气候变化领域集成服务门户(CCPortal): A systematic survey of PRMT interactomes reveals the key roles of arginine methylation in the global control of RNA splicing and translation

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DOI	10.1016/j.scib.2021.01.004
	A systematic survey of PRMT interactomes reveals the key roles of arginine methylation in the global control of RNA splicing and translation
	Wei H.-H.; Fan X.-J.; Hu Y.; Tian X.-X.; Guo M.; Mao M.-W.; Fang Z.-Y.; Wu P.; Gao S.-X.; Peng C.; Yang Y.; Wang Z.
发表日期	2021
ISSN	20959273
起始页码	1342
结束页码	1357
卷号	66 期号:13
英文摘要	Thousands of proteins undergo arginine methylation, a widespread post-translational modification catalyzed by several protein arginine methyltransferases (PRMTs). However, global understanding of their biological functions is limited due to the lack of a complete picture of the catalytic network for each PRMT. Here, we systematically identified interacting proteins for all human PRMTs and demonstrated their functional importance in mRNA splicing and translation. We demonstrated significant overlapping of interactomes of human PRMTs with the known methylarginine-containing proteins. Different PRMTs are functionally redundant with a high degree of overlap in their substrates and high similarities between their putative methylation motifs. Importantly, RNA-binding proteins involved in regulating RNA splicing and translation contain highly enriched arginine methylation regions. Moreover, inhibition of PRMTs globally alternates alternative splicing (AS) and suppresses translation. In particular, ribosomal proteins are extensively modified with methylarginine, and mutations in their methylation sites suppress ribosome assembly, translation, and eventually cell growth. Collectively, our study provides a global view of different PRMT networks and uncovers critical functions of arginine methylation in regulating mRNA splicing and translation. © 2021 Science China Press
关键词	Alternative splicing mRNA translation Post-translational modification Protein arginine methyltransferase Ribosomal proteins RNA-binding protein
英文关键词	Alkylation; Arginine; Cell proliferation; Methylation; Proteins; RNA; Alternative splicing; Biological functions; Catalytic networks; Critical functions; Methyltransferases; Post-translational modifications; Ribosomal proteins; RNA-binding protein; Translation (languages)
语种	英语
来源期刊	Science Bulletin
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/207605
作者单位	CAS Key Laboratory of Computational Biology, CAS Key Laboratory of Computational Biology, Bio-Med Big Data Center, Shanghai Institute of Nutrition and Health, CAS Center for Excellence in Molecular Cell Science, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Shanghai, 200031, China; National Facility for Protein Science in Shanghai, Zhang-Jiang Lab, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai, 201210, China; Xijing Hospital of Digestive Diseases, Fourth Military Medical University, Xi'an, 710000, China
推荐引用方式 GB/T 7714	Wei H.-H.,Fan X.-J.,Hu Y.,et al. A systematic survey of PRMT interactomes reveals the key roles of arginine methylation in the global control of RNA splicing and translation[J],2021,66(13).
APA	Wei H.-H..,Fan X.-J..,Hu Y..,Tian X.-X..,Guo M..,...&Wang Z..(2021).A systematic survey of PRMT interactomes reveals the key roles of arginine methylation in the global control of RNA splicing and translation.Science Bulletin,66(13).
MLA	Wei H.-H.,et al."A systematic survey of PRMT interactomes reveals the key roles of arginine methylation in the global control of RNA splicing and translation".Science Bulletin 66.13(2021).