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The CARM1-PKM2 axis serves as a metabolic reprogramming mechanism in tumorigenesis.
Arginine (di)methylated human leukocyte antigen class I peptides, which are asymmetrically dimethylated, most likely by CARM1, are favorably presented by HLA-B*07.
Estrogen receptor (show ESR1 ELISA Kits) recruits steroid receptor coactivator (show SRA1 ELISA Kits)-3 primary coactivator and secondary coactivators, p300/CBP (show CREBBP ELISA Kits) and CARM1 to regulate genetic transcription.
Arginine methylation of MDH1 by CARM1 regulates cellular redox homeostasis and suppresses glutamine metabolism of pancreatic cancer.
Here, the crystal structures of human CARM1 with the S-adenosylmethione (SAM (show TTN ELISA Kits)) mimic sinefungin and three different peptide sequences from histone H3 (show HIST3H3 ELISA Kits) and PABP1 (show PABPC1 ELISA Kits) are presented, with both nonmethylated and singly methylated arginine residues exemplified.
CARM1 associates with major nonsense-mediated mRNA decay factor UPF1 (show UPF1 ELISA Kits) and promotes its occupancy on premature terminating codon-containing transcripts in spinal muscular atrophy.
Monitoring of the CARM1-dependent production of monomethylated and dimethylated peptides over time by self-assembled monolayer and matrix-assisted laser desorption ionization mass spectrometry revealed that methylation by CARM1 is distributive.
no obvious association of CARM1 isoform expression and clinical correlates in breast cancer
disruption of CARM1 enhances the nuclear retention of mRNAs containing IRAlus
Data indicate that coactivator-associated arginine methyltransferase 1 (CARM1) regulates neural differentiation through Nanog homeobox (show NANOG ELISA Kits) protein and microRNA miR92a.
These observations demonstrate that oxidative stress destabilizes PRMT4 via GSK-3beta (show GSK3b ELISA Kits) signaling to impede lung epithelial cell migration that may hinder the lung repair and regeneration process.
AMPK deficiency results in nuclear CARM1 decrease mediated in part by SKP2, contributing to autophagy dysfunction in the aged heart.
Study identifies CARM1, which methylates histone H3 (show HIST3H3 ELISA Kits) at arginine 26 (H3R26), as an upstream regulator of Sox21 (show SOX21 ELISA Kits) expression. These results indicate that heterogeneity in gene expression patterns biases cell fate in the mouse embryo as early as the 4-cell stage.
findings demonstrate that CARM1-dependent histone arginine methylation is a crucial nuclear event in autophagy, and identify a new signalling axis of AMPK (show PRKAA1 ELISA Kits)-SKP2-CARM1 in the regulation of autophagy induction after nutrient starvation
CARM1 haploinsufficiency impairs transdifferentiation and wound healing in a mouse model.
PRMT4 might be a key regulator of high-glucose-induced insulin (show INS ELISA Kits) secretion from pancreatic beta cells via H3R17 methylation.
Data show that the methyltransferase CARM1 (coactivator-associated arginine methyltransferase 1; PRMT4) methylated Notch (show NOTCH1 ELISA Kits) intracellular domain (NICD (show NOTCH1 ELISA Kits)) at five conserved arginine residues.
we identify BAF155 (show SMARCC1 ELISA Kits) as a substrate for arginine methyltransferase CARM1.
Arginine methylation of Pax7 (show PAX7 ELISA Kits) by Carm1 functions as a molecular switch controlling the epigenetic induction of Myf5 (show MYF5 ELISA Kits) during satellite stem cell asymmetric division and entry into the myogenic program.
CARM1 is a key epigenetic regulator of hematopoiesis that affects multiple lineages at various stages of differentiation.
a combinatorial role of PRMT4/CARM1 and PRMT5 (show PRMT5 ELISA Kits) for proper myogenesis in zebrafish
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
histone-arginine methyltransferase CARM1
, protein arginine N-methyltransferase 4
, coactivator-associated arginine methyltransferase 1
, protein arginine methyltransferase