Evidence map›Paper›PMID 23170036›Full record

ArticleThe Plant cell2012

The ubiquitin ligase PUB22 targets a subunit of the exocyst complex required for PAMP-triggered responses in Arabidopsis.

Martin Stegmann, Ryan G Anderson, Kazuya Ichimura, Tamara Pecenkova, Patrick Reuter, Viktor Žársky, John M McDowell, Ken Shirasu, Marco Trujillo

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.

0numbers the graph read from it
0cells of the map it votes in
121citing papers in PubMed
6.2field-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

121 citing papers in PubMed, 237 citations in OpenAlex.

  1. Review
  2. Review
  3. Plants (Basel, Switzerland) · 2026
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  8. Interaction Between Glycoside Hydrolase FsGH28c fromInternational journal of molecular sciences · 2025
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  12. TheFrontiers in plant science · 2025
    Article
  13. Article
  14. The Multifaceted Ubiquitination of BIK1 During Plant Immunity inInternational journal of molecular sciences · 2024
    Review
  15. Review
  16. Article
  17. Proteolysis in plant immunity.The Plant cell · 2024
    Review
  18. Article
  19. Article
  20. Article

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

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

9 authors at 7 institutions in 4 countries.

Martin StegmannLeibniz Institute of Plant Biochemistry, D-06120 Halle (Saale), Germany.
Ryan G Anderson
Kazuya Ichimura
Tamara Pecenkova
Patrick Reuter
Viktor Žársky
John M McDowell
Ken Shirasu
Marco Trujillo
University of Würzburg · DEVirginia Tech · USCharles University · CZCzech Academy of Sciences, Institute of Experimental Botany · CZKagawa University · JPLeibniz Institute of Plant Biochemistry · DERIKEN Center for Sustainable Resource Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant pathogens are perceived by pattern recognition receptors, which are activated upon binding to pathogen-associated molecular patterns (PAMPs). Ubiquitination and vesicle trafficking have been linked to the regulation of immune signaling. However, little information exists about components of vesicle trafficking involved in immune signaling and the mechanisms that regulate them. In this study, we identified Arabidopsis thaliana Exo70B2, a subunit of the exocyst complex that mediates vesicle tethering during exocytosis, as a target of the plant U-box-type ubiquitin ligase 22 (PUB22), which acts in concert with PUB23 and PUB24 as a negative regulator of PAMP-triggered responses. We show that Exo70B2 is required for both immediate and later responses triggered by all tested PAMPs, suggestive of a role in signaling. Exo70B2 is also necessary for the immune response against different pathogens. Our data demonstrate that PUB22 mediates the ubiquitination and degradation of Exo70B2 via the 26S Proteasome. Furthermore, degradation is regulated by the autocatalytic turnover of PUB22, which is stabilized upon PAMP perception. We therefore propose a mechanism by which PUB22-mediated degradation of Exo70B2 contributes to the attenuation of PAMP-induced signaling.

Indexed as

ArabidopsisArabidopsis ProteinsCell DeathGene Expression Regulation, PlantHost-Pathogen InteractionsMutationOomycetesPhylogenyPlant DiseasesPlant LeavesPlant RootsProteasome Endopeptidase ComplexProteolysisPseudomonas syringaeReceptors, Pattern RecognitionRecombinant Fusion ProteinsArabidopsis ProteinsATP dependent 26S proteaseExo70B2 protein, ArabidopsisProteasome Endopeptidase ComplexPUB22 protein, ArabidopsisReceptors, Pattern RecognitionRecombinant Fusion ProteinsUbiquitinUbiquitin-Protein LigasesVesicular Transport Proteins

Identifiers

PMID23170036
PMCPMC3531861
OpenAlexW2124825049

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.