Evidence map›Paper›PMID 23894680›Full record

ArticlePloS one2013

Photosynthetic control of Arabidopsis leaf cytoplasmic translation initiation by protein phosphorylation.

Edouard Boex-Fontvieille, Marlène Daventure, Mathieu Jossier, Michel Zivy, Michael Hodges, Guillaume Tcherkez

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.7field-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

33 citing papers in PubMed, 73 citations in OpenAlex.

  1. Rapid COThe Plant journal : for cell and molecular biology · 2026
    Article
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  4. Physiological and Biochemical Responses ofLife (Basel, Switzerland) · 2025
    Article
  5. Review
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  18. The Role of Ribosomal Protein S6 Kinases in Plant Homeostasis.Frontiers in molecular biosciences · 2021
    Review
  19. Translational gene regulation in plants: A green new deal.Wiley interdisciplinary reviews. RNA · 2020
    Review
  20. Evidence That Phosphorylation of theFrontiers in plant science · 2020
    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

6 authors at 4 institutions in 1 country.

Edouard Boex-FontvieilleInstitut de Biologie des Plantes, CNRS UMR 8618, Saclay Plant Sciences, Université Paris-Sud, Orsay, France.
Marlène Daventure
Mathieu Jossier
Michel Zivy
Michael Hodges
Guillaume Tcherkez
Centre de Génétique Moléculaire · FRCentre National de la Recherche Scientifique · FRInstitut des Sciences des Plantes de Paris Saclay · FRUniversité Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photosynthetic CO2 assimilation is the carbon source for plant anabolism, including amino acid production and protein synthesis. The biosynthesis of leaf proteins is known for decades to correlate with photosynthetic activity but the mechanisms controlling this effect are not documented. The cornerstone of the regulation of protein synthesis is believed to be translation initiation, which involves multiple phosphorylation events in Eukaryotes. We took advantage of phosphoproteomic methods applied to Arabidopsis thaliana rosettes harvested under controlled photosynthetic gas-exchange conditions to characterize the phosphorylation pattern of ribosomal proteins (RPs) and eukaryotic initiation factors (eIFs). The analyses detected 14 and 11 new RP and eIF phosphorylation sites, respectively, revealed significant CO2-dependent and/or light/dark phosphorylation patterns and showed concerted changes in 13 eIF phosphorylation sites and 9 ribosomal phosphorylation sites. In addition to the well-recognized role of the ribosomal small subunit protein RPS6, our data indicate the involvement of eIF3, eIF4A, eIF4B, eIF4G and eIF5 phosphorylation in controlling translation initiation when photosynthesis varies. The response of protein biosynthesis to the photosynthetic input thus appears to be the result of a complex regulation network involving both stimulating (e.g. RPS6, eIF4B phosphorylation) and inhibiting (e.g. eIF4G phosphorylation) molecular events.

Indexed as

ArabidopsisArabidopsis ProteinsEukaryotic Initiation FactorsPhosphorylationPhotosynthesisPlant LeavesProtein BiosynthesisArabidopsis ProteinsEukaryotic Initiation Factors

Identifiers

PMID23894680
PMCPMC3722150
OpenAlexW1978199907

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.