WDR77 Antibody

1. A 3.7 A structure of PRMT5, solved in complex with regulatory binding subunit MEP50 (methylosome associated protein 50, WDR77, p44), by single particle (SP) cryo-Electron Microscopy (cryo-EM) using micrographs of particles that are visibly crowded and aggregated. The catalytic PRMT5 subunits form a core tetramer and the MEP50 subunits are arranged peripherally in complex with the PRMT5 N-terminal domain. PMID:29518110
2. Data indicate that ZNF326 is an interaction partner and substrate of the PRMT5/WDR77 complex. PMID:28977470
3. In an in vitro assay of vascular smooth muscle cells, circRNA WDR77 silencing significantly inhibited cell proliferation and migration. Bioinformatics methods revealed that miR-124 and fibroblast growth factor 2 (FGF-2) were downstream targets of circRNA WDR77. PMID:29042195
4. SFN treatment of tumors results in reduced MEP50 level and H4R3me2s formation, confirming that that SFN impacts this complex in vivo. These studies suggest that the PRMT5/MEP50 is required for tumor growth and that reduced expression of this complex is a part of the mechanism of SFN suppression of tumor formation. PMID:28854561
5. Results provide evidence that PRMT5 and p44 regulate gene expression of growth and anti-growth factors to promote lung tumorigenesis. PMID:27480244
6. TSC22D2 protein might be a member of the PRMT5 complex via direct binding of WDR77. PMID:27337956
7. MEP50 genes reduces gene expression through histone arginine methylation in keratinocytes. PMID:26763441
8. MEP50 can transform cells independent of AR and ER. PMID:25277535
9. Data indicate that MEP50 WD repeat protein is essential for methylation of histones H4 and H2A by PRMT5 arginine methyltransferase. PMID:25713080
10. These findings characterize PKG as a novel regulator of AR-mediated transcription by enhancing AR cofactor p44/WDR77's function. PMID:23755100
11. Data indicate a transcription complex androgen receptor (AR)-p44-Smad1, and confirmed for physical interaction by co-immunoprecipitaion. PMID:23734213
12. These studies suggest a novel mechanism by which proliferation and differentiation of prostate epithelial cells are controlled by WDR77's location in the cell. PMID:23145110
13. structure of the surprising hetero-octameric complex reveals the close interaction between the seven-bladed beta-propeller MEP50 and the N-terminal domain of PRMT5, and delineates the structural elements of substrate recognition. PMID:23071334
14. p44 plays a role in mediating the effects of hormones during ovarian tumorigenesis. PMID:22022581
15. These results provide a basis for understanding subcellular transport of p44/WDR77 during prostate development and tumorigenesis. PMID:21789256
16. expression and function of p44 in breast cancer; expression of p44 shows strong cytoplasmic expression in morphologically normal terminal ductal lobular units, while nuclear p44 is observed in both ductal carcinoma in situ and invasive carcinoma PMID:19840198
17. Here, we describe a novel component of the methylosome, a 50-kilodalton WD repeat protein termed methylosome protein 50 (MEP50). PMID:11756452
18. SUZ12 might have a role in transcriptional regulation through physical interaction with MEP50 that can be an adaptor between PRMT5 and its substrate H2A PMID:16712789
19. Forced nuclear localization of p44 inhibited prostate cancer cell growth by G1 cell-cycle arrest. PMID:17032745
20. results suggest distinct functions of the nuclear and the p44/protein arginine methyltransferase 5 complexes in the developing fetal testis and in the oncogenesis of testicular tumors. PMID:17437848
21. nuclear p44 and cytoplasmic p44 have distinct and opposing functions in the regulation of prostate cancer cell proliferation PMID:18356297

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HGNC: 29652

UNIGENE: Hs.204773

KEGG: hsa:79084

STRING: 9606.ENSP00000235090

OMIM: 611734