Evidence map›Paper›PMID 38321923›Full record

ArticleNucleic acids research2024

The unique dual targeting of AGO1 by two types of PRMT enzymes promotes phasiRNA loading in Arabidopsis thaliana.

Clément Barre-Villeneuve, Michèle Laudié, Marie-Christine Carpentier, Lauriane Kuhn, Thierry Lagrange, Jacinthe Azevedo-Favory

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
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  4. Review
  5. 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

6 authors at 1 institution in 1 country.

Clément Barre-VilleneuveCNRS, Laboratoire Génome et Développement des Plantes, UMR 5096, 66860 Perpignan, France.
Michèle LaudiéCNRS, Laboratoire Génome et Développement des Plantes, UMR 5096, 66860 Perpignan, France.
Marie-Christine CarpentierCNRS, Laboratoire Génome et Développement des Plantes, UMR 5096, 66860 Perpignan, France.ORCID 0000-0002-4795-9054
Lauriane KuhnPlateforme protéomique Strasbourg - Esplanade, CNRS FR1589, Université de Strasbourg, IBMC, 2 allée Konrad Roentgen, F-67084 Strasbourg, France.ORCID 0000-0002-2637-1024
Thierry LagrangeCNRS, Laboratoire Génome et Développement des Plantes, UMR 5096, 66860 Perpignan, France.
Jacinthe Azevedo-FavoryCNRS, Laboratoire Génome et Développement des Plantes, UMR 5096, 66860 Perpignan, France.ORCID 0000-0002-2096-0805
Centre National de la Recherche Scientifique · FR

Funding

CNRSEcole Universitaire de Recherche (EUR) ANR-18-EURE-0019GAFL laboratory (INRAE, Avignon, France)Laboratoires d'Excellences (LABEX) ANR-10-LABX-41Université de PerpignanUniversity of Strasbourg
6 · The paper itself

Abstract

Arginine/R methylation (R-met) of proteins is a widespread post-translational modification (PTM), deposited by a family of protein arginine/R methyl transferase enzymes (PRMT). Regulations by R-met are involved in key biological processes deeply studied in metazoan. Among those, post-transcriptional gene silencing (PTGS) can be regulated by R-met in animals and in plants. It mainly contributes to safeguard processes as protection of genome integrity in germlines through the regulation of piRNA pathway in metazoan, or response to bacterial infection through the control of AGO2 in plants. So far, only PRMT5 has been identified as the AGO/PIWI R-met writer in higher eukaryotes. We uncovered that AGO1, the main PTGS effector regulating plant development, contains unique R-met features among the AGO/PIWI superfamily, and outstanding in eukaryotes. Indeed, AGO1 contains both symmetric (sDMA) and asymmetric (aDMA) R-dimethylations and is dually targeted by PRMT5 and by another type I PRMT in Arabidopsis thaliana. We showed also that loss of sDMA didn't compromise AtAGO1 subcellular trafficking in planta. Interestingly, we underscored that AtPRMT5 specifically promotes the loading of phasiRNA in AtAGO1. All our observations bring to consider this dual regulation of AtAGO1 in plant development and response to environment, and pinpoint the complexity of AGO1 post-translational regulation.

Indexed as

ArabidopsisArabidopsis ProteinsArgonaute ProteinsProtein-Arginine N-MethyltransferasesAnimalsArginineEukaryotaPlantsRNA InterferenceAGO1 protein, ArabidopsisArabidopsis ProteinsArginineArgonaute ProteinsPRMT5 protein, ArabidopsisProtein-Arginine N-Methyltransferases

Identifiers

PMID38321923
PMCPMC10954461
OpenAlexW4391613254

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.