Evidence map›Paper›PMID 34791434›Full record

ArticlePlant physiology2022

A NYN domain protein directly interacts with DECAPPING1 and is required for phyllotactic pattern.

Marlene Schiaffini, Clara Chicois, Aude Pouclet, Tiphaine Chartier, Elodie Ubrig, Anthony Gobert, Hélène Zuber, Jérôme Mutterer, Johana Chicher, Lauriane Kuhn and 3 more

Abstract read
In one paragraph

Article in Plant physiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Endoribonuclease DNE1 Promotes Ethylene Response by ModulatingInternational journal of molecular sciences · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. How RNases Shape Mitochondrial Transcriptomes.International journal of molecular sciences · 2022
    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

13 authors.

Marlene SchiaffiniInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France.
Clara ChicoisInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France.
Aude PoucletInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France.
Tiphaine ChartierInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France.
Elodie UbrigInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France.
Anthony GobertInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France.ORCID 0000-0003-2626-8788
Hélène ZuberInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France.ORCID 0000-0002-2132-4536
Jérôme MuttererInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France.
Johana ChicherPlateforme protéomique Strasbourg Esplanade du CNRS, Université de Strasbourg, Strasbourg, France.ORCID 0000-0002-4403-7484
Lauriane KuhnPlateforme protéomique Strasbourg Esplanade du CNRS, Université de Strasbourg, Strasbourg, France.ORCID 0000-0002-2637-1024
Philippe HammannPlateforme protéomique Strasbourg Esplanade du CNRS, Université de Strasbourg, Strasbourg, France.ORCID 0000-0002-6883-9203
Dominique GagliardiInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France.ORCID 0000-0002-5871-7544
Damien GarciaInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, Strasbourg, France.ORCID 0000-0001-6142-1974

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotes, general mRNA decay requires the decapping complex. The activity of this complex depends on its catalytic subunit, DECAPPING2 (DCP2), and its interaction with decapping enhancers, including its main partner DECAPPING1 (DCP1). Here, we report that in Arabidopsis thaliana, DCP1 also interacts with a NYN domain endoribonuclease, hence named DCP1-ASSOCIATED NYN ENDORIBONUCLEASE 1 (DNE1). Interestingly, we found DNE1 predominantly associated with DCP1, but not with DCP2, and reciprocally, suggesting the existence of two distinct protein complexes. We also showed that the catalytic residues of DNE1 are required to repress the expression of mRNAs in planta upon transient expression. The overexpression of DNE1 in transgenic lines led to growth defects and a similar gene deregulation signature than inactivation of the decapping complex. Finally, the combination of dne1 and dcp2 mutations revealed a functional redundancy between DNE1 and DCP2 in controlling phyllotactic pattern formation. Our work identifies DNE1, a hitherto unknown DCP1 protein partner highly conserved in the plant kingdom and identifies its importance for developmental robustness.

Indexed as

RNA StabilityArabidopsisCatalytic DomainCo-Repressor ProteinsEndoribonucleasesRNA, PlantCo-Repressor ProteinsEndoribonucleasesRNA, Plant

Identifiers

PMID34791434
PMCPMC8825452

What OpenQuestion holds

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Registered trials

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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.