Evidence map›Paper›PMID 32889173›Full record

ArticleMolecular plant2020

Phosphorylation of the Pseudomonas Effector AvrPtoB by Arabidopsis SnRK2.8 Is Required for Bacterial Virulence.

Lei Lei, Danielle M Stevens, Gitta Coaker

Open access · bronzeAbstract read
In one paragraph

Article in Molecular plant, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
7.0field-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

24 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. SnRK2s: Kinases or Substrates?Plants (Basel, Switzerland) · 2025
    Review
  6. Article
  7. Abscisic Acid Can Play a Dual Role in thePlants (Basel, Switzerland) · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Multiple host targets ofbioRxiv : the preprint server for biology · 2023
    Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Ubiquitination of Receptorsomes, Frontline of Plant Immunity.International journal of molecular sciences · 2022
    Review
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

3 authors at 1 institution in 1 country.

Lei LeiDepartment of Plant Pathology, University of California, Davis, Davis, CA, USA.
Danielle M StevensDepartment of Plant Pathology, University of California, Davis, Davis, CA, USA.
Gitta CoakerDepartment of Plant Pathology, University of California, Davis, Davis, CA, USA. Electronic address: glcoaker@ucdavis.edu.
University of California, Davis · US

Funding

Immune Perception of Bacterial Pathogens in PlantsR35GM136402 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI Gitta Laurel Coaker · 2020 to 2026
$3.0M
Elucidating RIN4_Mediated Immune Signaling Cascades in ArabidopsisR01GM092772 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI COAKER, GITTA LAUREL · 2010 to 2018
$2.8M
Phinney - Orbitrap Fusion ETDS10OD021801 · OD · UNIVERSITY OF CALIFORNIA AT DAVIS · PI PHINNEY, BRETT S · 2016 to 2016
$600k
NIGMS NIH HHS R01 GM092772NIGMS NIH HHS R35 GM136402NIH HHS S10 OD021801
6 · The paper itself

Abstract

A critical component controlling bacterial virulence is the delivery of pathogen effectors into plant cells during infection. Effectors alter host metabolism and immunity for the benefit of pathogens. Multiple effectors are phosphorylated by host kinases, and this posttranslational modification is important for their activity. We sought to identify host kinases involved in effector phosphorylation. Multiple phosphorylated effector residues matched the proposed consensus motif for the plant calcium-dependent protein kinase (CDPK) and Snf1-related kinase (SnRK) superfamily. The conserved Pseudomonas effector AvrPtoB acts as an E3 ubiquitin ligase and promotes bacterial virulence. In this study, we identified a member of the Arabidopsis SnRK family, SnRK2.8, which interacts with AvrPtoB in yeast and in planta. We showed that SnRK2.8 was required for AvrPtoB virulence functions, including facilitating bacterial colonization, suppression of callose deposition, and targeting the plant defense regulator NPR1 and analyses receptor FLS2. Mass spectrometry analysis revealed that AvrPtoB phosphorylation occurs at multiple serine residues in planta, with S258 phosphorylation significantly reduced in the snrk2.8 knockout. AvrPtoB phospho-null mutants exhibited compromised virulence functions and were unable to suppress NPR1 accumulation, FLS2 accumulation, or inhibit FLS2-BAK1 complex formation upon flagellin perception. Taken together, these data identify a conserved plant kinase utilized by a pathogen effector to promote disease.

Indexed as

ArabidopsisArabidopsis ProteinsBacterial ProteinsCalcium-Calmodulin-Dependent Protein KinasesPhosphorylationProtein KinasesProtein Serine-Threonine KinasesPseudomonas syringaeUbiquitin-Protein LigasesVirulenceArabidopsis ProteinsavrPto protein, Pseudomonas syringaeBacterial ProteinsCalcium-Calmodulin-Dependent Protein KinasesFLS2 protein, ArabidopsisProtein KinasesProtein Serine-Threonine KinasesSNF1-related protein kinasesSnRK2 protein, ArabidopsisUbiquitin-Protein LigasesArabidopsisAvrPtoBeffectorkinasePseudomonas syringaeSnRK2.8

Identifiers

PMID32889173
PMCPMC7808569
OpenAlexW3082201168

What OpenQuestion holds

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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.