Evidence map›Paper›PMID 27436712›Full record

ArticleThe Plant cell2016

The Arabidopsis SR45 Splicing Factor, a Negative Regulator of Sugar Signaling, Modulates SNF1-Related Protein Kinase 1 Stability.

Raquel F Carvalho, Dóra Szakonyi, Craig G Simpson, Inês C R Barbosa, John W S Brown, Elena Baena-González, Paula Duque

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2016. 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
18.5field-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

40 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Genome-Wide Isoform Switching Reveals SR45-Mediated Splicing Control ofInternational journal of molecular sciences · 2025
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  11. Article
  12. Review
  13. Article
  14. Article
  15. Alternative Splicing Regulation ofFrontiers in plant science · 2022
    Article
  16. Review
  17. Review
  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

7 authors at 2 institutions in 2 countries.

Raquel F CarvalhoInstituto Gulbenkian de Ciência, 2780-156 Oeiras, Portugal.ORCID 0000-0002-6899-6516
Dóra SzakonyiInstituto Gulbenkian de Ciência, 2780-156 Oeiras, Portugal.ORCID 0000-0002-9189-629X
Craig G SimpsonThe James Hutton Institute, Invergowrie, Dundee DD2 5DA, Scotland, United Kingdom.ORCID 0000-0002-1723-1492
Inês C R BarbosaInstituto Gulbenkian de Ciência, 2780-156 Oeiras, Portugal.
John W S BrownThe James Hutton Institute, Invergowrie, Dundee DD2 5DA, Scotland, United Kingdom University of Dundee at The James Hutton Institute, Invergowrie, Dundee DD2 5DA, Scotland, United Kingdom.ORCID 0000-0003-2979-779X
Elena Baena-GonzálezInstituto Gulbenkian de Ciência, 2780-156 Oeiras, Portugal.ORCID 0000-0001-6598-3579
Paula DuqueInstituto Gulbenkian de Ciência, 2780-156 Oeiras, Portugal duquep@igc.gulbenkian.pt.ORCID 0000-0002-4910-2900
Instituto Gulbenkian de Ciência · PTJames Hutton Institute · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ability to sense and respond to sugar signals allows plants to cope with environmental and metabolic changes by adjusting growth and development accordingly. We previously reported that the SR45 splicing factor negatively regulates glucose signaling during early seedling development in Arabidopsis thaliana Here, we show that under glucose-fed conditions, the Arabidopsis sr45-1 loss-of-function mutant contains higher amounts of the energy-sensing SNF1-Related Protein Kinase 1 (SnRK1) despite unaffected SnRK1 transcript levels. In agreement, marker genes for SnRK1 activity are upregulated in sr45-1 plants, and the glucose hypersensitivity of sr45-1 is attenuated by disruption of the SnRK1 gene. Using a high-resolution RT-PCR panel, we found that the sr45-1 mutation broadly targets alternative splicing in vivo, including that of the SR45 pre-mRNA itself. Importantly, the enhanced SnRK1 levels in sr45-1 are suppressed by a proteasome inhibitor, indicating that SR45 promotes targeting of the SnRK1 protein for proteasomal destruction. Finally, we demonstrate that SR45 regulates alternative splicing of the Arabidopsis 5PTase13 gene, which encodes an inositol polyphosphate 5-phosphatase previously shown to interact with and regulate the stability of SnRK1 in vitro, thus providing a mechanistic link between SR45 function and the modulation of degradation of the SnRK1 energy sensor in response to sugars.

Indexed as

Alternative SplicingArabidopsisArabidopsis ProteinsPhosphoric Monoester HydrolasesProtein Serine-Threonine KinasesProtein StabilityReverse Transcriptase Polymerase Chain ReactionRNA-Binding Proteins5PTase13 protein, ArabidopsisArabidopsis ProteinsPhosphoric Monoester HydrolasesProtein Serine-Threonine KinasesRNA-Binding ProteinsSNF1-related protein kinasesSR45a protein, Arabidopsis

Identifiers

PMID27436712
PMCPMC5006706
OpenAlexW2490757565

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.