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The PRMT5/WDR77 complex regulates alternative splicing through ZNF326 in breast cancer
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2017 (English)In: Nucleic Acids Research, ISSN 0305-1048, E-ISSN 1362-4962, Vol. 45, no 19, p. 11106-11120Article in journal (Refereed) Published
Abstract [en]

We observed overexpression and increased intranuclear 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.

Place, publisher, year, edition, pages
Oxford University Press, 2017. Vol. 45, no 19, p. 11106-11120
National Category
Cell Biology
Identifiers
URN: urn:nbn:se:umu:diva-142249DOI: 10.1093/nar/gkx727ISI: 000414552300019PubMedID: 28977470OAI: oai:DiVA.org:umu-142249DiVA, id: diva2:1164792
Available from: 2017-12-12 Created: 2017-12-12 Last updated: 2018-11-27Bibliographically approved

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Aguilo, Francesca

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Aguilo, Francesca
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Department of Medical BiosciencesWallenberg Centre for Molecular Medicine at Umeå University (WCMM)
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