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The uncharacterized protein FAM47E interacts with PRMT5 and regulates its functions

Life Sci Alliance. 2020-12; 
Baskar Chakrapani, Mohd Imran K Khan, Rajashekar Varma Kadumuri, Somlee Gupta, Mamta Verma, Sharad Awasthi, Gayathri Govindaraju, Arun Mahesh, Arumugam Rajavelu, Sreenivas Chavali, Arunkumar Dhayalan
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Catalog Antibody The eluted proteins were immunoblotted and probed with anti-His antibody (Cat. no. A00186-100; GenScript) Get A Quote

摘要

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 i... More

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