Profiling PRMT methylome reveals roles of hnRNPA1 arginine methylation in RNA splicing and cell growth

• Published in: Nature communications Vol. 12; no. 1; pp. 1946 - 20
• Main Authors: 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
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 29.03.2021; Nature Publishing Group; Nature Portfolio
• Subjects: 13; 13/89; 14; 38; 45/22; 45/90; 45/91; 49/109; 631/337/1645/1946; 631/45/475; 631/45/612/1230; 631/80/458/1648; 82/58; 82/80; 82/83; 96; Alternative Splicing; Amino Acid Sequence; Arginine; Arginine - metabolism; Breast cancer; Breast Neoplasms - genetics; Breast Neoplasms - metabolism; Breast Neoplasms - pathology; Cancer; Cell Cycle - drug effects; Cell Cycle - genetics; Cell growth; Cell Line, Tumor; Colorectal Neoplasms - genetics; Colorectal Neoplasms - metabolism; Colorectal Neoplasms - pathology; Enzyme Inhibitors - pharmacology; Female; Gene Expression Profiling; Gene Expression Regulation, Neoplastic; Glycine; HEK293 Cells; Heterogeneous Nuclear Ribonucleoprotein A1 - antagonists & inhibitors; Heterogeneous Nuclear Ribonucleoprotein A1 - genetics; Heterogeneous Nuclear Ribonucleoprotein A1 - metabolism; Humanities and Social Sciences; Humans; Male; Mass spectrometry; Mass spectroscopy; Methylation; Methylation - drug effects; multidisciplinary; Mutation; Prostate cancer; Prostatic Neoplasms - genetics; Prostatic Neoplasms - metabolism; Prostatic Neoplasms - pathology; Protein Binding; Protein Processing, Post-Translational; Protein-Arginine N-Methyltransferases - antagonists & inhibitors; Protein-Arginine N-Methyltransferases - genetics; Protein-Arginine N-Methyltransferases - metabolism; Proteomics; Ribonucleic acid; RNA; RNA, Small Interfering - genetics; RNA, Small Interfering - metabolism; Science; Science (multidisciplinary); Spliceosomes - drug effects; Spliceosomes - genetics; Spliceosomes - metabolism; Splicing; Substrate Specificity; Substrates; Synergistic effect

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-regul...