Evidence map›Paper›PMID 29921904›Full record

ArticleNature communications2018

A phosphorylation switch turns a positive regulator of phototropism into an inhibitor of the process.

Paolo Schumacher, Emilie Demarsy, Patrice Waridel, Laure Allenbach Petrolati, Martine Trevisan, Christian Fankhauser

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
6.1field-weighted citation impact, top 4% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

  1. Plants (Basel, Switzerland) · 2026
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  8. CIPK23 regulates blue light-dependent stomatal opening in Arabidopsis thaliana.The Plant journal : for cell and molecular biology · 2020
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  9. Article
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  12. The continuing arc toward phototropic enlightenment.Journal of experimental botany · 2020
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  15. Article
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.

Paolo SchumacherCenter for Integrative Genomics, Faculty of Biology and Medicine, University of Lausanne, Genopode Building, 1015, Lausanne, Switzerland.
Emilie DemarsyCenter for Integrative Genomics, Faculty of Biology and Medicine, University of Lausanne, Genopode Building, 1015, Lausanne, Switzerland.ORCID http://orcid.org/0000-0002-0638-0812
Patrice WaridelProtein Analysis Facility, Center for Integrative Genomics, Faculty of Biology and Medicine, University of Lausanne, 1015, Lausanne, Switzerland.ORCID http://orcid.org/0000-0001-7248-5105
Laure Allenbach PetrolatiCenter for Integrative Genomics, Faculty of Biology and Medicine, University of Lausanne, Genopode Building, 1015, Lausanne, Switzerland.ORCID http://orcid.org/0000-0002-9074-5350
Martine TrevisanCenter for Integrative Genomics, Faculty of Biology and Medicine, University of Lausanne, Genopode Building, 1015, Lausanne, Switzerland.ORCID http://orcid.org/0000-0002-6610-6954
Christian FankhauserCenter for Integrative Genomics, Faculty of Biology and Medicine, University of Lausanne, Genopode Building, 1015, Lausanne, Switzerland. christian.fankhauser@unil.ch.ORCID http://orcid.org/0000-0003-4719-5901
University of Lausanne · CHUniversity of Geneva · CH

Funding

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (Swiss National Science Foundation) 3100A-160326Université de Lausanne (University of Lausanne) N/A
6 · The paper itself

Abstract

Phototropins are light-activated protein kinases, which contribute to photosynthesis optimization both through enhancement of photon absorption when light is limiting and avoidance responses in high light. This duality is in part endowed by the presence of phototropins with different photosensitivity (phot1 and phot2). Here we show that phot1, which senses low light to promote positive phototropism (growth towards the light), also limits the response in high light. This response depends in part on phot1-mediated phosphorylation of Phytochrome Kinase Substrate 4 (PKS4). This light-regulated phosphorylation switch changes PKS4 from a phototropism enhancer in low light to a factor limiting the process in high light. In such conditions phot1 and PKS4 phosphorylation prevent phototropic responses to shallow light gradients and limit phototropism in a natural high light environment. Hence, by modifying PKS4 activity in high light the phot1-PKS4 regulon enables appropriate physiological adaptations over a range of light intensities.

Indexed as

LightAdaptation, PhysiologicalArabidopsisArabidopsis ProteinsDose-Response Relationship, RadiationGene Expression Regulation, PlantIntracellular Signaling Peptides and ProteinsPhosphoproteinsPhosphorylationPhototropismPlants, Genetically ModifiedProtein Serine-Threonine KinasesArabidopsis ProteinsIntracellular Signaling Peptides and ProteinsNPH1 protein, ArabidopsisPhosphoproteinsPKS4 protein, ArabidopsisProtein Serine-Threonine Kinases

Identifiers

PMID29921904
PMCPMC6008296
OpenAlexW2808513041

What OpenQuestion holds

Textmetadata
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.