Evidence map›Paper›PMID 29182677›Full record

ArticlePloS one2017

Arabidopsis ubiquitin ligase PUB12 interacts with and negatively regulates Chitin Elicitor Receptor Kinase 1 (CERK1).

Koji Yamaguchi, Hirohisa Mezaki, Masayuki Fujiwara, Yuki Hara, Tsutomu Kawasaki

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
7.6field-weighted citation impact, top 4% 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

21 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Ubiquitination of Receptorsomes, Frontline of Plant Immunity.International journal of molecular sciences · 2022
    Review
  13. Interactome of Arabidopsis Thaliana.Plants (Basel, Switzerland) · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. The ubiquitin system affects agronomic plant traits.The Journal of biological chemistry · 2020
    Review
  19. Review
  20. Activation of Early Defense Signals in Seedlings ofPlants (Basel, Switzerland) · 2020
    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 2 institutions in 1 country.

Koji YamaguchiDepartment of Advanced Bioscience, Graduate School of Agriculture, Kindai University, Nakamachi, Nara, Japan.
Hirohisa MezakiDepartment of Advanced Bioscience, Graduate School of Agriculture, Kindai University, Nakamachi, Nara, Japan.
Masayuki FujiwaraInstitute for Advanced Biosciences, Keio University, Tsuruoka, Yamagata, Japan.
Yuki HaraDepartment of Advanced Bioscience, Graduate School of Agriculture, Kindai University, Nakamachi, Nara, Japan.
Tsutomu KawasakiDepartment of Advanced Bioscience, Graduate School of Agriculture, Kindai University, Nakamachi, Nara, Japan.ORCID http://orcid.org/0000-0003-2579-2000
Kindai University · JPKeio University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In Arabidopsis, fungal chitin is recognized as a pathogen-associated molecular pattern (PAMP) by the chitin receptor complex containing the lysin-motif (LysM) receptor-like kinases CERK1 and LYK5. Upon the perception of chitin, CERK1 phosphorylates the receptor-like cytoplasmic kinase, PBL27, which activates the intracellular mitogen-activated protein kinase (MAPK) cascade. However, the mechanisms by which the CERK1-PBL27 complex is regulated remain largely unknown. We identified ubiquitin ligase PUB12 as a component of the PBL27 complex using co-immunoprecipitation and mass spectrometry. However, PUB12 did not interact directly with PBL27. Instead, the ARM domains of PUB12 and its paralog PUB13 interacted with the intracellular domain of CERK1 in a manner that was dependent on its autophosphorylation, suggesting that the phosphorylation-based auto-activation of CERK1 may be required for its interaction with PUB12. The co-expression of PUB12 in Nicotiana benthamiana reduced the accumulation of CERK1. The pub12 pub13 mutant exhibited enhanced chitin-induced immune responses such as ROS production, MAPK activation, and callose deposition. These results suggest that PUB12 and PUB13 are involved in the negative regulation of the chitin receptor complex, which may contribute to the transient desensitization of chitin-induced responses.

Indexed as

ArabidopsisArabidopsis ProteinsEnzyme ActivationMass SpectrometryNicotianaProtein BindingProtein Serine-Threonine KinasesUbiquitinationUbiquitin-Protein LigasesArabidopsis ProteinsCERK1 protein, ArabidopsisProtein Serine-Threonine KinasesPUB12 protein, ArabidopsisUbiquitin-Protein Ligases

Identifiers

PMID29182677
PMCPMC5705137
OpenAlexW2770890715

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.