Evidence map›Paper›PMID 21994172›Full record

ArticleJournal of experimental botany2012

Evidence that abscisic acid promotes degradation of SNF1-related protein kinase (SnRK) 1 in wheat and activation of a putative calcium-dependent SnRK2.

Patricia Coello, Emi Hirano, Sandra J Hey, Nira Muttucumaru, Eleazar Martinez-Barajas, Martin A J Parry, Nigel G Halford

Open access · bronzeAbstract read
In one paragraph

Article in Journal of experimental botany, 2012. 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
7.0field-weighted citation impact, top 3% 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, 94 citations in OpenAlex.

  1. Article
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  12. Regulation of Flowering Timing by ABA-NnSnRK1 Signaling Pathway in Lotus.International journal of molecular sciences · 2021
    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

7 authors at 2 institutions in 3 countries.

Patricia CoelloDepartamento de Bioquímica, Facultad de Química, Universidad Nacional Autónoma de México, Distrito Federal 04510, Mexico.
Emi Hirano
Sandra J Hey
Nira Muttucumaru
Eleazar Martinez-Barajas
Martin A J Parry
Nigel G Halford
Rothamsted Research · GBUniversidad Nacional Autónoma de México · MX

Funding

Biotechnology and Biological Sciences Research Council BBS/E/C/00004150Biotechnology and Biological Sciences Research Council BBS/E/C/00004952
6 · The paper itself

Abstract

Sucrose nonfermenting-1 (SNF1)-related protein kinases (SnRKs) form a major family of signalling proteins in plants and have been associated with metabolic regulation and stress responses. They comprise three subfamilies: SnRK1, SnRK2, and SnRK3. SnRK1 plays a major role in the regulation of carbon metabolism and energy status, while SnRKs 2 and 3 have been implicated in stress and abscisic acid (ABA)-mediated signalling pathways. The burgeoning and divergence of this family of protein kinases in plants may have occurred to enable cross-talk between metabolic and stress signalling, and ABA-response-element-binding proteins (AREBPs), a family of transcription factors, have been shown to be substrates for members of all three subfamilies. In this study, levels of SnRK1 protein were shown to decline dramatically in wheat roots in response to ABA treatment, although the amount of phosphorylated (active) SnRK1 remained constant. Multiple SnRK2-type protein kinases were detectable in the root extracts and showed differential responses to ABA treatment. They included a 42 kDa protein that appeared to reduce in response to 3 h of ABA treatment but to recover after longer treatment. There was a clear increase in phosphorylation of this SnRK2 in response to the ABA treatment. Fractions containing this 42 kDa SnRK2 were shown to phosphorylate synthetic peptides with amino acid sequences based on those of conserved phosphorylation sites in AREBPs. The activity increased 8-fold with the addition of calcium chloride, indicating that it is calcium-dependent. The activity assigned to the 42 kDa SnRK2 also phosphorylated a heterologously expressed wheat AREBP.

Indexed as

Abscisic AcidAmino Acid SequenceCalcium ChlorideGene Expression Regulation, PlantPhosphorylationPlant ProteinsPlant RootsProtein Serine-Threonine KinasesProteolysisSequence AlignmentSignal TransductionStress, PhysiologicalTriticumAbscisic AcidCalcium ChloridePlant ProteinsProtein Serine-Threonine KinasesSNF1-related protein kinases

Identifiers

PMID21994172
PMCPMC3254688
OpenAlexW2097305183

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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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.