Evidence map›Paper›PMID 18768909›Full record

ArticlePlant physiology2008

Protein tyrosine kinases and protein tyrosine phosphatases are involved in abscisic acid-dependent processes in Arabidopsis seeds and suspension cells.

Thanos Ghelis, Gérard Bolbach, Gilles Clodic, Yvette Habricot, Emile Miginiac, Bruno Sotta, Emmanuelle Jeannette

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.7field-weighted citation impact, top 8% 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

40 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
  2. Emerging Functions of Protein Tyrosine Phosphatases in Plants.International journal of molecular sciences · 2024
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. ArabidopsisInternational journal of molecular sciences · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. H2Bub1 RegulatesPlant physiology · 2020
    Article
  15. Article
  16. Article
  17. Review
  18. GBS Mapping and Analysis of Genes Conserved betweenInternational journal of molecular sciences · 2018
    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

7 authors at 5 institutions in 1 country.

Thanos GhelisUPMC Université Paris 06, UMR 7180, Laboratoire de Physiologie Cellulaire et Moléculaire des Plantes, 94200 Ivry sur Seine, France. thanos.ghelis@upmc.fr
Gérard Bolbach
Gilles Clodic
Yvette Habricot
Emile Miginiac
Bruno Sotta
Emmanuelle Jeannette
Protéomique, Réponse Inflammatoire et Spectrométrie de Masse · FRCentre National de la Recherche Scientifique · FRLaboratoire de Chémo-biologie synthétique et thérapeutique · FRLaboratoire de physiologie cellulaire et moléculaireSorbonne Université · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein tyrosine (Tyr) phosphorylation plays a central role in many signaling pathways leading to cell growth and differentiation in animals. Tyr phosphorylated proteins have been detected in higher plants, and the roles of protein Tyr phosphatases and protein Tyr kinases in some physiological responses have been shown. We investigated the involvement of Tyr phosphorylation events in abscisic acid (ABA) signaling using a pharmacological approach. Phenylarsine oxide, a specific inhibitor of protein Tyr phosphatase activity, abolished the ABA-dependent accumulation of RAB18 (responsive to ABA 18) transcripts. Protein Tyr kinase inhibitors like genistein, tyrphostin A23, and erbstatin blocked the RAB18 expression induced by ABA in Arabidopsis (Arabidopsis thaliana). Stomatal closure induced by ABA was also inhibited by phenylarsine oxide and genistein. We studied the changes in the Tyr phosphorylation levels of proteins in Arabidopsis seeds after ABA treatment. Proteins were separated by two-dimensional gel electrophoresis, and those phosphorylated on Tyr residues were detected using an anti-phosphotyrosine antibody by western blot. Changes were detected in the Tyr phosphorylation levels of 19 proteins after ABA treatment. Genistein inhibited the ABA-dependent Tyr phosphorylation of proteins. The 19 proteins were analyzed by matrix-assisted laser-desorption ionization time-of-flight/time-of-flight mass spectrometry. Among the proteins identified were storage proteins like cruciferins, enzymes involved in the mobilization of lipid reserves like aconitase, enolase, aldolase, and a lipoprotein, and enzymes necessary for seedling development like the large subunit of Rubisco. Additionally, the identification of three putative signaling proteins, a peptidyl-prolyl isomerase, an RNA-binding protein, and a small ubiquitin-like modifier-conjugating enzyme, enlightens how Tyr phosphorylation might regulate ABA transduction pathways in plants.

Indexed as

Abscisic AcidArabidopsisElectrophoresis, Gel, Two-DimensionalEnzyme InhibitorsGenisteinHydroquinonesPhosphorylationProtein-Tyrosine KinasesProtein Tyrosine PhosphatasesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTyrphostinsAbscisic AcidEnzyme InhibitorserbstatinGenisteinHydroquinonesProtein-Tyrosine KinasesProtein Tyrosine Phosphatasestyrphostin A23Tyrphostins

Identifiers

PMID18768909
PMCPMC2577241
OpenAlexW1972243836

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.