Evidence map›Paper›PMID 32931489›Full record

ArticlePloS one2020

The rice NLR pair Pikp-1/Pikp-2 initiates cell death through receptor cooperation rather than negative regulation.

Rafał Zdrzałek, Sophien Kamoun, Ryohei Terauchi, Hiromasa Saitoh, Mark J Banfield

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
7.4field-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

29 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Plant NLRs are getting into higher-order architectures.The Plant journal : for cell and molecular biology · 2026
    Review
  3. Article
  4. Precision Editing of NLRS Improves Effector Recognition for Enhanced Disease Resistance.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  5. Article
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  11. Review
  12. Bioengineering a plant NLR immune receptor with a robust binding interface toward a conserved fungal pathogen effector.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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  15. Review
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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 4 institutions in 2 countries.

Rafał ZdrzałekDepartment of Biological Chemistry, John Innes Centre, Norwich, United Kingdom.ORCID 0000-0003-3669-924X
Sophien KamounThe Sainsbury Laboratory, University of East Anglia, Norwich, United Kingdom.ORCID 0000-0002-0290-0315
Ryohei TerauchiDivision of Genomics and Breeding, Iwate Biotechnology Research Centre, Iwate, Japan.ORCID 0000-0002-0095-4651
Hiromasa SaitohLaboratory of Plant Symbiotic and Parasitic Microbes, Department of Molecular Microbiology, Faculty of Life Sciences, Tokyo University of Agriculture, Tokyo, Japan.ORCID 0000-0002-0124-9276
Mark J BanfieldDepartment of Biological Chemistry, John Innes Centre, Norwich, United Kingdom.ORCID 0000-0001-8921-3835
John Innes Centre · GBKyoto University · JPTokyo University of Agriculture · JPUniversity of East Anglia · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M011216/1Biotechnology and Biological Sciences Research Council BB/M02198XBiotechnology and Biological Sciences Research Council BB/P012574
6 · The paper itself

Abstract

Plant NLR immune receptors are multidomain proteins that can function as specialized sensor/helper pairs. Paired NLR immune receptors are generally thought to function via negative regulation, where one NLR represses the activity of the second and detection of pathogen effectors relieves this repression to initiate immunity. However, whether this mechanism is common to all NLR pairs is not known. Here, we show that the rice NLR pair Pikp-1/Pikp-2, which confers resistance to strains of the blast pathogen Magnaporthe oryzae (syn. Pyricularia oryzae) expressing the AVR-PikD effector, functions via receptor cooperation, with effector-triggered activation requiring both NLRs to trigger the immune response. To investigate the mechanism of Pikp-1/Pikp-2 activation, we expressed truncated variants of these proteins, and made mutations in previously identified NLR sequence motifs. We found that any domain truncation, in either Pikp-1 or Pikp-2, prevented cell death in the presence of AVR-PikD, revealing that all domains are required for activity. Further, expression of individual Pikp-1 or Pikp-2 domains did not result in cell death. Mutations in the conserved P-loop and MHD sequence motifs in both Pikp-1 and Pikp-2 prevented cell death activation, demonstrating that these motifs are required for the function of the two partner NLRs. Finally, we showed that Pikp-1 and Pikp-2 associate to form homo- and hetero-complexes in planta in the absence of AVR-PikD; on co-expression the effector binds to Pikp-1 generating a tri-partite complex. Taken together, we provide evidence that Pikp-1 and Pikp-2 form a fine-tuned system that is activated by AVR-PikD via receptor cooperation rather than negative regulation.

Indexed as

Amino Acid MotifsAmino Acid SequenceCell DeathNLR ProteinsOryzaPlant ProteinsProtein BindingProtein DomainsNLR ProteinsPlant Proteins

Identifiers

PMID32931489
PMCPMC7491719
OpenAlexW3087344576

What OpenQuestion holds

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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.