gopubmed logo
 
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Protein arginine methyltransferase 5

PRMT5, Skb1, protein arginine methyltransferase 5, JBP1
Involved in vernalization. Required for epigenetic silencing of FLC, and for vernalization-mediated histone modification. (from NCBI)
Top mentioned proteins: Histone, CAN, H4, Protein-Arginine N-Methyltransferase, V1a
Papers on PRMT5
Small Molecule Inhibitors of Protein Arginine Methyltransferases.
New
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.
Arginine methylation of SREBP1a via PRMT5 promotes de novo lipogenesis and tumor growth.
New
Huang et al., Shanghai, China. In Cancer Res, Feb 2016
Mass spectrometry revealed protein arginine methyltransferase 5 (PRMT5) as a binding partner of SREBP1a that symmetrically dimethylated it on R321, thereby promoting transcriptional activity.
Expression of mep50 in adult and embryos of medaka fish (Oryzias latipes).
New
Zhao et al., Wuhan, China. In Fish Physiol Biochem, Feb 2016
Methylosome protein 50 (Mep50) is identified as a partner of protein arginine methyltransferase 5 (Prmt5), a major enzyme capable of symmetric dimethylation, in mammals and Xenopus.
SMN and symmetric arginine dimethylation of RNA polymerase II C-terminal domain control termination.
New
Impact
Greenblatt et al., Toronto, Canada. In Nature, Feb 2016
This R1810me2s modification requires protein arginine methyltransferase 5 (PRMT5) and recruits the Tudor domain of the survival of motor neuron (SMN, also known as GEMIN1) protein, which is mutated in spinal muscular atrophy.
MEP50/PRMT5 Reduces Gene Expression by Histone Arginine Methylation and this Is Reversed by PKCδ/p38δ Signaling.
New
Eckert et al., Baltimore, United States. In J Invest Dermatol, Jan 2016
Protein arginine methyltransferase 5 (PRMT5) is an arginine methyltransferase that symmetrically dimethylates arginine residues.
MYC regulates the core pre-mRNA splicing machinery as an essential step in lymphomagenesis.
New
Impact
Guccione et al., Singapore, Singapore. In Nature, Aug 2015
Here we show that during lymphomagenesis in Eµ-myc transgenic mice, MYC directly upregulates the transcription of the core small nuclear ribonucleoprotein particle assembly genes, including Prmt5, an arginine methyltransferase that methylates Sm proteins.
The PRMT5 arginine methyltransferase: many roles in development, cancer and beyond.
Review
New
Shechter et al., Anchorage, United States. In Cell Mol Life Sci, Jun 2015
The protein arginine methyltransferase 5 (PRMT5, also known as Hsl7, Jbp1, Skb1, Capsuleen, or Dart5) is the major enzyme responsible for mono- and symmetric dimethylation of arginine.
PRMT5 Is Upregulated in HTLV-1-Mediated T-Cell Transformation and Selective Inhibition Alters Viral Gene Expression and Infected Cell Survival.
Green et al., Columbus, United States. In Viruses, 2014
Herein, we examined the role of protein arginine methyltransferase 5 (PRMT5) on HTLV-1-mediated cellular transformation and viral gene expression.
Protein arginine methyltransferase 5 is essential for growth of lung cancer cells.
GeneRIF
Wang et al., Houston, United States. In Biochem J, 2012
Data suggest that PRMT5 is highly expressed in lung cancer cells; PRMT5 expression is not detectable in benign lung tissues. Silencing PRMT5 expression strongly inhibits proliferation of lung adenocarcinoma cells in culture and in a xenograft model.
Protein arginine methyltransferase 5 is a potential oncoprotein that upregulates G1 cyclins/cyclin-dependent kinases and the phosphoinositide 3-kinase/AKT signaling cascade.
GeneRIF
Yu et al., Taiwan. In Cancer Sci, 2012
Protein arginine methyltransferase 5 is a potential oncoprotein that upregulates G1 cyclins/cyclin-dependent kinases and the phosphoinositide 3-kinase/AKT signaling cascade.
HOXA9 methylation by PRMT5 is essential for endothelial cell expression of leukocyte adhesion molecules.
GeneRIF
Dicorleto et al., Cleveland, United States. In Mol Cell Biol, 2012
HOXA9 is required for TNF-alpha-dependent binding of PRMT5 to the E-selectin promoter in endothelial cells.
Protein arginine methyltransferase 5 (Prmt5) promotes gene expression of peroxisome proliferator-activated receptor γ2 (PPARγ2) and its target genes during adipogenesis.
GeneRIF
Imbalzano et al., Worcester, United States. In Mol Endocrinol, 2012
Prmt5 acts as a coactivator for the activation of adipogenic gene expression and promotes adipogenic differentiation.
Evolutionarily conserved protein arginine methyltransferases in non-mammalian animal systems.
Review
Li et al., T'ai-chung-shih, Taiwan. In Febs J, 2012
We show the conservation of the most typical type I PRMT1 and type II PRMT5 in all of the species examined, the wide yet different distribution of PRMT3, 4 and 7 in non-mammalian animals, the vertebrate-restricted distribution of PRMT8 and the special reptile/avian-deficient distribution of PRMT2 and 6.
Disordered epigenetic regulation in the pathophysiology of myeloproliferative neoplasms.
Review
Abdel-Wahab et al., New York City, United States. In Curr Hematol Malig Rep, 2012
In addition to mutation, alterations in the expression or activity of chromatin-modifying/reading proteins PRMT5 and L3MBTL1 have been found to be important in MPN development.
Protein arginine methyltransferase 5 is an essential component of the hypoxia-inducible factor 1 signaling pathway.
GeneRIF
Park et al., Seoul, South Korea. In Biochem Biophys Res Commun, 2012
PRMT5 probably promotes tumor growth by stimulating cell proliferation and by participating in the construction of a tumor-favorable microenvironment via HIF-1 activation.
Versatility of PRMT5-induced methylation in growth control and development.
Review
GeneRIF
Sif et al., Columbus, United States. In Trends Biochem Sci, 2011
The results not only provide insight into the molecular mechanisms by which PRMT5 contributes to growth control, but also justify therapeutic targeting of PRMT5.
Alternative splicing at the right time.
Review
GeneRIF
Yanovsky et al., Buenos Aires, Argentina. In Rna Biol, 2011
Studies indicate that protein arginine methyltransferase 5 (PRMT5) plays a role in circadian clocks regulated alternative splicing process.
JAK2V617F-mediated phosphorylation of PRMT5 downregulates its methyltransferase activity and promotes myeloproliferation.
Impact
GeneRIF
Nimer et al., New York City, United States. In Cancer Cell, 2011
results indicate that phosphorylation of PRMT5 contributes to the mutant JAK2-induced myeloproliferative phenotype
HiJAKing the methylosome in myeloproliferative disorders.
Impact
Schwaller et al., Basel, Switzerland. In Cancer Cell, 2011
(2011) demonstrate that these JAK2 mutants, but not wild-type JAK2, directly phosphorylate PRMT5 and inhibit its arginine methyltransferase activity, establishing a link between mutant JAK2 and histone arginine methylation.
Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation negatively modulates EGFR-mediated ERK activation.
Impact
Hung et al., Houston, United States. In Nat Cell Biol, 2011
Here, we show that EGFR Arg 1175 is methylated by an arginine methyltransferase, PRMT5.
share on facebooktweetadd +1mail to friends