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- W2748589070 abstract "We observed overexpression and increased intra-nuclear accumulation of the PRMT5/WDR77 in breast cancer cell lines relative to immortalized breast epithelial cells. Utilizing mass spectrometry and biochemistry approaches we identified the Zn-finger protein ZNF326, as a novel interaction partner and substrate of the nuclear PRMT5/WDR77 complex. ZNF326 is symmetrically dimethylated at arginine 175 (R175) and this modification is lost in a PRMT5 and WDR77-dependent manner. Loss of PRMT5 or WDR77 in MDA-MB-231 cells leads to defects in alternative splicing, including inclusion of A-T rich exons in target genes, a phenomenon that has previously been observed upon loss of ZNF326. We observed that the alternatively spliced transcripts of a subset of these genes, involved in proliferation and tumor cell migration like REPIN1/AP4, ST3GAL6, TRNAU1AP and PFKM are degraded upon loss of PRMT5. In summary, we have identified a novel mechanism through which the PRMT5/WDR77 complex maintains the balance between splicing and mRNA stability through methylation of ZNF326." @default.
- W2748589070 created "2017-08-31" @default.
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- W2748589070 date "2017-08-21" @default.
- W2748589070 modified "2023-10-01" @default.
- W2748589070 title "The PRMT5/WDR77 complex regulates alternative splicing through ZNF326 in breast cancer" @default.
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- W2748589070 doi "https://doi.org/10.1093/nar/gkx727" @default.
- W2748589070 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5737218" @default.
- W2748589070 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28977470" @default.
- W2748589070 hasPublicationYear "2017" @default.
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