Evidence map›Paper›PMID 31589140›Full record

ArticleeLife2019

Dynamic ubiquitination determines transcriptional activity of the plant immune coactivator NPR1.

Michael J Skelly, James J Furniss, Heather Grey, Ka-Wing Wong, Steven H Spoel

Open access · goldAbstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
8.1field-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

33 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Towards an integrated molecular understanding of plant hormones.Journal of integrative plant biology · 2026
    Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Protein Dynamics in Plant Immunity: Insights into Plant-Pest Interactions.International journal of molecular sciences · 2024
    Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Proteolysis in plant immunity.The Plant cell · 2024
    Review
  16. Ubiquitin-specific protease UBP14 stabilizes HY5 by deubiquitination to promote photomorphogenesis inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Article
  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

5 authors at 1 institution in 1 country.

Michael J SkellyInstitute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, Edinburgh, United Kingdom.ORCID 0000-0002-9024-0037
James J FurnissInstitute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, Edinburgh, United Kingdom.
Heather GreyInstitute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, Edinburgh, United Kingdom.
Ka-Wing WongInstitute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, Edinburgh, United Kingdom.
Steven H SpoelInstitute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, Edinburgh, United Kingdom.ORCID 0000-0003-4340-7591
University of Edinburgh · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L006219/1H2020 European Research Council 678511Royal Society UF090321
6 · The paper itself

Abstract

Activation of systemic acquired resistance in plants is associated with transcriptome reprogramming induced by the unstable coactivator NPR1. Immune-induced ubiquitination and proteasomal degradation of NPR1 are thought to facilitate continuous delivery of active NPR1 to target promoters, thereby maximising gene expression. Because of this potentially costly sacrificial process, we investigated if ubiquitination of NPR1 plays transcriptional roles prior to its proteasomal turnover. Here we show ubiquitination of NPR1 is a progressive event in which initial modification by a Cullin-RING E3 ligase promotes its chromatin association and expression of target genes. Only when polyubiquitination of NPR1 is enhanced by the E4 ligase, UBE4, it is targeted for proteasomal degradation. Conversely, ubiquitin ligase activities are opposed by UBP6/7, two proteasome-associated deubiquitinases that enhance NPR1 longevity. Thus, immune-induced transcriptome reprogramming requires sequential actions of E3 and E4 ligases balanced by opposing deubiquitinases that fine-tune activity of NPR1 without strict requirement for its sacrificial turnover.

Indexed as

Transcription, GeneticUbiquitinationArabidopsisArabidopsis ProteinsCrops, AgriculturalProteasome Endopeptidase ComplexArabidopsis ProteinsNPR1 protein, ArabidopsisProteasome Endopeptidase ComplexA. thalianaNPR1plant biologyplant immunitysalicylic acidsystemic acquired resistanceubiquitin

Identifiers

PMID31589140
PMCPMC6850887
OpenAlexW2979583772

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.