Evidence map›Paper›PMID 25792598›Full record

ArticleGenes & development2015

Protein arginine methyltransferase CARM1 attenuates the paraspeckle-mediated nuclear retention of mRNAs containing IRAlus.

Shi-Bin Hu, Jian-Feng Xiang, Xiang Li, Yefen Xu, Wei Xue, Min Huang, Catharine C Wong, Cari A Sagum, Mark T Bedford, Li Yang and 2 more

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

65 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. The emerging role of CARM1 in cancer.Cellular oncology (Dordrecht, Netherlands) · 2024
    Review
  10. Article
  11. Article
  12. Nono induces Gadd45b to mediate DNA repair.Life science alliance · 2024
    Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
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  20. Review

5 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 4 institutions in 2 countries.

Shi-Bin HuState Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China;
Jian-Feng XiangState Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China;
Xiang LiState Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China;
Yefen XuState Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China;
Wei XueKey Laboratory of Computational Biology, Chinese Academy of Sciences (CAS)-German Max Planck Society (MPG) Partner Institute for Computational Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China;
Min HuangState Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China;
Catharine C WongState Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China;
Cari A SagumThe University of Texas M.D. Anderson Cancer Center, Smithville, Texas 78957, USA;
Mark T BedfordThe University of Texas M.D. Anderson Cancer Center, Smithville, Texas 78957, USA;
Li YangKey Laboratory of Computational Biology, Chinese Academy of Sciences (CAS)-German Max Planck Society (MPG) Partner Institute for Computational Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China; School of Life Science and Technology, ShanghaiTech University, Shanghai 200031, China.
Donghang ChengThe University of Texas M.D. Anderson Cancer Center, Smithville, Texas 78957, USA; linglingchen@sibcb.ac.cn dcheng@mdanderson.org.
Ling-Ling ChenState Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China; School of Life Science and Technology, ShanghaiTech University, Shanghai 200031, China linglingchen@sibcb.ac.cn dcheng@mdanderson.org.
Chinese Academy of Sciences · CNShanghai Institutes for Biological Sciences · CNThe University of Texas MD Anderson Cancer Center · USCenter for Excellence in Molecular Cell Science · CN

Funding

The Functional Analysis of the Coactivator CARM1R01DK062248 · NIDDK · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI BEDFORD, MARK T. · 2002 to 2015
$4.2M
The Functional Analysis of the Coactivator CARM1R56DK062248 · NIDDK · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI BEDFORD, MARK T · 2007 to 2007
$77k
NIDDK NIH HHS DK062248NIDDK NIH HHS R01 DK062248NIDDK NIH HHS R56 DK062248
6 · The paper itself

Abstract

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 p54(nrb), resulting in reduced binding of p54(nrb) 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.

Indexed as

Alu ElementsAnimalsCell LineCell NucleusDNA MethylationGene Expression RegulationHEK293 CellsHeLa CellsHumansInverted Repeat SequencesMiceProtein-Arginine N-MethyltransferasesProtein BindingProtein Processing, Post-TranslationalProtein TransportRNA, Long Noncodingcoactivator-associated arginine methyltransferase 1Protein-Arginine N-MethyltransferasesRNA, Long NoncodingRNA, MessengerCARM1NEAT1nuclear retentionp54nrbparaspeckles

Identifiers

PMID25792598
PMCPMC4378195
OpenAlexW2008900314

What OpenQuestion holds

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.