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Human PRMT5 Protein expressed in Wheat germ - ABIN1316333
Kanamaluru, Xiao, Fang, Choi, Kim, Veenstra, Kemper: Arginine methylation by PRMT5 at a naturally occurring mutation site is critical for liver metabolic regulation by small heterodimer partner. in Molecular and cellular biology 2011
The present study demonstrated that PRMT5 epigenetically silenced the expression of the tumor suppressor FBW7, leading to increased cMyc levels and the subsequent enhancement of the proliferation of and aerobic glycolysis in pancreatic cancer cells.
Inhibition of PRMT5 in B-cell lymphoma lines led to significant upregulation of BCL6 target genes, and the concomitant inhibition of both BCL6 and PRMT5 exhibited synergistic killing of BCL6-expressing lymphoma cells.
Studies suggest that the protein arginine N-methyltransferase 5 (PRMT5)/miR-99 family/fibroblast growth factor receptor 3 (FGFR3) axis in regulating lung cancer progression and identifies PRMT5 as a promising prognostic biomarker and therapeutic target.
Evidence for the importance of PRMT5 for the post-translational regulation of TDP1 and repair of topoisomerase I covalent complexes.
PRMT5 knockdown markedly inhibited in vitro HCC proliferation and in vivo tumorigenesis. Authors revealed that the mechanism of PRMT5-induced proliferation was partially mediated by BTG downregulation, leading to cell cycle arrest during the G1 phase in HCC cells.
LINC01138 interacts with PRMT5 to increase arginine methylation and protein stability of SREBP1, promoting lipid desaturation and cell proliferation in Clear cell renal cell carcinoma.
identified a LUBAC-independent role for SHARPIN in enhancing PRMT5 activity that contributes to melanomagenesis through the SKI/SOX10 regulatory axis.
curcumin affects the PRMT5-MEP50 methyltransferase expression might be explored for its therapeutic application.
High PRMT5 nuclear expression was also associated with higher nuclear liver kinase B1 (LKB1), suggesting that a functional relationship may occur. Consistently, several approaches provided evidence that PRMT5 and LKB1 interact directly in the cytoplasm of mammary epithelial cells.
CAPG competes with the transcriptional repressor arginine methyltransferase 5 (PRMT5) for binding to the STC-1 promoter.
The findings therefore indicate that Pb exposure increasing the PRMT5 expression might be one of the contributing epigenetic factors in the lead-mediated disease processes.
CARM1-mediated asymmetric methylation of PRMT5 is critical for its dimerization and methyltransferase activity leading to the repression of gamma-globin expression.
Study demonstrated that PRMT5 regulates OCT4/A, KLF4, and C-MYC in breast cancer to govern stemness and affects the doxorubicin resistance of breast cancer.
High PRMT5 expression is associated with glioblastoma.
Expression of PRMT5 was significantly increased in human gastric cancer (GC) tissues compared with normal gastric mucosa. Multiple evidences suggested that PRMT5 repressed transcription of tumor suppressor IRX1 via recruitment of DNMT3A on promoter.
PRMT5 may play a role from early oncogenesis through to the progression of oral squamous cell carcinoma , particularly in the aggressive mode of stromal invasion
he phosphorylation of the MP inhibitory MYPT1(T850) and the regulatory PRMT5(T80) residues as well as the symmetric dimethylation of H2A/4 were elevated in human hepatocellular carcinoma and in other types of cancers.
The polymerase-associated factor complex regulates Prmt5 to facilitate leukemic progression and is a potential therapeutic target for acute myeloid leukemias.
our results indicated that PRMT5 overexpression in hepatocellular carcinoma (HCC)and colon cancer cells contributed to their acquisition of aggressive characteristics, such as invasiveness, thus presenting a promising therapeutic target for the treatment of these diseases
PRMT5 as a key in vitro and in vivo regulator of breast cancer stem cells proliferation. PRMT5 epigenetically regulates FOXP1.
PRMT5 contributes to germinal center formation and affinity maturation at least in part through its direct interaction with and methylation of BCL6 at arginine 305 (R305), a modification necessary for the full transcriptional repressive effects of BCL6.
Prmt5 is necessary for antibody responses and has essential but distinct functions in all proliferative B cell stages in mice. Prmt5 is necessary for B cell development by preventing p53-dependent and p53-independent blocks in Pro-B and Pre-B cells, respectively.
Results indicate protein arginine N-methyltransferase 5 (PRMT5) as critical for oligodendrocyte differentiation and developmental myelination.
Targeting PRMT5 using small-molecule inhibitors in the treatment of leukemias harboring MLL rearrangements.
PRMT activity is selectively augmented during the initial activation of exercise-induced skeletal muscle remodeling in vivo.
