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Protein arginine methyltransferase 1

Protein-Arginine N-Methyltransferase, PRMT1, protein arginine methyltransferase 1
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. [provided by RefSeq, Dec 2011] (from NCBI)
Top mentioned proteins: Histone, CAN, CARM1, ACID, H4
Papers on Protein-Arginine N-Methyltransferase
Small Molecule Inhibitors of Protein Arginine Methyltransferases.
Zheng et al., Athens, United States. In Expert Opin Investig Drugs, Feb 2016
Great efforts are seen in screening and designing potent and selective PRMT inhibitors, and a number of micromolar and submicromolar inhibitors have been obtained for key PRMT enzymes such as PRMT1, CARM1, and PRMT5.
Protein arginine methyltransferase 1 interacts with Gli1 and regulates its transcriptional activity.
Chen et al., Shanghai, China. In Tumour Biol, Feb 2016
Our previous studies have shown that PRMT1 activated Hedgehog signaling in the esophageal squamous cell carcinoma (ESCC) cells and promoted the growth and migration of cancer cells.
Targeting Aberrant Epigenetic Networks Mediated by PRMT1 and KDM4C in Acute Myeloid Leukemia.
So et al., Los Angeles, United States. In Cancer Cell, Feb 2016
Here we provide experimental evidence for the functional involvement and therapeutic potential of targeting PRMT1, an H4R3 methyltransferase, in various MLL and non-MLL leukemias.
Tumor suppressor BTG1 promotes PRMT1-mediated ATF4 function in response to cellular stress.
van Leeuwen et al., Nijmegen, Netherlands. In Oncotarget, Jan 2016
We show that BTG1 interacts with ATF4 and positively modulates its activity by recruiting the protein arginine methyl transferase PRMT1 to methylate ATF4 on arginine residue 239.
Genotype polymorphisms of genes regulating nitric oxide synthesis determine long-term arteriovenous fistula patency in male hemodialysis patients.
Lin et al., Taipei, Taiwan. In Ren Fail, Jan 2016
Genotype polymorphisms of NO-biosynthesis regulating enzymes (DDAH-1, DDAH-2, eNOS and PRMT1) were compared between HD patients with (n = 161) and without (n = 419) history of AVF malfunction.
Severe Hypomyelination and Developmental Defects Are Caused in Mice Lacking Protein Arginine Methyltransferase 1 (PRMT1) in the Central Nervous System.
Fukamizu et al., Tsukuba, Japan. In J Biol Chem, Jan 2016
UNASSIGNED: Protein arginine methyltransferase 1 (PRMT1) is involved in cell proliferation, DNA damage response, and transcriptional regulation.
Effect of phosphorylation and methylation on the function of the p16(INK4a) protein in non-small cell lung cancer A549 cells.
Wang et al., Changchun, China. In Oncol Lett, Oct 2015
Furthermore, the protein arginine methyltransferases (PRMTs), such as PRMT1, PRMT4 and PRMT6, were determined to be involved in the methylation of the p16 arginine residues.
Roles of protein arginine methyltransferases in the control of glucose metabolism.
Koo et al., Seoul, South Korea. In Endocrinol Metab (seoul), 2015
More specifically, we summarize the roles of four PRMTs: PRMT1, PRMT 4, PRMT 5, and PRMT 6, in the control of hepatic gluconeogenesis through specific regulation of FoxO1- and CREB-dependent transcriptional events.
Role of PRMTs in cancer: Could minor isoforms be leaving a mark?
Côté et al., Ottawa, Canada. In World J Biol Chem, 2014
Specifically, PRMT1, PRMT2, CARM1 and PRMT7 have been shown to have alternative isoforms and others may be currently unrealized.
Nutritional models of foetal programming and nutrigenomic and epigenomic dysregulations of fatty acid metabolism in the liver and heart.
Guéant-Rodriguez et al., Vandœuvre-lès-Nancy, France. In Pflugers Arch, 2014
High-fat diet and overfeeding impair AMPK-dependent phosphorylation of PGC-1α, while MDD decreases PGC-1α methylation through decreased expression of PRMT1 and cellular level of S-adenosyl methionine.
Epigenetic regulation of pregnane X receptor activity.
Tian, College Station, United States. In Drug Metab Rev, 2013
Chromatin modifications are carried out, in part, through interaction with coregulator complexes, including steroid coactivators (SRCs), corepressors (NcoR/SMRT), hepatocyte nuclear factor 4 alpha, proliferator activated receptor γ coactivator 1 alpha and protein arginine methyltransferase 1. PXR can be modified by acetylation, phosphorylation and sumoylation, and the promoter of PXR can be methylated at the "CpG" island.
Multidomain integration in the structure of the HNF-4α nuclear receptor complex.
Rastinejad et al., Orlando, United States. In Nature, 2013
An arginine target of PRMT1 methylation protrudes directly into this convergence zone and sustains its integrity.
Proteinuria elevates asymmetric dimethylarginine levels via protein arginine methyltransferase-1 overexpression in a rat model of nephrotic syndrome.
Okuda et al., Kurume, Japan. In Life Sci, 2012
proteinuria might enhance asymmetric dimethylarginine generation in tubular cells, at least in part via the overexpression of PRMT-1 triggered by oxidative stress
Protein arginine methylation of SERBP1 by protein arginine methyltransferase 1 affects cytoplasmic/nuclear distribution.
Li et al., T'ai-chung-shih, Taiwan. In J Cell Biochem, 2012
The RG-rich and RGG box of SERBP1 is asymmetrically dimethylated by PRMT1 and the modification affects protein interaction and intracellular localization of the protein.
PRMT1 interacts with AML1-ETO to promote its transcriptional activation and progenitor cell proliferative potential.
Zhang et al., San Diego, United States. In Blood, 2012
PRMT1 interacts with AML1-ETO to promote its transcriptional activation and progenitor cell proliferative potential.
Upregulated protein arginine methyltransferase 1 by IL-4 increases eotaxin-1 expression in airway epithelial cells and participates in antigen-induced pulmonary inflammation in rats.
Lu et al., Xi'an, China. In J Immunol, 2012
PRMT1 was expressed in bronchus & alveolus epithelium & upregulated in lungs from AIPI rats. The inhibition of PRMT downregulated eotaxin-1 & CCR3 induction by IL-4 in epithelial cells. PRMT1 plays an important role in asthma pathogenesis.
[Construction and identification of human PRMT1 gene eukaryotic vector].
Lv et al., Xi'an, China. In Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi, 2012
Results idicate that pcDNA3.1(+)-PRMT1 recombinant was successfully constructed.
Protein arginine-methyltransferase-dependent oncogenesis.
So et al., London, United Kingdom. In Nat Cell Biol, 2007
Study uncovers an essential function of PRMTs in oncogenesis and reveals their potential as novel therapeutic targets in human cancer.
Human PAD4 regulates histone arginine methylation levels via demethylimination.
Coonrod et al., New York City, United States. In Science, 2004
PAD4 targets multiple sites in histones H3 and H4, including those sites methylated by coactivators CARM1 (H3 Arg17) and PRMT1 (H4 Arg3).
Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53.
Roeder et al., New York City, United States. In Cell, 2004
In an extension of previous studies showing a role for acetyltransferase p300/CBP in p53 function, we have used systems reconstituted with recombinant chromatin templates and (co)activators to demonstrate (1) the additional involvement of protein arginine methyltransferases PRMT1 and CARM1 in p53 function; (2) both independent and ordered cooperative functions of p300, PRMT1, and CARM1; and (3) mechanisms that involve direct interactions with p53 and, most importantly, obligatory modifications of corresponding histone substrates.
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