Evidence map›Paper›PMID 41068994›Full record

ArticlePhysiologia plantarum

AtSnRK2.4 Functions as an ABA-Responsive Protein Kinase in Arabidopsis.

Mattia Adamo, Colette Tournaire-Roux, Valérie Rofidal, Philippe Nacry, Vincent Demolombe, Amandine Crabos, Christophe Maurel, Véronique Santoni

Abstract read
In one paragraph

Article in Physiologia plantarum. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Review
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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

8 authors.

Mattia AdamoInstitute for Plant Sciences of Montpellier, University Montpellier, CNRS, INRAE, Institut Agro, Montpellier, France.
Colette Tournaire-RouxInstitute for Plant Sciences of Montpellier, University Montpellier, CNRS, INRAE, Institut Agro, Montpellier, France.
Valérie RofidalInstitute for Plant Sciences of Montpellier, University Montpellier, CNRS, INRAE, Institut Agro, Montpellier, France.
Philippe NacryInstitute for Plant Sciences of Montpellier, University Montpellier, CNRS, INRAE, Institut Agro, Montpellier, France.
Vincent DemolombeInstitute for Plant Sciences of Montpellier, University Montpellier, CNRS, INRAE, Institut Agro, Montpellier, France.
Amandine CrabosInstitute for Plant Sciences of Montpellier, University Montpellier, CNRS, INRAE, Institut Agro, Montpellier, France.
Christophe MaurelInstitute for Plant Sciences of Montpellier, University Montpellier, CNRS, INRAE, Institut Agro, Montpellier, France.
Véronique SantoniInstitute for Plant Sciences of Montpellier, University Montpellier, CNRS, INRAE, Institut Agro, Montpellier, France.ORCID https://orcid.org/0000-0002-1437-0921

Funding

Agence Nationale de la Recherche ANR-18-CE92-0055-01
6 · The paper itself

Abstract

In Arabidopsis, members of subclasses I and III of sucrose non-fermenting 1-related subfamily protein kinases 2 (SnRK2) are considered to be mainly osmotic- and ABA-responsive, respectively. In this work, we report on the role of SnRK2.4, a member of subclass I, in shaping plant root architecture (e.g., lateral root growth and root primordia emergence) in response to exogenous ABA. We show that SnRK2.4 is active in standard conditions and upon ABA treatment, with a higher ABA sensitivity than SnRK2.2 and SnRK2.3 from class III. To identify the molecular substrates of SnRK2.4, we compared the transcriptome, proteome, and phosphoproteome of wild-type and snrk2.4 plants, in standard conditions and after a 1 μM ABA treatment. The phosphoproteomic analysis, which relies on 3858 unique phosphopeptides corresponding to 1820 phosphoproteins, revealed that 186 and 277 proteins were under-phosphorylated in snrk2.4 mutants, in control conditions and upon ABA treatment, respectively. A regulation by SnRK2.4 of membrane transporters and cell-to-cell communication was highlighted in both conditions. By contrast, in response to ABA, SnRK2.4 specifically induced a decreased abundance of RNA helicases, suggesting that SnRK2.4 can interfere with mRNA splicing. SnRK2.4 also modulated the phosphorylation of proteins putatively involved in attenuation of ABA signaling, in lipid signaling, and in cellulose biosynthesis, via a complex PK cascade involving mainly calcium-dependent PKs. This work shows that SnRK2.4 is an ABA-responsive SnRK2, with high hormone sensitivity and putative roles in fundamental aspects of cell physiology.

Indexed as

Abscisic AcidArabidopsisArabidopsis ProteinsProtein KinasesProtein Serine-Threonine KinasesGene Expression Regulation, PlantPhosphorylationPlant Growth RegulatorsPlant RootsAbscisic AcidArabidopsis ProteinsPlant Growth RegulatorsProtein KinasesProtein Serine-Threonine KinasesSnRK2 protein, Arabidopsisabscisic acidphospho‐proteomicsprotein kinaseroot developmentsignalingSnRK2.4

Identifiers

PMID41068994
PMCPMC12511474

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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.