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The Overexpression of CARM1 Promotes Human Osteosarcoma Cell Proliferation through the pGSK3beta/beta-Catenin (show CTNNB1 Proteins)/cyclinD1 Signaling Pathway
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 Proteins) recruits steroid receptor coactivator (show SRA1 Proteins)-3 primary coactivator and secondary coactivators, p300/CBP (show CREBBP Proteins) 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 Proteins)) mimic sinefungin and three different peptide sequences from histone H3 (show HIST3H3 Proteins) and PABP1 (show PABPC1 Proteins) are presented, with both nonmethylated and singly methylated arginine residues exemplified.
CARM1 associates with major nonsense-mediated mRNA decay factor UPF1 (show UPF1 Proteins) 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
Study describes peptide-based transition state mimics that form stable complexes with CARM1 resulting in high-resolution co-crystal structures. The findings provide an exciting approach to understanding protein arginine methyltransferase (PRMT) substrate recognition and the regulation of arginine methylation.
CARM1 promotes EZH2 (show EZH2 Proteins)-mediated silencing of EZH2 (show EZH2 Proteins)/BAF155 (show SMARCC1 Proteins) target tumor suppressor genes by methylating BAF155 (show SMARCC1 Proteins).
These observations demonstrate that oxidative stress destabilizes PRMT4 via GSK-3beta 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 Proteins) at arginine 26 (H3R26), as an upstream regulator of Sox21 (show SOX21 Proteins) 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 Proteins)-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 Proteins) secretion from pancreatic beta cells via H3R17 methylation.
Data show that the methyltransferase CARM1 (coactivator-associated arginine methyltransferase 1; PRMT4) methylated Notch (show NOTCH1 Proteins) intracellular domain (NICD (show NOTCH1 Proteins)) at five conserved arginine residues.
we identify BAF155 (show SMARCC1 Proteins) as a substrate for arginine methyltransferase CARM1.
a combinatorial role of PRMT4/CARM1 and PRMT5 (show PRMT5 Proteins) 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