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metabolism
tamoxifen treatment induces a decrease in the enzyme (PRMT2) and an increase in ER-alpha36 as well as ER-alpha36-mediated non-genomic effect in MDA-MB-231 cells, which are relatively resistant to tamoxifen by contrast to MCF-7 cells. PRMT2 is able to interact with ER-alpha36 directly, suppress ER-alpha36 and downstream PI3K/Akt and MAPK/ERK signaling, reversing the tamoxifen resistance of breast cancer cells
drug target
given the dual functions of PRMT1 (promotion of migration and invasion and inhibition of proliferation in gastric cancer cells), it is a potential drug target of gastric cancer with extreme caution
drug target
investigation of the role of the enzyme (PRMT2) in breast cancer progression and for developing a new endocrine therapeutic strategy for breast cancer patients with tamoxifen resistance
drug target
PRMT6 is overexpressed in several cancer types and is therefore considered as a potential anti-cancer drug target
drug target
protein arginine N-methyltransferase 1 expression is significantly upregulated in hepatocellular carcinoma cell lines and clinical tissues. Downregulation of protein arginine N-methyltransferase 1 in hepatocellular carcinoma cells by small interfering RNA could inhibit cell proliferation, migration, and invasion in vitro. The enzyme may contribute to hepatocellular carcinoma progression and serves as a promising target for the treatment of hepatocellular carcinoma patients
drug target
the enzme is associated with several human cancers including breast, colon, prostate and lung cancers and thus, is a potential oncological target
drug target
the enzyme (PRMT1) is a promising target for the treatment of cancer
malfunction
disruption of CARM1 enhances the nuclear retention of mRNAs containing inverted repeated Alu elements (IRAlus)
malfunction
knockdown of PRMT1 reverses epithelial-mesenchymal transition in HCC cell lines and inhibits the proliferation of HepG2 and Hep3B cells
malfunction
loss of Carm1 leads to a low sperm count and deformed sperm heads that can be attributed to defective elongation of round spermatids. RNA-seq analysis of Carm1-null spermatids reveals that the deregulated genes fell into similar categories as those impacted by p300-loss, thus providing a link between Carm1 and p300 (a major Carm1 substrate). CREMtau, a key testis-specific transcription factor, associates with p300 through its activator, ACT. This interaction is negatively regulates by the methylation of p300 by Carm1. Thus, high nuclear Carm1 levels negatively impact the p300/ACT/CREMtau axis during late stages of spermiogenesis
malfunction
Prmt1 ablation in adipocytes impairs thermogenic activation induced by cold exposure or beta3-adrenergic stimulation. Loss of enzyme (PRMT1) in mature adipocytes does not affect adipose tissue function at basal level. Loss of PRMT1 or overexpression of PRMT1 does not affect adipogenesis in fat cells
malfunction
PRMT6-deficient mice exhibit enhanced antiviral innate immunity. PRMT6 deficiency promotes the TBK1-IRF3 interaction and subsequently enhances IRF3 activation and type-I interferon production
malfunction
the null mutant of Caenorhabditis elegans prmt-1 is viable with no severe phenotype, despite loss of asymmetric arginine dimethylation
physiological function
arginine methyltransferases type II PRMT5 and type I PRMT4 mutants show similar alterations in flowering time, photomorphogenic responses and salt stress tolerance, while only prmt5 mutants exhibits alterations in circadian rhythms. PRMT5 and PRMT4s coregulate the expression and splicing of key regulatory genes associated with transcription, RNA processing, responses to light, flowering, and abiotic stress tolerance
physiological function
disruption of gene expression does not result in a significant growth defect in procyclic form Trypanosoma brucei. Isoform PRMT1 knock down leads to a dramatic decrease in the cellular level of asymmetric dimethylarginine
physiological function
knockdown of isoform PRMT1 results in delayed growth, shortened body-length, curled tails and cardiac edema. PRMT1 protein level, type I protein arginine methyltransferase activity, specific asymmetric protein arginine methylation and histone H4 R3 methylation all decreased in the knockdown mutants. The mutants show defective convergence and extension and the abnormalities are more severe at the posterior than the anterior parts. Cell migration defects are observed in the mutant embryos
physiological function