OGG1 affects PRMT5 binding on histone H4 and the formation of dimethylation of histone H4 arginine-3 via PRMT5.
observed the progressive decrease in PRMT5 during oligodendrocyte differentiation
the present study increases our understanding of PRMT1, -4, and -5 biology during the plasticity of skeletal muscle development. Our results provide evidence for a role of PRMT1, via a mitochondrially mediated mechanism, in driving the muscle differentiation program.
the nuclear localized CA-VI B selectively promotes IL-12 expression by interaction with protein arginine N-methyltransferase 5 (PRMT5), which reduces symmetric dimethylation of histone H3 arginine 8 modification (H3R8me2s) at Il12 promoters to facilitate chromatin accessibility, selectively enhancing c-Rel binding to the Il12b promoter.
this study demonstrates for the first time that oncogenic stress orchestrates a p53-dependent response that is controlled by PRMT5-mediated arginine methylation and identifies the Fanconi anemia pathway as an integral part of this versatile cellular mechanism
PRMT5 is an osteoclastogenesis activator and PRMT5 inhibition suppresses osteoclast differentiation via downregulation of CXCL10 and RSAD2.
PRMT1 inhibition prevents gastric cancer progression by downregulating eIF4E and targeting type II PRMT5.
PRMT5 regulates internal ribosome entry site-dependent translation via methylation of hnRNP A1.
PRMT5 maintains progenitor cells through its regulation of Bmp4; adult and embryonic stem cells also require PRMT5 for maintaining pluripotency, suggesting that similar mechanisms might regulate lineage-restricted progenitor cells during organogenesis.
Menin and PRMT5 suppress GLP1R transcript levels and PKA-mediated phosphorylation of FOXO1 and CREB.
findings show that PRMT5 is an important modulator of CD4(+) T cell expansion; PRMT5 was transiently upregulated during maximal proliferation of mouse and human memory Th cells; data implicate PRMT5 in the regulation of adaptive memory Th cell responses
Prmt5 facilitates promoter-enhancer looping and gene expression at the PPARgamma2 locus, which encodes a critical lineage-determining factor that drives the differentiation of adipose tissue.
Taken together, our data reveal a pathophysiologically relevant role for PRMT5 in MHC II transactivation in macrophages
Prmt5 is required for germ cell survival during spermatogenesis in mice.
Prmt5 controls proliferation of adult muscle stem cells by direct epigenetic silencing of the cell cycle inhibitor p21.
a combinatorial role of PRMT4/CARM1 and PRMT5 for proper myogenesis in zebrafish
Data indicate that MEP50 WD repeat protein is essential for methylation of histones H4 and H2A by PRMT5 arginine methyltransferase.
data support a mechanism in which MEP50 binds substrate and stimulates PRMT5 activity modulated by substrate post-translational modifications
Protein arginine methyltransferase Prmt5-Mep50 methylates histones H2A and H4 and the histone chaperone nucleoplasmin in Xenopus laevis eggs
The results suggested that medaka Mep50 could be a partner of Prmt5 and might play major roles in a variety of tissues in medaka.
It show the morphological and functional phenotypes of single or double null alleles of prmt-5 in Caenorhabditis elegans. The prmt-1;prmt-5 double mutants are viable, and exhibit short body length and small brood size compared to N2 and each of the single mutants.
The PRMT-5 catalyzes the symmetric dimethylation of substrates containing monomethylarginine residues in vivo.
Analysis of prmt-5-deficient worms indicated that methylation promoted the dopamine-mediated modulation of chemosensory and locomotory behaviors through the DOP-3 receptor.
data confirm that MEP50 plays a key role in substrate recognition and activates PRMT5 activity by increasing its affinity for protein substrates.
the substrate specificity, processivity, and kinetic mechanism of bacterially expressed Caenorhabditis elegans PRMT5 (cPRMT5).
analysis of structural insights into protein arginine symmetric dimethylation by PRMT5
PRMT-5 represses CEP-1 transcriptional activity through CBP-1, which represents a novel regulatory mechanism of p53-dependent apoptosis.
Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3)\; such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. Plays a role in the assembly of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. May regulate the SUPT5H transcriptional elongation properties. May be part of a pathway that is connected to a chloride current, possibly through cytoskeletal rearrangement. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage. Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR\; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation. Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity (By similarity). Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation (By similarity). Methylates HOXA9 (By similarity).
72 kDa ICln-binding protein
, HMT1 hnRNP methyltransferase-like 5
, SKB1 homolog
, histone-arginine N-methyltransferase PRMT5
, jak-binding protein 1
, protein arginine N-methyltransferase 5
, shk1 kinase-binding protein 1 homolog
, protein arginine methyltransferase 5
, Jak-binding protein 1
, putative arginine N-methyltransferase, type II
, protein arginine methyltransferase
, protein arginine N-methyltransferase 5-like