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PRMT1 encodes a member of the protein arginine N-methyltransferase (PRMT) family.
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there is an imbalance in the vasoconstriction-vasodilation status toward constriction. It is our hypothesis that, in hypoxic stress, a key player in initiating this imbalance is the enzyme, protein arginine methyltransferase-1 (PRMT1).
Pharmacological inhibition of KDM4C (show KDM4C Proteins)/PRMT1 suppresses transcription and transformation ability of MLL (show MLL Proteins) fusions
Methylation by PRMT1 may regulate Smurf2 (show SMURF2 Proteins) stability and control TGF-beta (show TGFB1 Proteins) signaling.
PRMT1 regulates glucose-stimulated insulin (show INS Proteins) secretion through enhanced methylation-induced nuclear localization of FOXO1 (show FOXO1 Proteins), which subsequently suppresses the nuclear localization of PDX-1 (show PDX1 Proteins)
we define the arginines within the RGG/RG motifs as the site of methylation by PRMT1 both in vitro and in vivo. The arginines within the human hnRNPUL1 RGG/RG motifs were substituted with lysines to generate hnRNPUL1(RK).
PRMT1-mediated methylation of the EGF receptor (show EGFR Proteins) regulates signaling and cetuximab response.
miR (show MLXIP Proteins)-503-mediated PRMT1 could emerge as a potential important biomarker for hepatocellular carcinoma progression and metastasis
results challenge the unilateral view that increased PRMT1 expression necessarily results in increased ADMA synthesis and demonstrate that enzymatic activity can be regulated in a redox-sensitive manner
High PRMT1 expression is associated with Epithelial-Mesenchymal-Transition and metastasis in Non-small Cell Lung Cancer.
The ATXN2L (show ATXN2L Proteins) associates with the protein arginine-N-methyltransferase 1 (PRMT1).
PRMT1 is required for CNS development, especially for oligodendrocyte maturation processes
PRMT1 knockdown reduced H4R3me2a expression to alter potential H3K9/K14 (show KRT14 Proteins) acetylation by acetyltransferases, and to eventually result in diminished acH3K9/K14 (show KRT14 Proteins) modification in nucleus accumbens. PRMT1 is the main enzyme responsible for this modification.
Study provides evidence for loss of PRMT1 function as a consequence of cytoplasmic accumulation of FUS (show FUS Proteins) in the pathogenesis of amyotrophic lateral sclerosis, including changes in the histone code regulating gene transcription.
In vivo, levels of lipogenic proteins, inflammatory molecules, PGC-1alpha, and PRMT1 were increased in the livers of HFD mice compared with those fed a chow diet, and were ameliorated in HFD Txnip (show TXNIP Proteins)(-/-) mice.
GSK3- and PRMT-1-dependent modifications of desmoplakin control desmoplakin-cytoskeleton dynamics.
PRMT1 concentrates in cytoplasmic bodies, which respond to DNA injury in the cell nucleus
PRMT1-mediated arginine methylation could be implicated in the nucleus-cytoplasmic shuttling of FUS/TLS (show FUS Proteins).
PRMT1-dependent regulation of FoxO1 (show FOXO1 Proteins) is critical in hepatic glucose metabolism in vivo.
Depletion of PRMT1 diminished the ability of ALS-linked FUS (show FUS Proteins) mutants to localize to the cytoplasm.
This gene encodes a member of the protein arginine N-methyltransferase (PRMT) family. Post-translational modification of target proteins by PRMTs plays an important regulatory role in many biological processes, whereby PRMTs methylate arginine residues by transferring methyl groups from S-adenosyl-L-methionine to terminal guanidino nitrogen atoms. The encoded protein is a type I PRMT and is responsible for the majority of cellular arginine methylation activity. Increased expression of this gene may play a role in many types of cancer. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene, and a pseudogene of this gene is located on the long arm of chromosome 5.
HMT1 (hnRNP methyltransferase, S. cerevisiae)-like 2
, heterogeneous nuclear ribonucleoprotein methyltransferase 1-like 2
, histone-arginine N-methyltransferase PRMT1
, interferon receptor 1-bound protein 4
, protein arginine N-methyltransferase 1
, arginine N-methyltransferase 1
, heterogeneous nuclear ribonucleoproteins methyltransferase-like 2