Baskar, Chakrapani and Gayathri, Govindaraju and Arumugam, Rajavelu (2021) The uncharacterized protein FAM47E interacts with PRMT5 and regulates its functions. Life science alliance, 4 (3). ISSN 2575-1077

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Abstract

Protein arginine methyltransferase 5 (PRMT5) symmetrically dimethylates arginine residues in various proteins affecting diverse cellular processes such as transcriptional regulation, splicing, DNA repair, differentiation, and cell cycle. Elevated levels of PRMT5 are observed in several types of cancers and are associated with poor clinical outcomes, making PRMT5 an important diagnostic marker and/or therapeutic target for cancers. Here, using yeast two-hybrid screening, followed by immunoprecipitation and pull-down assays, we identify a previously uncharacterized protein, FAM47E, as an interaction partner of PRMT5. We report that FAM47E regulates steady-state levels of PRMT5 by affecting its stability through inhibition of its proteasomal degradation. Importantly, FAM47E enhances the chromatin association and histone methylation activity of PRMT5. The PRMT5-FAM47E interaction affects the regulation of PRMT5 target genes expression and colony-forming capacity of the cells. Taken together, we identify FAM47E as a protein regulator of PRMT5, which promotes the functions of this versatile enzyme. These findings imply that disruption of PRMT5-FAM47E interaction by small molecules might be an alternative strategy to attenuate the oncogenic function(s) of PRMT5

Item Type:	Article
Subjects:	Interdisciplinary Biology
Depositing User:	Central Library RGCB
Date Deposited:	21 Jan 2022 06:28
Last Modified:	21 Jan 2022 06:28
URI:	http://rgcb.sciencecentral.in/id/eprint/1107

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