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Li, Wen-Juan; He, Yao-Hui; Yang, Jing-Jing; Hu, Guo-Sheng; Lin, Yi-An; Ran, Ting; Peng, Bing-Ling; Xie, Bing-Lan; Huang, Ming-Feng; Gao, Xiang; Huang, Hai-Hua; Zhu, Helen He; Ye, Feng; Liu, Wen
Nature communications, 03/2021, Letnik: 12, Številka: 1Journal Article
Numerous substrates have been identified for Type I and II arginine methyltransferases (PRMTs). However, the full substrate spectrum of the only type III PRMT, PRMT7, and its connection to type I and II PRMT substrates remains unknown. Here, we use mass spectrometry to reveal features of PRMT7-regulated methylation. We find that PRMT7 predominantly methylates a glycine and arginine motif; multiple PRMT7-regulated arginine methylation sites are close to phosphorylations sites; methylation sites and proximal sequences are vulnerable to cancer mutations; and methylation is enriched in proteins associated with spliceosome and RNA-related pathways. We show that PRMT4/5/7-mediated arginine methylation regulates hnRNPA1 binding to RNA and several alternative splicing events. In breast, colorectal and prostate cancer cells, PRMT4/5/7 are upregulated and associated with high levels of hnRNPA1 arginine methylation and aberrant alternative splicing. Pharmacological inhibition of PRMT4/5/7 suppresses cancer cell growth and their co-inhibition shows synergistic effects, suggesting them as targets for cancer therapy.
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