Evidence map›Paper›PMID 23569110›Full record

ArticlePlant physiology2013

Nuclear accumulation of cytosolic glyceraldehyde-3-phosphate dehydrogenase in cadmium-stressed Arabidopsis roots.

Marco Vescovi, Mirko Zaffagnini, Margherita Festa, Paolo Trost, Fiorella Lo Schiavo, Alex Costa

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
14.8field-weighted citation impact, top 1% 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

60 citing papers in PubMed, 116 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Perception and processing of stress signals by plant mitochondria.The Plant journal : for cell and molecular biology · 2024
    Review
  10. Article
  11. Identification and expression profiling ofFrontiers in plant science · 2024
    Article
  12. Phosphatidic acid signaling and function in nuclei.Progress in lipid research · 2024
    Review
  13. 'Autophagy · 2023
    Article
  14. Redox Signaling in Plant Heat Stress Response.Antioxidants (Basel, Switzerland) · 2023
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  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

6 authors at 3 institutions in 1 country.

Marco VescoviDepartment of Biology, University of Padua, 35131 Padua, Italy.
Mirko Zaffagnini
Margherita Festa
Paolo Trost
Fiorella Lo Schiavo
Alex Costa
University of Bologna · ITUniversity of Padua · ITUniversity of Milan · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NAD-dependent glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a ubiquitous enzyme involved in the glycolytic pathway. It has been widely demonstrated that mammalian GAPDH, in addition to its role in glycolysis, fulfills alternative functions mainly linked to its susceptibility to oxidative posttranslational modifications. Here, we investigated the responses of Arabidopsis (Arabidopsis thaliana) cytosolic GAPDH isoenzymes GAPC1 and GAPC2 to cadmium-induced stress in seedlings roots. GAPC1 was more responsive to cadmium than GAPC2 at the transcriptional level. In vivo, cadmium treatments induced different concomitant effects, including (1) nitric oxide accumulation, (2) cytosolic oxidation (e.g. oxidation of the redox-sensitive Green fluorescent protein2 probe), (3) activation of the GAPC1 promoter, (4) GAPC1 protein accumulation in enzymatically inactive form, and (5) strong relocalization of GAPC1 to the nucleus. All these effects were detected in the same zone of the root tip. In vitro, GAPC1 was inactivated by either nitric oxide donors or hydrogen peroxide, but no inhibition was directly provided by cadmium. Interestingly, nuclear relocalization of GAPC1 under cadmium-induced oxidative stress was stimulated, rather than inhibited, by mutating into serine the catalytic cysteine of GAPC1 (C155S), excluding an essential role of GAPC1 nitrosylation in the mechanism of nuclear relocalization, as found in mammalian cells. Although the function of GAPC1 in the nucleus is unknown, our results suggest that glycolytic GAPC1, through its high sensitivity to the cellular redox state, may play a role in oxidative stress signaling or protection in plants.

Indexed as

ArabidopsisArabidopsis ProteinsCadmiumCell NucleusCytosolGene ExpressionGenotypeGlutathioneGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)Hydrogen PeroxideMutagenesis, InsertionalNitric OxideOxidation-ReductionOxidative StressPlant RootsPlants, Genetically ModifiedArabidopsis ProteinsCadmiumGAPC1 protein, ArabidopsisGlutathioneGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)Hydrogen PeroxideNitric OxideRecombinant Fusion ProteinsRNA, MessengerRNA, Plant

Identifiers

PMID23569110
PMCPMC3641213
OpenAlexW2161003382

What OpenQuestion holds

Textmetadata
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.