Evidence map›Paper›PMID 25368622›Full record

ArticleFrontiers in plant science2014

Sustained mitogen-activated protein kinase activation reprograms defense metabolism and phosphoprotein profile in Arabidopsis thaliana.

Ines Lassowskat, Christoph Böttcher, Lennart Eschen-Lippold, Dierk Scheel, Justin Lee

Open access · goldAbstract read
In one paragraph

Article in Frontiers in plant science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
11.7field-weighted citation impact, top 2% 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

32 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. MAPK Cascades in Plant Microbiota Structure and Functioning.Journal of microbiology (Seoul, Korea) · 2024
    Review
  5. Article
  6. Review
  7. Article
  8. TALEN-BasedFrontiers in plant science · 2021
    Article
  9. Sustained Incompatibility between MAPK Signaling and Pathogen Effectors.International journal of molecular sciences · 2020
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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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

5 authors at 2 institutions in 1 country.

Ines LassowskatDepartment of Stress and Developmental Biology, Leibniz Institute of Plant Biochemistry Halle/Saale, Germany.
Christoph BöttcherDepartment of Stress and Developmental Biology, Leibniz Institute of Plant Biochemistry Halle/Saale, Germany ; Federal Research Centre for Cultivated Plants, Institute for Ecological Chemistry, Plant Analysis and Stored Product Protection, Julius Kühn Institute Berlin, Germany.
Lennart Eschen-LippoldDepartment of Stress and Developmental Biology, Leibniz Institute of Plant Biochemistry Halle/Saale, Germany.
Dierk ScheelDepartment of Stress and Developmental Biology, Leibniz Institute of Plant Biochemistry Halle/Saale, Germany.
Justin LeeDepartment of Stress and Developmental Biology, Leibniz Institute of Plant Biochemistry Halle/Saale, Germany.
Leibniz Institute of Plant Biochemistry · DEJulius Kühn-Institut · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitogen-activated protein kinases (MAPKs) target a variety of protein substrates to regulate cellular signaling processes in eukaryotes. In plants, the number of identified MAPK substrates that control plant defense responses is still limited. Here, we generated transgenic Arabidopsis thaliana plants with an inducible system to simulate in vivo activation of two stress-activated MAPKs, MPK3, and MPK6. Metabolome analysis revealed that this artificial MPK3/6 activation (without any exposure to pathogens or other stresses) is sufficient to drive the production of major defense-related metabolites, including various camalexin, indole glucosinolate and agmatine derivatives. An accompanying (phospho)proteome analysis led to detection of hundreds of potential phosphoproteins downstream of MPK3/6 activation. Besides known MAPK substrates, many candidates on this list possess typical MAPK-targeted phosphosites and in many cases, the corresponding phosphopeptides were detected by mass spectrometry. Notably, several of these putative phosphoproteins have been reported to be associated with the biosynthesis of antimicrobial defense substances (e.g., WRKY transcription factors and proteins encoded by the genes from the "PEN" pathway required for penetration resistance to filamentous pathogens). Thus, this work provides an inventory of candidate phosphoproteins, including putative direct MAPK substrates, for future analysis of MAPK-mediated defense control. (Proteomics data are available with the identifier PXD001252 via ProteomeXchange, http://proteomecentral.proteomexchange.org).

Indexed as

defenseMAPK substratesmetabolomicsphosphoproteomicsphosphorylationphytoalexins

Identifiers

PMID25368622
PMCPMC4202796
OpenAlexW2041536977

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.