Evidence map›Paper›PMID 24247251›Full record

ArticleCell research2014

Lsm2 and Lsm3 bridge the interaction of the Lsm1-7 complex with Pat1 for decapping activation.

Donghui Wu, Denise Muhlrad, Matthew W Bowler, Shimin Jiang, Zhou Liu, Roy Parker, Haiwei Song

Open access · hybridAbstract read
In one paragraph

Article in Cell research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

32 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Analysis of the mechanism of tripropylamine-enhanced lycopene accumulation in Blakeslea trispora through transcriptome.International microbiology : the official journal of the Spanish Society for Microbiology · 2025
    Article
  5. Article
  6. Article
  7. Review
  8. Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022
    Review
  9. Article
  10. Variants inHGG advances · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Pat1 activates late steps in mRNA decay by multiple mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. Article
  19. Review
  20. mRNA decapping: finding the right structures.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 4 countries.

Donghui WuInstitute of Molecular and Cell Biology, 61 Biopolis Drive, Singapore 138673.
Denise MuhlradDepartment of Biochemistry and Howard Hughes Medical Institute, University of Colorado, Boulder, Boulder CO 80303, USA.
Matthew W Bowler1] European Molecular Biology Laboratory, 6 rue Jules Horowitz, BP 181, 38042, Grenoble, France [2] Unit of Virus Host-Cell Interactions, UJF-EMBL-CNRS, UMI 3265, 6 rue Jules Horowitz, 38042 Grenoble Cedex 9, France.
Shimin JiangInstitute of Molecular and Cell Biology, 61 Biopolis Drive, Singapore 138673.
Zhou LiuLife Sciences Institute, Zhejiang University, 388 Yuhangtang Road, Hangzhou, Zhejiang 310000, China.
Roy ParkerDepartment of Biochemistry and Howard Hughes Medical Institute, University of Colorado, Boulder, Boulder CO 80303, USA.
Haiwei Song1] Institute of Molecular and Cell Biology, 61 Biopolis Drive, Singapore 138673 [2] Life Sciences Institute, Zhejiang University, 388 Yuhangtang Road, Hangzhou, Zhejiang 310000, China [3] Department of Biochemistry, National University of Singapore, 14 Science Drive, Singapore 117543.
Institute of Molecular and Cell Biology · SGUniversity of Colorado Boulder · USZhejiang University · CNEuropean Molecular Biology Laboratory · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The evolutionarily conserved Lsm1-7-Pat1 complex is the most critical activator of mRNA decapping in eukaryotic cells and plays many roles in normal decay, AU-rich element-mediated decay, and miRNA silencing, yet how Pat1 interacts with the Lsm1-7 complex is unknown. Here, we show that Lsm2 and Lsm3 bridge the interaction between the C-terminus of Pat1 (Pat1C) and the Lsm1-7 complex. The Lsm2-3-Pat1C complex and the Lsm1-7-Pat1C complex stimulate decapping in vitro to a similar extent and exhibit similar RNA-binding preference. The crystal structure of the Lsm2-3-Pat1C complex shows that Pat1C binds to Lsm2-3 to form an asymmetric complex with three Pat1C molecules surrounding a heptameric ring formed by Lsm2-3. Structure-based mutagenesis revealed the importance of Lsm2-3-Pat1C interactions in decapping activation in vivo. Based on the structure of Lsm2-3-Pat1C, a model of Lsm1-7-Pat1 complex is constructed and how RNA binds to this complex is discussed.

Indexed as

Crystallography, X-RayMutagenesisProtein BindingProtein Structure, QuaternaryProtein Structure, TertiaryRibonucleoproteins, Small NuclearRNARNA-Binding ProteinsRNA CapsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsLsm2 protein, S cerevisiaeLSM3 protein, S cerevisiaePAT1 protein, S cerevisiaeRibonucleoproteins, Small NuclearRNARNA-Binding ProteinsRNA CapsSaccharomyces cerevisiae Proteins

Identifiers

PMID24247251
PMCPMC3915908
OpenAlexW2046181612

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.