Evidence map›Paper›PMID 26451844›Full record

ArticlePLoS genetics2015

IBR5 Modulates Temperature-Dependent, R Protein CHS3-Mediated Defense Responses in Arabidopsis.

Jingyan Liu, Haibian Yang, Fei Bao, Kevin Ao, Xiaoyan Zhang, Yuelin Zhang, Shuhua Yang

Erratum issuedOpen access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PLoS genetics, 2015. 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 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

11 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Emerging Functions of Protein Tyrosine Phosphatases in Plants.International journal of molecular sciences · 2024
    Review
  4. International journal of molecular sciences · 2022
    Article
  5. HSP90 Contributes toFrontiers in plant science · 2022
    Article
  6. Molecular mapping and characterization of QBp.caas-3BL for black point resistance in wheat (Triticum aestivum L.).TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2021
    Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 2 countries.

Jingyan LiuState Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, National Plant Gene Research Center, China Agricultural University, Beijing, China.
Haibian YangState Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, National Plant Gene Research Center, China Agricultural University, Beijing, China.
Fei BaoState Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, National Plant Gene Research Center, China Agricultural University, Beijing, China.
Kevin AoDepartment of Botany, University of British Columbia, Vancouver, British Columbia, Canada.
Xiaoyan ZhangState Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, National Plant Gene Research Center, China Agricultural University, Beijing, China.
Yuelin ZhangDepartment of Botany, University of British Columbia, Vancouver, British Columbia, Canada.
Shuhua YangDepartment of Botany, University of British Columbia, Vancouver, British Columbia, Canada.
State Key Laboratory of Plant Genomics · CNUniversity of British Columbia · CAChina Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant responses to low temperature are tightly associated with defense responses. We previously characterized the chilling-sensitive mutant chs3-1 resulting from the activation of the Toll and interleukin 1 receptor-nucleotide binding-leucine-rich repeat (TIR-NB-LRR)-type resistance (R) protein harboring a C-terminal LIM (Lin-11, Isl-1 and Mec-3 domains) domain. Here we report the identification of a suppressor of chs3, ibr5-7 (indole-3-butyric acid response 5), which largely suppresses chilling-activated defense responses. IBR5 encodes a putative dual-specificity protein phosphatase. The accumulation of CHS3 protein at chilling temperatures is inhibited by the IBR5 mutation. Moreover, chs3-conferred defense phenotypes were synergistically suppressed by mutations in HSP90 and IBR5. Further analysis showed that IBR5, with holdase activity, physically associates with CHS3, HSP90 and SGT1b (Suppressor of the G2 allele of skp1) to form a complex that protects CHS3. In addition to the positive role of IBR5 in regulating CHS3, IBR5 is also involved in defense responses mediated by R genes, including SNC1 (Suppressor of npr1-1, Constitutive 1), RPS4 (Resistance to P. syringae 4) and RPM1 (Resistance to Pseudomonas syringae pv. maculicola 1). Thus, the results of the present study reveal a role for IBR5 in the regulation of multiple R protein-mediated defense responses.

Indexed as

ArabidopsisArabidopsis ProteinsCell Cycle ProteinsChitin SynthaseCold TemperatureDisease ResistanceDual-Specificity PhosphatasesGene Expression Regulation, PlantHSP90 Heat-Shock ProteinsMutationPlant DiseasesPlant ProteinsArabidopsis ProteinsCell Cycle ProteinsChitin SynthaseCHS3 protein, ArabidopsisDual-Specificity PhosphatasesHsp90-1 protein, ArabidopsisHSP90 Heat-Shock ProteinsIBR5 protein, ArabidopsisPlant ProteinsRPM1 protein, Arabidopsisrps4 protein, plantSGT1b protein, Arabidopsis

Identifiers

PMID26451844
PMCPMC4599859
OpenAlexW2207520376

What OpenQuestion holds

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LicenceCC BY
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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.