Evidence map›Paper›PMID 35915109›Full record

ArticleNature communications2022

The receptor kinase SRF3 coordinates iron-level and flagellin dependent defense and growth responses in plants.

Matthieu Pierre Platre, Santosh B Satbhai, Lukas Brent, Matias F Gleason, Min Cao, Magali Grison, Marie Glavier, Ling Zhang, Christophe Gaillochet, Christian Goeschl and 9 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. 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
8.0field-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, 41 citations in OpenAlex.

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  6. A century ofPlant signaling & behavior · 2025
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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

19 authors at 5 institutions in 7 countries.

Matthieu Pierre PlatreSalk Institute For Biological Studies, Plant Molecular and Cellular Biology Laboratory, 10010 North Torrey Pines Road, La Jolla, CA, 92037, USA.ORCID http://orcid.org/0000-0002-4934-3050
Santosh B SatbhaiSalk Institute For Biological Studies, Plant Molecular and Cellular Biology Laboratory, 10010 North Torrey Pines Road, La Jolla, CA, 92037, USA.ORCID http://orcid.org/0000-0002-2770-656X
Lukas BrentSalk Institute For Biological Studies, Plant Molecular and Cellular Biology Laboratory, 10010 North Torrey Pines Road, La Jolla, CA, 92037, USA.
Matias F GleasonSalk Institute For Biological Studies, Plant Molecular and Cellular Biology Laboratory, 10010 North Torrey Pines Road, La Jolla, CA, 92037, USA.
Min CaoSalk Institute For Biological Studies, Plant Molecular and Cellular Biology Laboratory, 10010 North Torrey Pines Road, La Jolla, CA, 92037, USA.
Magali GrisonUniversity of Bordeaux, CNRS, Laboratoire de Biogenèse Membranaire, UMR 5200 CNRS, 33140, Villenave d'Ornon, France.ORCID http://orcid.org/0000-0002-3080-3686
Marie GlavierUniversity of Bordeaux, CNRS, Laboratoire de Biogenèse Membranaire, UMR 5200 CNRS, 33140, Villenave d'Ornon, France.ORCID http://orcid.org/0000-0002-7100-7045
Ling ZhangSalk Institute For Biological Studies, Plant Molecular and Cellular Biology Laboratory, 10010 North Torrey Pines Road, La Jolla, CA, 92037, USA.
Christophe GaillochetSalk Institute For Biological Studies, Plant Molecular and Cellular Biology Laboratory, 10010 North Torrey Pines Road, La Jolla, CA, 92037, USA.
Christian GoeschlGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna Biocenter (VBC), Dr. Bohr-Gasse 3, 1030, Vienna, Austria.
Marco GiovannettiGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna Biocenter (VBC), Dr. Bohr-Gasse 3, 1030, Vienna, Austria.ORCID http://orcid.org/0000-0003-4637-9880
Balaji EnuguttiGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna Biocenter (VBC), Dr. Bohr-Gasse 3, 1030, Vienna, Austria.ORCID http://orcid.org/0000-0002-0816-024X
Julie NeveuPlant Science Research Laboratory (LRSV), UMR5546 CNRS/Université Toulouse 3, 24 Chemin De Borde Rouge, 31320, Auzeville-Tolosane, France.
Marcel von RethDepartment of Plant-Microbe Interactions, Max Planck Institute for Plant Breeding Research, Cologne, Germany.
Ruben AlcázarDepartment of Plant-Microbe Interactions, Max Planck Institute for Plant Breeding Research, Cologne, Germany.
Jane E ParkerDepartment of Plant-Microbe Interactions, Max Planck Institute for Plant Breeding Research, Cologne, Germany.ORCID http://orcid.org/0000-0002-4700-6480
Grégory VertPlant Science Research Laboratory (LRSV), UMR5546 CNRS/Université Toulouse 3, 24 Chemin De Borde Rouge, 31320, Auzeville-Tolosane, France.ORCID http://orcid.org/0000-0002-0844-9991
Emmanuelle BayerUniversity of Bordeaux, CNRS, Laboratoire de Biogenèse Membranaire, UMR 5200 CNRS, 33140, Villenave d'Ornon, France.ORCID http://orcid.org/0000-0001-8642-5293
Wolfgang BuschSalk Institute For Biological Studies, Plant Molecular and Cellular Biology Laboratory, 10010 North Torrey Pines Road, La Jolla, CA, 92037, USA. wbusch@salk.edu.ORCID http://orcid.org/0000-0003-2042-7290
Salk Institute for Biological Studies · USCentre National de la Recherche Scientifique · FRGregor Mendel Institute of Molecular Plant Biology · ATMax Planck Institute for Plant Breeding Research · DECluster of Excellence on Plant Sciences · DE

Funding

Molecular Signal Integration for Root Growth ControlR01GM127759 · NIGMS · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI Wolfgang Busch · 2018 to 2026
$3.2M
NIGMS NIH HHS R01 GM127759
6 · The paper itself

Abstract

Iron is critical for host-pathogen interactions. While pathogens seek to scavenge iron to spread, the host aims at decreasing iron availability to reduce pathogen virulence. Thus, iron sensing and homeostasis are of particular importance to prevent host infection and part of nutritional immunity. While the link between iron homeostasis and immunity pathways is well established in plants, how iron levels are sensed and integrated with immune response pathways remains unknown. Here we report a receptor kinase SRF3, with a role in coordinating root growth, iron homeostasis and immunity pathways via regulation of callose synthases. These processes are modulated by iron levels and rely on SRF3 extracellular and kinase domains which tune its accumulation and partitioning at the cell surface. Mimicking bacterial elicitation with the flagellin peptide flg22 phenocopies SRF3 regulation upon low iron levels and subsequent SRF3-dependent responses. We propose that SRF3 is part of nutritional immunity responses involved in sensing external iron levels.

Indexed as

ArabidopsisArabidopsis ProteinsFlagellinIronProtein KinasesArabidopsis ProteinsFlagellinIronProtein Kinases

Identifiers

PMID35915109
PMCPMC9343624
OpenAlexW4289313504

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.