globalchange  > 气候变化与战略
DOI: 10.1016/j.scib.2021.01.004
论文题名:
A systematic survey of PRMT interactomes reveals the key roles of arginine methylation in the global control of RNA splicing and translation
作者: 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.
刊名: Science Bulletin
ISSN: 20959273
出版年: 2021
卷: 66, 期:13
起始页码: 1342
结束页码: 1357
语种: 英语
中文关键词: 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)
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
Citation statistics:
资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/170439
Appears in Collections:气候变化与战略

Files in This Item:

There are no files associated with this item.


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

Recommended Citation:
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]. Science Bulletin,2021-01-01,66(13)
Service
Recommend this item
Sava as my favorate item
Show this item's statistics
Export Endnote File
Google Scholar
Similar articles in Google Scholar
[Wei H.-H.]'s Articles
[Fan X.-J.]'s Articles
[Hu Y.]'s Articles
百度学术
Similar articles in Baidu Scholar
[Wei H.-H.]'s Articles
[Fan X.-J.]'s Articles
[Hu Y.]'s Articles
CSDL cross search
Similar articles in CSDL Cross Search
[Wei H.-H.]‘s Articles
[Fan X.-J.]‘s Articles
[Hu Y.]‘s Articles
Related Copyright Policies
Null
收藏/分享
所有评论 (0)
暂无评论
 

Items in IR are protected by copyright, with all rights reserved, unless otherwise indicated.