Evidence map›Paper›PMID 18708476›Full record

ArticleThe Plant cell2008

RD19, an Arabidopsis cysteine protease required for RRS1-R-mediated resistance, is relocalized to the nucleus by the Ralstonia solanacearum PopP2 effector.

Maud Bernoux, Ton Timmers, Alain Jauneau, Christian Brière, Pierre J G M de Wit, Yves Marco, Laurent Deslandes

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
16.0field-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

104 citing papers in PubMed, 218 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Pathogen-inspired engineering of plant protease enhances late blight resistance.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  13. APlants (Basel, Switzerland) · 2025
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  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
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  20. Article

44 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 2 countries.

Maud BernouxLaboratoire des Interactions Plantes Microorganismes, Unité Mixte de Recherche, Centre National de la Recherche Scientifique-Institut National de la Recherche Agronomique 2594/441, F-31320 Castanet-Tolosan, France.
Ton Timmers
Alain Jauneau
Christian Brière
Pierre J G M de Wit
Yves Marco
Laurent Deslandes
Centre National de la Recherche Scientifique · FRLaboratoire des Interactions Plantes Micro-Organismes · FRCentre for BioSystems Genomics · NLInstitut d'Imagerie Biomédicale · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial wilt, a disease impacting cultivated crops worldwide, is caused by the pathogenic bacterium Ralstonia solanacearum. PopP2 (for Pseudomonas outer protein P2) is an R. solanacearum type III effector that belongs to the YopJ/AvrRxv protein family and interacts with the Arabidopsis thaliana RESISTANT TO RALSTONIA SOLANACEARUM 1-R (RRS1-R) resistance protein. RRS1-R contains the Toll/Interleukin1 receptor-nucleotide binding site-Leu-rich repeat domains found in several cytoplasmic R proteins and a C-terminal WRKY DNA binding domain. In this study, we identified the Arabidopsis Cys protease RESPONSIVE TO DEHYDRATION19 (RD19) as being a PopP2-interacting protein whose expression is induced during infection by R. solanacearum. An Arabidopsis rd19 mutant in an RRS1-R genetic background is compromised in resistance to the bacterium, indicating that RD19 is required for RRS1-R-mediated resistance. RD19 normally localizes in mobile vacuole-associated compartments and, upon coexpression with PopP2, is specifically relocalized to the plant nucleus, where the two proteins physically interact. No direct physical interaction between RRS1-R and RD19 in the presence of PopP2 was detected in the nucleus as determined by Förster resonance energy transfer. We propose that RD19 associates with PopP2 to form a nuclear complex that is required for activation of the RRS1-R-mediated resistance response.

Indexed as

ArabidopsisArabidopsis ProteinsBacterial ProteinsCell NucleusCysteine EndopeptidasesGene Expression Regulation, PlantMicroscopy, FluorescencePlant DiseasesPlants, Genetically ModifiedRalstonia solanacearumReverse Transcriptase Polymerase Chain ReactionArabidopsis ProteinsBacterial ProteinsCysteine Endopeptidases

Identifiers

PMID18708476
PMCPMC2553607
OpenAlexW2116439866

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.