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

Coactivator-associated arginine methyltransferase 1

CARM1, coactivator-associated arginine methyltransferase 1, PRMT4
Protein arginine N-methyltransferases, such as CARM1, catalyze the transfer of a 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. Protein arginine methylation has been implicated in signal transduction, metabolism of nascent pre-RNA, and transcriptional activation (Frankel et al., 2002 [PubMed 11724789]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: Histone, Protein-Arginine N-Methyltransferase, CAN, p300, CBP
Papers using CARM1 antibodies
Techniques in protein methylation
Asahara Hiroshi et al., In BMC Developmental Biology, 2003
... Generation and characterization of v5-CARM1 transgenic mice ...
Papers on CARM1
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.
A novel role for CARM1 in promoting nonsense-mediated mRNA decay: potential implications for spinal muscular atrophy.
Côté et al., Ottawa, Canada. In Nucleic Acids Res, Jan 2016
We previously uncovered that Coactivator-Associated Methyltransferase-1 (CARM1) is abnormally up-regulated in SMA, leading to mis-regulation of a number of transcriptional and alternative splicing events.
MED12 methylation by CARM1 sensitizes human breast cancer cells to chemotherapy drugs.
Xu et al., Madison, United States. In Sci Adv, Oct 2015
We identified MED12 as a substrate for coactivator-associated arginine methyltransferase 1 (CARM1).
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.
PRMT1 and PRMT4 Regulate Oxidative Stress-Induced Retinal Pigment Epithelial Cell Damage in SIRT1-Dependent and SIRT1-Independent Manners.
Park et al., Kwangju, South Korea. In Oxid Med Cell Longev, 2014
H2O2 treatment increased PRMT1 and PRMT4 expression but decreased SIRT1 expression.
Transcriptome profiling of bovine inner cell mass and trophectoderm derived from in vivo generated blastocysts.
Sirard et al., Eşfahān, Iran. In Bmc Dev Biol, 2014
Moreover, a great majority of genes that were found to be misregulated following in vitro culture of bovine embryos were known genes involved in epigenetic regulation of pluripotency and cell differentiation including DNMT1, GADD45, CARM1, ELF5 HDAC8, CCNB1, KDM6A, PRDM9, CDX2, ARID3A, IL6, GADD45A, FGFR2, PPP2R2B, and SMARCA2.
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.
CARM1 methylates chromatin remodeling factor BAF155 to enhance tumor progression and metastasis.
Xu et al., Madison, United States. In Cancer Cell, 2014
Coactivator-associated arginine methyltransferase 1 (CARM1), a coactivator for various cancer-relevant transcription factors, is overexpressed in breast cancer.
CARMA: CARM1 methylation of SWI/SNF in breast cancer.
Roberts et al., Boston, United States. In Cancer Cell, 2014
In this issue of Cancer Cell, Wang and colleagues report that CARM1, a protein arginine methyltransferase, specifically methylates BAF155/SMARCC1, a core subunit of the SWI/SNF chromatin remodeling/tumor suppressor complex.
Identification of 15 new psoriasis susceptibility loci highlights the role of innate immunity.
Trembath et al., Ann Arbor, United States. In Nat Genet, 2012
Notably, they included candidate genes whose products are involved in innate host defense, including interferon-mediated antiviral responses (DDX58), macrophage activation (ZC3H12C) and nuclear factor (NF)-κB signaling (CARD14 and CARM1).
CARM1/PRMT4 is necessary for the glycogen gene expression programme in skeletal muscle cells.
Muscat et al., Brisbane, Australia. In Biochem J, 2012
PRMT4 is necessary for selective control of a specific gene expression program associated with glycogen metabolism.
Roles of protein arginine methylation in DNA damage signaling pathways is CARM1 a life-or-death decision point?
Stallcup et al., United States. In Cell Cycle, 2011
Signal transduction in cell death and survival involves a role for CARM1 in arginine methylation.
A coactivator role of CARM1 in the dysregulation of β-catenin activity in colorectal cancer cell growth and gene expression.
Stallcup et al., Los Angeles, United States. In Mol Cancer Res, 2011
A coactivator role of CARM1 in the dysregulation of beta-catenin activity in colorectal cancer cell growth and gene expression
The C-terminal domain of RNA polymerase II is modified by site-specific methylation.
Reinberg et al., New York City, United States. In Science, 2011
Here, we show that the CTD of RNAPII is methylated at a single arginine (R1810) by the coactivator-associated arginine methyltransferase 1 (CARM1).
The methyltransferases PRMT4/CARM1 and PRMT5 control differentially myogenesis in zebrafish.
Vandel et al., Toulouse, France. In Plos One, 2010
a combinatorial role of PRMT4/CARM1 and PRMT5 for proper myogenesis in zebrafish
CARM1 mediates modulation of Sox2.
Shen et al., Beijing, China. In Plos One, 2010
found that CARM1 facilitates Sox2-mediated transactivation and directly methylates Sox2 at arginine 113
Protein methylation: a new mechanism of p53 tumor suppressor regulation.
Chen et al., Davis, United States. In Histol Histopathol, 2008
Finally, protein arginine methyltransferases CARM1 and PRMT1 are co-activators of p53 involved in the methylation of histones H3 and H4 to facilitate p53-mediated transcription.
Vitamin D: molecular mechanism of action.
Joshi et al., Newark, United States. In Ann N Y Acad Sci, 2007
In our laboratory we have identified various factors that cooperate with the vitamin D receptor in regulating 24(OH)ase expression including C/EBP beta, SWI/SNF (complexes that remodel chromatin using the energy of ATP hydrolysis) and the methyltransferases, CARM1 and G9a.
Histone arginine methylation regulates pluripotency in the early mouse embryo.
Zernicka-Goetz et al., Cambridge, United Kingdom. In Nature, 2007
We confirm this prediction by overexpressing the H3-specific arginine methyltransferase CARM1 in individual blastomeres and show that this directs their progeny to the ICM and results in a dramatic upregulation of Nanog and Sox2.
Bile salt excretory pump: biology and pathobiology.
Ananthanarayanan et al., New York City, United States. In J Pediatr Gastroenterol Nutr, 2006
We have recently demonstrated a role for the coactivator-associated arginine methyltransferase 1 (CARM1), as a coactivator of the FXR/RXR receptor and regulator of FXR responsive genes such as BSEP.
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