulating flowering time were validated that the correspondi...
ORGANISM(S): Arabidopsis thaliana 
PRMT5 is a type II protein arginine methyltransferase with roles in stem cell biology, reprogramming, cancer and neurogenesis. During embryogenesis in the mouse it was hypothesized that PRMT5 functions with the master germline determinant BLIMP1 to promote primordial germ cell (PGC) specification. U...
ORGANISM(S): Mus musculus 
Primordial germ cells (PGCs) and preimplantation embryos undergo epigenetic reprogramming, which entails comprehensive erasure of DNA methylation. We found that PRMT5, an arginine methyltransferase, translocates from the cytoplasm to the nucleus during this process. Here we show that conditional los...
ORGANISM(S): Mus musculus 
Protein arginine methylation plays essential roles in diverse biological processes, but its role in regulating shoot regeneration remains elusive. In this study, we analyzed the function of the protein arginine methyltransferase AtPRMT5 during de novo shoot regeneration in Arabidopsis. AtPRMT5 encod...
ORGANISM(S): Arabidopsis thaliana 
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