Evidence map›Paper›PMID 26494731›Full record

ArticleJournal of experimental botany2016

Stability of small ubiquitin-like modifier (SUMO) proteases OVERLY TOLERANT TO SALT1 and -2 modulates salicylic acid signalling and SUMO1/2 conjugation in Arabidopsis thaliana.

Mark Bailey, Anjil Srivastava, Lucio Conti, Stuart Nelis, Cunjin Zhang, Hannah Florance, Andrew Love, Joel Milner, Richard Napier, Murray Grant and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of experimental botany, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
10.3field-weighted citation impact, top 2% 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

28 citing papers in PubMed, 61 citations in OpenAlex.

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  12. SUMO enables substrate selectivity by mitogen-activated protein kinases to regulate immunity in plants.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Review
  14. Global SUMOylome Adjustments in Basal Defenses ofFrontiers in cell and developmental biology · 2021
    Article
  15. Review
  16. A role for S-nitrosylation of the SUMO-conjugating enzyme SCE1 in plant immunity.Proceedings of the National Academy of Sciences of the United States of America · 2019
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  17. 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

11 authors at 7 institutions in 2 countries.

Mark BaileyBiological & Biomedical Sciences, Durham University, Durham DH1 3LE, UK Present address: Plant proteolysis and signalling laboratory, School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.
Anjil SrivastavaBiological & Biomedical Sciences, Durham University, Durham DH1 3LE, UK.
Lucio ContiBiological & Biomedical Sciences, Durham University, Durham DH1 3LE, UK Department of BioSciences, Università degli Studi di Milano, Via Celoria 26, 20133 Milano, Italy.
Stuart NelisBiological & Biomedical Sciences, Durham University, Durham DH1 3LE, UK.
Cunjin ZhangBiological & Biomedical Sciences, Durham University, Durham DH1 3LE, UK.
Hannah FloranceGeoffrey Pope Building, Biosciences, College of Life and Environmental Sciences, University of Exeter, Stocker Road, Exeter EX4 4QD, UK.
Andrew LoveCell and Molecular Sciences, The James Hutton Institute, Dundee DD2 5DA, UK.
Joel MilnerPlant Science Group, School of Life Sciences, College of Medical Veterinary & Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK.
Richard NapierSchool of Life Sciences, University of Warwick, Gibbet Hill Road, Coventry CV4 7ES, UK.
Murray GrantGeoffrey Pope Building, Biosciences, College of Life and Environmental Sciences, University of Exeter, Stocker Road, Exeter EX4 4QD, UK.
Ari SadanandomBiological & Biomedical Sciences, Durham University, Durham DH1 3LE, UK ari.sadanandom@durham.ac.uk.
Durham University · GBUniversity of Exeter · GBJames Hutton Institute · GBUniversity of Birmingham · GBUniversity of Glasgow · GBUniversity of Milan · ITUniversity of Warwick · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D007046/1Biotechnology and Biological Sciences Research Council BB/D017319Biotechnology and Biological Sciences Research Council BB/D017319/1Biotechnology and Biological Sciences Research Council BB/F005903/1
6 · The paper itself

Abstract

Small ubiquitin-like modifier proteases 1 and 2 (SUMO1/2) have been linked to the regulation of salicylic acid (SA)-mediated defence signalling in Arabidopsis thaliana. In order to define the role of the SUMO proteases OVERLY TOLERANT TO SALT1 and -2 (OTS1/2) in defence and to provide insight into SUMO1/2-mediated regulation of SA signalling, we examined the status of SA-mediated defences in ots1/2 mutants. The ots1 ots2 double mutant displayed enhanced resistance to virulent Pseudomonas syringae and higher levels of SA compared with wild-type (WT) plants. Furthermore, ots1 ots2 mutants exhibited upregulated expression of the SA biosynthesis gene ICS1 in addition to enhanced SA-responsive ICS1 expression beyond that of WT. SA stimulated OTS1/2 degradation and promoted accumulation of SUMO1/2 conjugates. These results indicate that OTS1 and -2 act in a feedback loop in SA signalling and that de novo OTS1/2 synthesis works antagonistically to SA-promoted degradation, adjusting the abundance of OTS1/2 to moderate SA signalling. Accumulation of SUMO1/2 conjugates coincides with SA-promoted OTS degradation and may play a positive role in SA-mediated signalling in addition to its repressive roles reported elsewhere.

Indexed as

Gene Expression Regulation, PlantArabidopsisArabidopsis ProteinsCysteine EndopeptidasesPlant DiseasesPlant ImmunityPseudomonas syringaeSalicylic AcidSignal TransductionArabidopsis ProteinsCysteine EndopeptidasesOTS1 protein, ArabidopsisOTS2 protein, ArabidopsisSalicylic AcidSUM1 protein, ArabidopsisSUM2 protein, ArabidopsisArabidopsis thalianadefencepathogensalicylic acid (SA)small ubiquitin-like modifier (SUMO)SUMO proteaseSUMOylation.

Identifiers

PMID26494731
PMCPMC4682439
OpenAlexW2173615261

What OpenQuestion holds

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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.