Protein arginine methyltransferase CARM1 attenuates the paraspeckle-mediated nuclear retention of mRNAs containing IRAlus
2015-03-15
发表期刊GENES & DEVELOPMENT
ISSN0890-9369
卷号29期号:6页码:630-645
发表状态已发表
DOI10.1101/gad.257048.114
摘要In many cells, mRNAs containing inverted repeated Alu elements (IRAlus) in their 3' untranslated regions (UTRs) are inefficiently exported to the cytoplasm. Such nuclear retention correlates with paraspeckle-associated protein complexes containing p54(nrb). However, nuclear retention of mRNAs containing IRAlus is variable, and how regulation of retention and export is achieved is poorly understood. Here we show one mechanism of such regulation via the arginine methyltransferase CARM1 (coactivator-associated arginine methyltransferase 1). We demonstrate that disruption of CARM1 enhances the nuclear retention of mRNAs containing IRAlus. CARM1 regulates this nuclear retention pathway at two levels: CARM1 methylates the coiled-coil domain of p54nrb, resulting in reduced binding of p54nrb to mRNAs containing IRAlus, and also acts as a transcription regulator to suppress NEAT1 transcription, leading to reduced paraspeckle formation. These actions of CARM1 work together synergistically to regulate the export of transcripts containing IRAlus from paraspeckles under certain cellular stresses, such as poly(I:C) treatment. This work demonstrates how a post-translational modification of an RNA-binding protein affects protein-RNA interaction and also uncovers a mechanism of transcriptional regulation of the long noncoding RNA NEAT1.
关键词paraspeckles p54(nrb) nuclear retention CARM1 NEAT1
收录类别SCI
语种英语
资助项目National Institutes of Health[DK062248]
WOS研究方向Cell Biology ; Developmental Biology ; Genetics & Heredity
WOS类目Cell Biology ; Developmental Biology ; Genetics & Heredity
WOS记录号WOS:000351556700006
出版者COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
WOS关键词LONG NONCODING RNA ; INVERTED REPEATS ; GENE-EXPRESSION ; BINDING PROTEIN ; METHYLATION ; TRANSCRIPTION ; BODIES ; DIFFERENTIATION ; ACTIVATION ; RELOCATION
原始文献类型Article
引用统计
被引频次:75[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/2243
专题生命科学与技术学院_特聘教授组_杨力组
生命科学与技术学院_特聘教授组_陈玲玲组
通讯作者Yang, Li
作者单位
1.Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, State Key Lab Mol Biol, Shanghai 200031, Peoples R China
2.Chinese Acad Sci, Shanghai Inst Biol Sci, German Max Planck Soc MPG Partner Inst Computat, Key Lab Computat Biol, Shanghai 200031, Peoples R China
3.Univ Texas MD Anderson Canc Ctr, Smithville, TX 78957 USA
4.ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai 200031, Peoples R China
通讯作者单位生命科学与技术学院
推荐引用方式
GB/T 7714
Hu, Shi-Bin,Xiang, Jian-Feng,Li, Xiang,et al. Protein arginine methyltransferase CARM1 attenuates the paraspeckle-mediated nuclear retention of mRNAs containing IRAlus[J]. GENES & DEVELOPMENT,2015,29(6):630-645.
APA Hu, Shi-Bin.,Xiang, Jian-Feng.,Li, Xiang.,Xu, Yefen.,Xue, Wei.,...&Chen, Ling-Ling.(2015).Protein arginine methyltransferase CARM1 attenuates the paraspeckle-mediated nuclear retention of mRNAs containing IRAlus.GENES & DEVELOPMENT,29(6),630-645.
MLA Hu, Shi-Bin,et al."Protein arginine methyltransferase CARM1 attenuates the paraspeckle-mediated nuclear retention of mRNAs containing IRAlus".GENES & DEVELOPMENT 29.6(2015):630-645.
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