Evidence map›Paper›PMID 26071421›Full record

ArticleThe Plant cell2015

Phytosulfokine Regulates Growth in Arabidopsis through a Response Module at the Plasma Membrane That Includes CYCLIC NUCLEOTIDE-GATED CHANNEL17, H+-ATPase, and BAK1.

Friederike Ladwig, Renate I Dahlke, Nils Stührwohldt, Jens Hartmann, Klaus Harter, Margret Sauter

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.

0numbers the graph read from it
0cells of the map it votes in
114citing papers in PubMed
30.5field-weighted citation impact, top 1% 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

114 citing papers in PubMed, 225 citations in OpenAlex.

  1. Review
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  5. SERK5 genetically compensates for the loss of BAK1 and BKK1 in regulating elf18-triggered immune signaling inProceedings of the National Academy of Sciences of the United States of America · 2025
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  10. Analysis ofInternational journal of molecular sciences · 2025
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54 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 1 country.

Friederike LadwigUniversität Tübingen, ZMBP, Plant Physiology, D-72076 Tübingen, Germany.
Renate I DahlkeEntwicklungsbiologie und Physiologie der Pflanzen, Universität Kiel, D-24118 Kiel, Germany.
Nils StührwohldtEntwicklungsbiologie und Physiologie der Pflanzen, Universität Kiel, D-24118 Kiel, Germany.ORCID http://orcid.org/0000-0003-4166-3786
Jens HartmannEntwicklungsbiologie und Physiologie der Pflanzen, Universität Kiel, D-24118 Kiel, Germany.
Klaus HarterUniversität Tübingen, ZMBP, Plant Physiology, D-72076 Tübingen, Germany.ORCID http://orcid.org/0000-0002-2150-6970
Margret SauterEntwicklungsbiologie und Physiologie der Pflanzen, Universität Kiel, D-24118 Kiel, Germany msauter@bot.uni-kiel.de.ORCID http://orcid.org/0000-0002-7370-643X
Christian-Albrechts-Universität zu Kiel · DEUniversity of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phytosulfokine (PSK) is perceived by the leucine-rich repeat receptor kinase PSKR1 and promotes growth in Arabidopsis thaliana. PSKR1 is coexpressed with the CYCLIC NUCLEOTIDE-GATED CHANNEL gene CNGC17. PSK promotes protoplast expansion in the wild type but not in cngc17. Protoplast expansion is likewise promoted by cGMP in a CNGC17-dependent manner. Furthermore, PSKR1-deficient protoplasts do not expand in response to PSK but are still responsive to cGMP, suggesting that cGMP acts downstream of PSKR1. Mutating the guanylate cyclase center of PSKR1 impairs seedling growth, supporting a role for PSKR1 signaling via cGMP in planta. While PSKR1 does not interact directly with CNGC17, it interacts with the plasma membrane-localized H(+)-ATPases AHA1 and AHA2 and with the BRI-associated receptor kinase 1 (BAK1). CNGC17 likewise interacts with AHA1, AHA2, and BAK1, suggesting that PSKR1, BAK1, CNGC17, and AHA assemble in a functional complex. Roots of deetiolated bak1-3 and bak1-4 seedlings were unresponsive to PSK, and bak1-3 and bak1-4 protoplasts expanded less in response to PSK but were fully responsive to cGMP, indicating that BAK1 acts in the PSK signal pathway upstream of cGMP. We hypothesize that CNGC17 and AHAs form a functional cation-translocating unit that is activated by PSKR1/BAK1 and possibly other BAK1/RLK complexes.

Indexed as

ArabidopsisArabidopsis ProteinsCell MembraneCyclic Nucleotide-Gated Cation ChannelsGene Expression Regulation, PlantPeptide HormonesPlant Growth RegulatorsPlant ProteinsProtein Serine-Threonine KinasesProton-Translocating ATPasesReceptors, Cell SurfaceSeedlingsArabidopsis ProteinsBAK1 protein, ArabidopsisCNGC17 protein, ArabidopsisCyclic Nucleotide-Gated Cation ChannelsPeptide HormonesPlant Growth RegulatorsPlant ProteinsProtein Serine-Threonine KinasesProton-Translocating ATPasesPSK-alpha protein, plantPSKR1 protein, ArabidopsisReceptors, Cell Surface

Identifiers

PMID26071421
PMCPMC4498212
OpenAlexW2128691304

What OpenQuestion holds

Textmetadata
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.