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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
Data suggest that the protein arginine methyltransferase 5 (PRMT5)-E2F1 transcription factor (E2F-1 (show E2F1 Proteins)) pathway may act as a common target for exogenous lectins including Anguilla japonica lectin 1 (AJL1), and the cellular response to exogenous AJL1 may suggest a novel agent for cancer gene therapy.
These results could be helpful in discovering new potent and specific inhibitors of PRMT5, as well as in designing mutant residue assay to modulate the catalytic activity of PRMT5.
PRMT1 (show PRMT1 Proteins) inhibition prevents gastric cancer progression by downregulating eIF4E (show EIF4E Proteins) and targeting type II PRMT5.
Data indicate that ZNF326 (show ZNF326 Proteins) is an interaction partner and substrate of the PRMT5/WDR77 (show WDR77 Proteins) complex.
ERG (show ERG Proteins) signaling in prostate cancer is driven through PRMT5-dependent methylation of the androgen receptor (show AR Proteins).
SFN (show SFN Proteins) treatment of tumors results in reduced MEP50 (show WDR77 Proteins) level and H4R3me2s formation, confirming that that SFN (show SFN Proteins) impacts this complex in vivo. These studies suggest that the PRMT5/MEP50 (show WDR77 Proteins) is required for tumor growth and that reduced expression of this complex is a part of the mechanism of SFN (show SFN Proteins) suppression of tumor formation.
High nuclear PRMT5 expression is associated with oropharyngeal squamous cell carcinoma.
High PRMT5 expression is associated with prostate cancer.
Results provide evidence that PRMT5 and p44 regulate gene expression of growth and anti-growth factors to promote lung tumorigenesis.
PRMT5 regulates internal ribosome entry site-dependent translation via methylation of hnRNP A1 (show HNRNPA1 Proteins).
PRMT5 is an osteoclastogenesis activator and PRMT5 inhibition suppresses osteoclast differentiation via downregulation of CXCL10 and RSAD2.
PRMT5 maintains progenitor cells through its regulation of Bmp4 (show BMP4 Proteins); 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 (show GLP1R Proteins) transcript levels and PKA-mediated phosphorylation of FOXO1 (show FOXO1 Proteins) and CREB (show CREB1 Proteins).
findings show that PRMT5 is an important modulator of CD4 (show CD4 Proteins)(+) 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 (show PPARG Proteins) 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 (show CARM1 Proteins) and PRMT5 for proper myogenesis in zebrafish
Data indicate that MEP50 (show WDR77 Proteins) WD repeat protein (show DCAF7 Proteins) is essential for methylation of histones H4 and H2A (show H2AFX Proteins) by PRMT5 arginine methyltransferase.
data support a mechanism in which MEP50 (show WDR77 Proteins) binds substrate and stimulates PRMT5 activity modulated by substrate post-translational modifications
Protein arginine methyltransferase Prmt5-Mep50 (show WDR77 Proteins) methylates histones H2A (show H2AFX Proteins) and H4 and the histone chaperone nucleoplasmin (show NPM1 Proteins) in Xenopus laevis eggs
The results suggested that medaka Mep50 (show WDR77 Proteins) 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 (show PRMT1 Proteins);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 (show COPB2 Proteins)-3 receptor.
data confirm that MEP50 (show WDR77 Proteins) 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 (show TP53 Proteins)-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