Evidence map›Paper›PMID 26662259›Full record

ArticleThe Plant journal : for cell and molecular biology2016

SUMOylation represses SnRK1 signaling in Arabidopsis.

Pierre Crozet, Leonor Margalha, Rafal Butowt, Noémia Fernandes, Carlos A Elias, Beatriz Orosa, Konstantin Tomanov, Markus Teige, Andreas Bachmair, Ari Sadanandom and 1 more

Abstract read
In one paragraph

Article in The Plant journal : for cell and molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Sugar signaling modulates SHOOT MERISTEMLESS expression and meristem function inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Article
  9. Review
  10. Signalling mechanisms and cellular functions of SUMO.Nature reviews. Molecular cell biology · 2022
    Review
  11. Article
  12. Article
  13. Article
  14. Cells · 2021
    Article
  15. Review
  16. Review
  17. Article
  18. 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

11 authors.

Pierre Crozet *Rua da Quinta Grande 6, Instituto Gulbenkian de Ciência, Oeiras 2780-156, Portugal.
Leonor Margalha *Rua da Quinta Grande 6, Instituto Gulbenkian de Ciência, Oeiras 2780-156, Portugal.
Rafal ButowtRua da Quinta Grande 6, Instituto Gulbenkian de Ciência, Oeiras 2780-156, Portugal.
Noémia FernandesRua da Quinta Grande 6, Instituto Gulbenkian de Ciência, Oeiras 2780-156, Portugal.
Carlos A EliasRua da Quinta Grande 6, Instituto Gulbenkian de Ciência, Oeiras 2780-156, Portugal.
Beatriz OrosaSchool of Biological and Biomedical Sciences, University of Durham, Durham, UK.
Konstantin TomanovDepartment of Biochemistry and Cell Biology, Max F. Perutz Laboratories, Vienna BioCenter, University of Vienna, Vienna A-1030, Austria.
Markus TeigeDepartment of Ecogenomics and Systems Biology, University of Vienna, Althanstr. 14, Vienna A-1090, Austria.
Andreas BachmairDepartment of Biochemistry and Cell Biology, Max F. Perutz Laboratories, Vienna BioCenter, University of Vienna, Vienna A-1030, Austria.
Ari SadanandomSchool of Biological and Biomedical Sciences, University of Durham, Durham, UK.
Elena Baena-GonzálezRua da Quinta Grande 6, Instituto Gulbenkian de Ciência, Oeiras 2780-156, Portugal.

Funding

Austrian Science Fund FWF P 23435Austrian Science Fund FWF P 25488Austrian Science Fund FWF P 28491
6 · The paper itself

Abstract

The SnRK1 protein kinase balances cellular energy levels in accordance with extracellular conditions and is thereby key for plant stress tolerance. In addition, SnRK1 has been implicated in numerous growth and developmental processes from seed filling and maturation to flowering and senescence. Despite its importance, the mechanisms that regulate SnRK1 activity are poorly understood. Here, we demonstrate that the SnRK1 complex is SUMOylated on multiple subunits and identify SIZ1 as the E3 Small Ubiquitin-like Modifier (SUMO) ligase responsible for this modification. We further show that SnRK1 is ubiquitinated in a SIZ1-dependent manner, causing its degradation through the proteasome. In consequence, SnRK1 degradation is deficient in siz1-2 mutants, leading to its accumulation and hyperactivation of SnRK1 signaling. Finally, SnRK1 degradation is strictly dependent on its activity, as inactive SnRK1 variants are aberrantly stable but recover normal degradation when expressed as SUMO mimetics. Altogether, our data suggest that active SnRK1 triggers its own SUMOylation and degradation, establishing a negative feedback loop that attenuates SnRK1 signaling and prevents detrimental hyperactivation of stress responses.

Indexed as

Signal TransductionSumoylationArabidopsisArabidopsis ProteinsGene Expression Regulation, PlantLigasesMutationProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesSeedsUbiquitin-Protein LigasesArabidopsis ProteinsAt3g01090 protein, ArabidopsisLigasesProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesSIZ1 protein, ArabidopsisUbiquitin-Protein LigasesArabidopsis thalianaenergy signalingSIZ1SNF1-related protein kinase (SnRK1)stressSUMOylationubiquitination

Identifiers

PMID26662259
PMCPMC4817235

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Registered trials

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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.