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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Protein arginine methyltransferase 6

PRMT6, protein arginine methyltransferase 6
The protein encoded by this gene belongs to the arginine N-methyltransferase family, which catalyze the sequential transfer of methyl group from S-adenosyl-L-methionine to the side chain nitrogens of arginine residues within proteins, to form methylated arginine derivatives and S-adenosyl-L-homocysteine. This protein can catalyze both, the formation of omega-N monomethylarginine and asymmetrical dimethylarginine, with a strong preference for the latter. It specifically mediates the asymmetric dimethylation of Arg2 of histone H3, and the methylated form represents a specific tag for epigenetic transcriptional repression. This protein also forms a complex with, and methylates DNA polymerase beta, resulting in stimulation of polymerase activity by enhancing DNA binding and processivity. [provided by RefSeq, Sep 2011] (from NCBI)
Top mentioned proteins: Histone, Protein-Arginine N-Methyltransferase, CAN, CARM1, fibrillin-1
Papers on PRMT6
The protein arginine methyltransferase PRMT6 inhibits HIV-1 Tat nucleolar retention.
Jans et al., Australia. In Biochim Biophys Acta, Feb 2016
Here we show for the first time that Tat localisation can be modulated by specific methylation, whereby overexpression of active but not catalytically inactive PRMT6 methyltransferase specifically leads to exclusion of Tat from the nucleolus.
Protein Arginine Methyltransferase 6 (Prmt6) Is Essential for Early Zebrafish Development through the Direct Suppression of gadd45αa Stress Sensor Gene.
Li et al., Shanghai, China. In J Biol Chem, Feb 2016
H3R2me2a, generated by protein arginine methyltransferase 6 (Prmt6), is a repressive mark.
A Potent, Selective, and Cell-Active Inhibitor of Human Type I Protein Arginine Methyltransferases.
Jin et al., Toronto, Canada. In Acs Chem Biol, Jan 2016
A crystal structure of PRMT6 in complex with MS023 revealed that MS023 binds the substrate binding site.
PRMT6 increases cytoplasmic localization of p21CDKN1A in cancer cells through arginine methylation and makes more resistant to cytotoxic agents.
Hamamoto et al., Chicago, United States. In Oncotarget, Nov 2015
Here we demonstrate that protein arginine methyltransferase 6 (PRMT6) methylates p21 at arginine 156 and promotes phosphorylation of threonine 145 on p21, resulting in the increase of cytoplasmic localization of p21.
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.
pUL69 of Human Cytomegalovirus Recruits the Cellular Protein Arginine Methyltransferase 6 via a Domain That Is Crucial for mRNA Export and Efficient Viral Replication.
Stamminger et al., Erlangen, Germany. In J Virol, Sep 2015
Second, we observed a specific electrophoretic mobility shift upon overexpression of the catalytically active protein arginine methyltransferase 6 (PRMT6).
Functional insights from high resolution structures of mouse protein arginine methyltransferase 6.
Cavarelli et al., Illkirch-Graffenstaden, France. In J Struct Biol, Aug 2015
PRMT6 is a protein arginine methyltransferase involved in transcriptional regulation, human immunodeficiency virus pathogenesis, DNA base excision repair, and cell cycle progression.
Exchange Factor TBL1 and Arginine Methyltransferase PRMT6 Cooperate in Protecting G Protein Pathway Suppressor 2 (GPS2) from Proteasomal Degradation.
Perissi et al., Montréal, Canada. In J Biol Chem, Aug 2015
Unexpectedly, interaction with the exchange factor TBL1 is required to protect GPS2 from degradation, with methylation of GPS2 by arginine methyltransferase PRMT6 regulating the interaction with TBL1 and inhibiting proteasome-dependent degradation.
Aryl Pyrazoles as Potent Inhibitors of Arginine Methyltransferases: Identification of the First PRMT6 Tool Compound.
Copeland et al., Cambridge, United States. In Acs Med Chem Lett, Jul 2015
Synthesis of analogues within this series yielded the first potent, selective, small molecule PRMT6 inhibitor tool compound, EPZ020411.
A novel BLAST-Based Relative Distance (BBRD) method can effectively group members of protein arginine methyltransferases and suggest their evolutionary relationship.
Li et al., T'ai-chung-shih, Taiwan. In Mol Phylogenet Evol, Mar 2015
The tree placed the uncharacterized PRMT9 with PRMT7 in the same clade, outside of all the Type I PRMTs including PRMT1 and its vertebrate paralogue PRMT8, PRMT3, PRMT6, PRMT2 and PRMT4.
Protein arginine methyltransferase 6 enhances polyglutamine-expanded androgen receptor function and toxicity in spinal and bulbar muscular atrophy.
Pennuto et al., Genova, Italy. In Neuron, Feb 2015
We show here that protein arginine methyltransferase 6 (PRMT6) is a specific co-activator of normal and mutant AR and that the interaction of PRMT6 with AR is significantly enhanced in the AR mutant.
Protein Arginine Methyltransferase 6 Involved in Germ Cell Viability during Spermatogenesis and Down-Regulated by the Androgen Receptor.
Gui et al., Shantou, China. In Int J Mol Sci, 2014
In this study, we found that the expression levels of Prmt6 mRNA and protein were significantly up-regulated in the testes of ARKO mice compared to wild type (WT) mice.
Contributions of the histone arginine methyltransferase PRMT6 to the epigenetic function of RUNX1.
Lausen, Frankfurt am Main, Germany. In Crit Rev Eukaryot Gene Expr, 2012
In this article, the recent observation that RUNX1 is associated with the protein arginine methyltransferase 6 will be reviewed.
Protein arginine methyltransferase 6-dependent gene expression and splicing: association with breast cancer outcomes.
Muscat et al., Brisbane, Australia. In Endocr Relat Cancer, 2012
dysregulation of PRMT6-dependent transcription and alternative splicing may be involved in breast cancer pathophysiology and the molecular consequences identifying a unique and informative biomarker profile.
Kinetic mechanism of protein arginine methyltransferase 6 (PRMT6).
Thompson et al., Jupiter, United States. In J Biol Chem, 2012
the molecular mechanisms of PRMT catalysis
A genome-wide association study in Chinese men identifies three risk loci for non-obstructive azoospermia.
Sha et al., Nanjing, China. In Nat Genet, 2012
The combined analyses identified significant (P < 5.0 × 10(-8)) associations between NOA risk and common variants near PRMT6 (rs12097821 at 1p13.3: odds ratio (OR) = 1.25, P = 5.7 × 10(-10)), PEX10 (rs2477686 at 1p36.32: OR = 1.39,
Dysregulation of PRMT1 and PRMT6, Type I arginine methyltransferases, is involved in various types of human cancers.
Hamamoto et al., Tokyo, Japan. In Int J Cancer, 2011
PRMT6 may be involved in human carcinogenesis and may thus be a therapeutic target for various types of cancer.
Förster resonance energy transfer measurements of cofactor-dependent effects on protein arginine N-methyltransferase homodimerization.
Frankel et al., Vancouver, Canada. In Protein Sci, 2010
In this study, we use Forster resonance energy transfer (FRET) to determine dissociation constant (K(D)) values for dimerization of PRMT1 and PRMT6.
Thrombospondin-1 is a transcriptional repression target of PRMT6.
Richard et al., Montréal, Canada. In J Biol Chem, 2009
TSP-1 is a transcriptional repression target of PRMT6
Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive.
Amati et al., Milano, Italy. In Nature, 2007
the arginine methyltransferase PRMT6 catalyses H3R2 di-methylation in vitro and controls global levels of H3R2me2a in vivo
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