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knockdown of isoform PRMT1 results in increased Smurf2 expression as well as inhibition of TGF-beta-mediated reporter activity
physiological function
knockdown of isoform PRMT6 in both procyclic form and bloodstream form Trypanosoma brucei leads to a modest but reproducible effect on parasite growth in culture. Upon PRMT6 depletion, both procyclic form and bloodstream form exhibit aberrant morphologies indicating defects in cell division, and these defects differ in the two life cycle stages. PRMT6-associated proteins are histones, components of the nuclear pore complex, and flagellar proteins
physiological function
PRMT1 contributes the major type I protein arginine methyltransferase enzyme activity present in mammalian cells and tissues
physiological function
similar to H2O2 treatment, isoforms PRMT1 or PRMT4 overexpression increases retinal pigment epithelial cell damage. The H2O2-induced cell damage is attenuated by PRMT1 or PRMT4 knockdown and sirtuin SIRT1 overexpression
physiological function
similar to H2O2 treatment, isoforms PRMT1 or PRMT4 overexpression increases retinal pigment epithelial cell damage. The H2O2-induced cell damage is attenuated by PRMT1 or PRMT4 knockdown and sirtuin SIRT1 overexpression. SIRT1 expression is regulated by PRMT1
physiological function
a splicing isoform is characterized which does not affect the amino-terminus of the protein like the seven known isoforms, but rather lacks exons 8 and 9 which encode the dimerization arm of the enzyme that is essential for enzymatic activity. Consequently, the isoform does not form catalytically active oligomers with the other endogenous PRMT1 isoforms. This isoform is found in a variety of cell lines, but is increased in cell lines of cancer origin or after expression of the EMT-inducing transcriptional repressor Snail1. The novel isoform could act as a modulator of PRMT1 activity in cancer cells by acting as a competitive inhibitor that shields substrates from access to active PRMT1 oligomers
physiological function
dysregulation of PRMT1 is involved in a diverse range of diseases, including cancer
physiological function
enzyme (PRMT1) plays a regulatory role in thermogenic fat function
physiological function
important roles of the enzyme (PRMT1) in progression of gastric cancer. The enzyme is up-regulated and promotes migration, invasion and proliferation in wide range of cancers. PRMT1 promotes migration and invasion and inhibits proliferation in gastric cancer cells,whereas PRMT1 knockdown reverses the above abilities. PRMT1 reduces the expression of epithelial marker E-cadherin and increases the expression of mesenchymal markers including N-cadherin, Vimentin, snail and beta-catenin in gastric cancer cells. PRMT1 silencing promotes the phosphorylation of LATS1, and then induces YAP phosphorylation, while overexpression of PRMT1 down-regulates the phosphorylation of LATS1 and YAP, indicating that PRMT1 inhibits EMT probably via Hippo signaling
physiological function
overexpression or dysregulation of PRMT1 is associated with many diseases, particularly cancer
physiological function
PRMT1 expression, localization, and activity are altered following denervation-induced inactivity. Evidence from correlation, colocalization, and interaction analyses strongly support the existence of a novel, functional PRMT1-AMPKPGC-1alpha axis in skeletal muscle that is active during phenotypic remodeling elicited by denervation-evoked atrophy
physiological function
PRMT1 plays a regulatory role in thermogenic fat function
physiological function
PRMT2 is involved in a variety of cellular processes and has diverse roles in transcriptional regulation through different mechanisms depending on its binding partners
physiological function
PRMT2 is involved in a variety of cellular processes and has diverse roles in transcriptional regulation through different mechanisms depending on its binding partners
physiological function
PRMT4 expression, localization, and activity are altered following denervation-induced inactivity
physiological function
PRMT5 and PRMT1 are involved in the interaction between CFLARL (a CASP8 and FADD-like apoptosis regulator) and the E3 ligase ITCH. The PRMT5 silencing and PRMT1 overexpression enhance the interaction between CFLARL and ITCH, leading to an altered ubiquitination level and, eventually, the degradation of CFLARL
physiological function
protein arginine methyltransferase 4 (PRMT4) is an essential epigenetic regulator of fundamental and conserved processes during vertebrate development, such as pluripotency and differentiation
