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Data indicate that MEP50 WD repeat protein (show DCAF7 Proteins) is essential for methylation of histones H4 and H2A (show H2AFX Proteins) by PRMT5 (show PRMT5 Proteins) arginine methyltransferase.
Structure of MEP50/Wdr77 in the PRMT5 (show PRMT5 Proteins)-MEP50 complex
Protein arginine methyltransferase Prmt5 (show PRMT5 Proteins)-Mep50 methylates histones H2A (show H2AFX Proteins) and H4 and the histone chaperone nucleoplasmin (show NPM1 Proteins) in Xenopus laevis eggs
In an in vitro assay of vascular smooth muscle cells, circRNA WDR77 silencing significantly inhibited cell proliferation and migration. Bioinformatics methods revealed that miR (show MLXIP Proteins)-124 and fibroblast growth factor 2 (FGF-2 (show FGF2 Proteins)) were downstream targets of circRNA WDR77.
SFN (show SFN Proteins) treatment of tumors results in reduced MEP50 level and H4R3me2s formation, confirming that that SFN (show SFN Proteins) impacts this complex in vivo. These studies suggest that the PRMT5 (show PRMT5 Proteins)/MEP50 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.
Results provide evidence that PRMT5 and p44 regulate gene expression of growth and anti-growth factors to promote lung tumorigenesis.
TSC22D2 protein might be a member of the PRMT5 (show PRMT5 Proteins) complex via direct binding of WDR77.
MEP50 genes reduces gene expression through histone arginine methylation in keratinocytes.
MEP50 can transform cells independent of AR and ER.
Data indicate that MEP50 WD repeat protein (show DCAF7 Proteins) is essential for methylation of histones H4 and H2A by PRMT5 (show PRMT5 Proteins) arginine methyltransferase.
These findings characterize PKG (show PRKG1 Proteins) as a novel regulator of AR-mediated transcription by enhancing AR cofactor p44/WDR77's function.
Data indicate a transcription complex androgen receptor (AR (show AR Proteins))-p44 (show GTF2H2 Proteins)-Smad1 (show GARS Proteins), and confirmed for physical interaction by co-immunoprecipitaion.
These studies suggest a novel mechanism by which proliferation and differentiation of prostate epithelial cells are controlled by WDR77's location in the cell.
WDR77 expression is associated with E2F1 (show E2F1 Proteins), E2F3, GATA2 (show GATA2 Proteins) and GATA6 (show GATA6 Proteins) occupancy on the WDR77 gene, whereas, in contrast, E2F6 (show E2F6 Proteins), GATA1 (show GATA1 Proteins) and GATA3 (show GATA3 Proteins) occupancy is associated with the loss of WDR77 expression during erythroid maturation and lung development
Silencing p21(Cip1 (show CDKN1A Proteins)) or NF-kappaB (show NFKB1 Proteins) p65 (show NFkBP65 Proteins) expression with short hairpin RNA (shRNA) abolished astrocyte activation and rescued the astrocyte growth inhibition induced by deletion of the p44/WDR77 gene.
WDR77 is a component of the 20S PRMT5 (MIM 604045)-containing methyltransferase complex, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins (see MIM 601061). This modification targets Sm proteins to the survival of motor neurons (SMN) complex (see MIM 600354) for assembly into small nuclear ribonucleoprotein core particles (Friesen et al., 2002
WD repeat-containing protein 77
, methylosome protein 50
, WD repeat domain 77
, methylosome protein 50-like
, androgen receptor cofactor p44