Evidence map›Paper›PMID 30601114›Full record

ArticleeLife2019

RNA-binding proteins distinguish between similar sequence motifs to promote targeted deadenylation by Ccr4-Not.

Michael W Webster, James Aw Stowell, Lori A Passmore

Open access · goldAbstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

58 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. The molecular determinants of PABPC-mediated deadenylation rate.bioRxiv : the preprint server for biology · 2026
    Article
  6. Phosphorylation-dependent tuning of mRNA deadenylation rates.Nature structural & molecular biology · 2026
    Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. A higher order PUF complex is central to regulation ofbioRxiv : the preprint server for biology · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. Article
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

3 authors at 1 institution in 1 country.

Michael W WebsterMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
James Aw StowellMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Lori A PassmoreMRC Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID 0000-0003-1815-3710
MRC Laboratory of Molecular Biology · GB

Funding

European Research Council 261151Horizon 2020 Framework Programme 725685Medical Research Council MC_U105192715Seventh Framework Programme 261151
6 · The paper itself

Abstract

The Ccr4-Not complex removes mRNA poly(A) tails to regulate eukaryotic mRNA stability and translation. RNA-binding proteins contribute to specificity by interacting with both Ccr4-Not and target mRNAs, but this is not fully understood. Here, we reconstitute accelerated and selective deadenylation of RNAs containing AU-rich elements (AREs) and Pumilio-response elements (PREs). We find that the fission yeast homologues of Tristetraprolin/TTP and Pumilio/Puf (Zfs1 and Puf3) interact with Ccr4-Not via multiple regions within low-complexity sequences, suggestive of a multipartite interface that extends beyond previously defined interactions. Using a two-color assay to simultaneously monitor poly(A) tail removal from different RNAs, we demonstrate that Puf3 can distinguish between RNAs of very similar sequence. Analysis of binding kinetics reveals that this is primarily due to differences in dissociation rate constants. Consequently, motif quality is a major determinant of mRNA stability for Puf3 targets in vivo and can be used for the prediction of mRNA targets.

Indexed as

AnimalsBase SequenceBinding SitesMultiprotein ComplexesNuclear ProteinsNucleotide MotifsPoly APolyadenylationProtein BindingRNARNA-Binding ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsSf9 CellsSpodopteraMultiprotein ComplexesNuclear ProteinsPoly ARNARNA-Binding ProteinsSchizosaccharomyces pombe ProteinsZfs1 protein, S pombebiochemistrychemical biologydeadenylationgene expressionpoly(A) tailS. cerevisiaeS. pombe

Identifiers

PMID30601114
PMCPMC6340701
OpenAlexW2907781352

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.