Evidence map›Paper›PMID 27114555›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Recruitment of the NineTeen Complex to the activated spliceosome requires AtPRMT5.

Xian Deng, Tiancong Lu, Lulu Wang, Lianfeng Gu, Jing Sun, Xiangfeng Kong, Chunyan Liu, Xiaofeng Cao

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
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

37 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. TheProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Assessing the Role ofPlants (Basel, Switzerland) · 2024
    Article
  9. Review
  10. Article
  11. Light controls mesophyll-specific post-transcriptional splicing of photoregulatory genes by AtPRMT5.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. PNAS nexus · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Function of Cajal Bodies in Nuclear RNA Retention inInternational journal of molecular sciences · 2022
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 5 institutions in 1 country.

Xian DengState Key Laboratory of Plant Genomics and National Center for Plant Gene Research, CAS Center for Excellence in Molecular Plant Sciences, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China;
Tiancong LuState Key Laboratory of Plant Genomics and National Center for Plant Gene Research, CAS Center for Excellence in Molecular Plant Sciences, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China;
Lulu WangState Key Laboratory of Plant Genomics and National Center for Plant Gene Research, CAS Center for Excellence in Molecular Plant Sciences, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China;
Lianfeng GuState Key Laboratory of Plant Genomics and National Center for Plant Gene Research, CAS Center for Excellence in Molecular Plant Sciences, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China;
Jing SunState Key Laboratory of Plant Genomics and National Center for Plant Gene Research, CAS Center for Excellence in Molecular Plant Sciences, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China;
Xiangfeng KongState Key Laboratory of Plant Genomics and National Center for Plant Gene Research, CAS Center for Excellence in Molecular Plant Sciences, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China;
Chunyan LiuState Key Laboratory of Plant Genomics and National Center for Plant Gene Research, CAS Center for Excellence in Molecular Plant Sciences, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China; cyliu@genetics.ac.cn xfcao@genetics.ac.cn.
Xiaofeng CaoState Key Laboratory of Plant Genomics and National Center for Plant Gene Research, CAS Center for Excellence in Molecular Plant Sciences, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China; Collaborative Innovation Center for Genetics and Development, Fudan University, Shanghai 200438, China cyliu@genetics.ac.cn xfcao@genetics.ac.cn.
Institute of Genetics and Developmental Biology · CNCenter for Excellence in Molecular Plant Sciences · CNChinese Academy of Sciences · CNFudan University · CNState Key Laboratory of Plant Genomics · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein arginine methylation, catalyzed by protein arginine methyltransferases (PRMTs), is involved in a multitude of biological processes in eukaryotes. Symmetric arginine dimethylation mediated by PRMT5 modulates constitutive and alternative pre-mRNA splicing of diverse genes to regulate normal growth and development in multiple species; however, the underlying molecular mechanism remains largely unknown. A genetic screen for suppressors of an Arabidopsis symmetric arginine dimethyltransferase mutant, atprmt5, identified two gain-of-function alleles of pre-mRNA processing factor 8 gene (prp8-8 and prp8-9), the highly conserved core component of the U5 small nuclear ribonucleoprotein (snRNP) and the spliceosome. These two atprmt5 prp8 double mutants showed suppression of the developmental and splicing alterations of atprmt5 mutants. In atprmt5 mutants, the NineTeen complex failed to be assembled into the U5 snRNP to form an activated spliceosome; this phenotype was restored in the atprmt5 prp8-8 double mutants. We also found that loss of symmetric arginine dimethylation of Sm proteins prevents recruitment of the NineTeen complex and initiation of spliceosome activation. Together, our findings demonstrate that symmetric arginine dimethylation has important functions in spliceosome assembly and activation, and uncover a key molecular mechanism for arginine methylation in pre-mRNA splicing that impacts diverse developmental processes.

Indexed as

ArabidopsisArabidopsis ProteinsProtein-Arginine N-MethyltransferasesRNA PrecursorsRNA SplicingSaccharomyces cerevisiae ProteinsSpliceosomesArabidopsis ProteinsPRMT5 protein, ArabidopsisProtein-Arginine N-MethyltransferasesRNA PrecursorsSaccharomyces cerevisiae ProteinsSpp382 protein, S cerevisiaearginine methylationAtPRMT5pre-mRNA splicingprotein arginine methyltransferasePrp19C/NTC

Identifiers

PMID27114555
PMCPMC4868449
OpenAlexW2343767855

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.