physiological function
the enzyme (CARM1) functions as a coactivator for various proteins that have been linked to cancer such as p53, NF-kappabeta, beta-catenin, E2F1 and steroid hormone receptor ERalpha. CARM1 is involved in transcriptional activation, cellular differentiation, cell cycle progression, RNA splicing and DNA damage response
physiological function
the enzyme (CARM1) is firmly implicated in transcriptional regulation
physiological function
the enzyme (CARM1) regulates this nuclear retention pathway at two levels: CARM1 methylates the coiled-coil domain of p54nrb, resulting in reduced binding of p54nrb to mRNAs containing inverted repeated Alu elements (IRAlus), and also acts as a transcription regulator to suppress NEAT1 transcription, leading to reduced paraspeckle formation. These actions of CARM1 work together synergistically to regulate the export of transcripts containing IRAlus from paraspeckles under certain cellular stresses, such as poly(I:C) treatment
physiological function
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the enzyme (PRMT1) is important for cell division and growth. The enzyme (PRMT1) is a significant contributor to arginine monomethylation in Toxoplasma gondii
physiological function
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the enzyme (PRMT1) methylate a number of key proteins and alters the transcription of a variety of genes involved in developmental processes. Appropriate levels of expression of type I PRMTs are necessary for the proper growth and development of Eucalyptus grandis roots. The enzyme (PRMT1) has a key role in root hair initiation and elongation and is involved in the methylation of beta-tubulin, a key protein in cytoskeleton formation
physiological function
the enzyme (PRMT1) represses MHC II transcription in macrophages by methylating Class II transactivator (CIITA)
physiological function
the enzyme (PRMT6) attenuates antiviral innate immunity by blocking TBK1-IRF3 signaling. Mechanistically, viral infection enhances the binding of PRMT6 to IRF3 and inhibited the interaction between IRF3 and TBK1. This mechanism is independent of PRMT6 methyltransferase activity
physiological function
the enzyme (PRMT6) is a protein arginine methyltransferase involved in transcriptional regulation, human immunodeficiency virus pathogenesis, DNA base excision repair, and cell cycle progression
physiological function
the enzyme catalyzes asymmetric arginine dimethylation of cellular proteins and thus modulates various biological processes, including gene regulation, RNA metabolism, cell signaling and DNA repair
physiological function
the enzyme is associated with various diseases including cancers
physiological function
the enzyme is involved in a variety of processes including transcription, DNA repair, and signal transduction
physiological function
the enzyme plays a critical role in the regulation of encystation
physiological function
the protein arginine methyltransferases 1 and 5 affect Myc properties in glioblastoma stem cells. Myc associates with both PRMT1 and PRMT5 being differentially dimethylated. Symmetric (S) by PRMT1 dimethylation protects Myc from degradation, while asymmetric (AS) dimethylation by PRMT5 allows Myc proper turnover. We hypothesize S-Myc as typical of aggressive glioblastoma stem cells, as S-Myc/AS-Myc ratio decreases in differentiating, less aggressive, cells
physiological function
via a mitochondrially mediated mechanism, the enzyme (PRMT1) is involved in driving the muscle differentiation program
physiological function
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
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disruption of gene expression does not result in a significant growth defect in procyclic form Trypanosoma brucei. Isoform PRMT1 knock down leads to a dramatic decrease in the cellular level of asymmetric dimethylarginine
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physiological function
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
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knockdown of isoform PRMT6 in both procyclic form and bloodstream form Trypanosoma brucei leads to a modest but reproducible effect on parasite growth in culture. Upon PRMT6 depletion, both procyclic form and bloodstream form exhibit aberrant morphologies indicating defects in cell division, and these defects differ in the two life cycle stages. PRMT6-associated proteins are histones, components of the nuclear pore complex, and flagellar proteins
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