Evidence map›Paper›PMID 41719245›Full record

ArticleThe Plant cell2026

Reversible phosphorylation of NPH3/RPT2-like proteins regulates phototropin receptor signaling.

Stuart Sullivan, Pawel Hermanowicz, Takeshi Higa, Thomas Waksman, Eiji Gotoh, Arran Horne, Louise Henderson, Aneta Prochwicz, Masamitsu Wada, Masato Nakai and 3 more

Abstract read
In one paragraph

Article in The Plant cell, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. 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

13 authors.

Stuart SullivanSchool of Molecular Biosciences, College of Medical, Veterinary and Life Sciences, Bower Building, University of Glasgow, Glasgow G12 8QQ, United Kingdom.ORCID 0000-0002-1042-7855
Pawel HermanowiczMalopolska Centre of Biotechnology, Jagiellonian University, Gronostajowa 7A, Kraków 30-387, Poland.ORCID 0000-0002-4708-442X
Takeshi HigaGraduate School of Arts and Sciences, The University of Tokyo, Tokyo 153-8902, Japan.ORCID 0000-0002-3196-2160
Thomas WaksmanSchool of Molecular Biosciences, College of Medical, Veterinary and Life Sciences, Bower Building, University of Glasgow, Glasgow G12 8QQ, United Kingdom.ORCID 0000-0001-5939-8517
Eiji GotohFaculty of Agriculture, Kyushu University, Fukuoka 812-8581, Japan.ORCID 0000-0002-8952-987X
Arran HorneSchool of Molecular Biosciences, College of Medical, Veterinary and Life Sciences, Bower Building, University of Glasgow, Glasgow G12 8QQ, United Kingdom.ORCID 0009-0003-3010-496X
Louise HendersonSchool of Molecular Biosciences, College of Medical, Veterinary and Life Sciences, Bower Building, University of Glasgow, Glasgow G12 8QQ, United Kingdom.ORCID 0009-0003-3827-8796
Aneta ProchwiczMalopolska Centre of Biotechnology, Jagiellonian University, Gronostajowa 7A, Kraków 30-387, Poland.ORCID 0009-0000-9306-7025
Masamitsu WadaDepartment of Biological Sciences, Tokyo Metropolitan University, Tokyo 192-0397, Japan.ORCID 0000-0001-6672-7411
Masato NakaiInstitute for Protein Research, Osaka University, Suita 565-0871, Japan.ORCID 0000-0003-4744-9916
Noriyuki SuetsuguGraduate School of Arts and Sciences, The University of Tokyo, Tokyo 153-8902, Japan.ORCID 0000-0002-3328-3313
Justyna ŁabuzMalopolska Centre of Biotechnology, Jagiellonian University, Gronostajowa 7A, Kraków 30-387, Poland.ORCID 0000-0002-2612-1658
John M ChristieSchool of Molecular Biosciences, College of Medical, Veterinary and Life Sciences, Bower Building, University of Glasgow, Glasgow G12 8QQ, United Kingdom.ORCID 0000-0002-9976-0055

Funding

Collaborative Research Program of the Institute for Protein ResearchCollege of MedicalGatsby Charitable FoundationJapan Society for the Promotion of Science JP15KK0254Japan Society for the Promotion of Science JP17J06717Japan Society for the Promotion of Science JP19H03183Japan Society for the Promotion of Science JP21H05666Leverhulme Trust RPG-2020-338Ohsumi Frontier Science FoundationPolish National Science Centre OPUS21 UMO-2021/41/B/NZ1/02826UK Biotechnology and Biological Sciences Research Council BB/R001499/1UK Biotechnology and Biological Sciences Research Council BB/V00056X/1UK Biotechnology and Biological Sciences Research Council BB/Y010027/1University of GlasgowUniversity of Osaka CR-21-03Veterinary and Life Sciences
6 · The paper itself

Abstract

Phototropin receptor kinases (phot1 and phot2) enhance photosynthesis by coordinating light responses such as phototropism and chloroplast repositioning under low blue light conditions. These processes rely on NON-PHOTOTROPIC HYPOCOTYL 3 (NPH3)/ROOT PHOTOTROPISM 2-like (NRL) proteins. The Arabidopsis (Arabidopsis thaliana) NRL protein NPH3 is phosphorylated by phot1 at S744, a modification that alters its localization and promotes hypocotyl phototropism. Although reversible phosphorylation of S744 is necessary for reassembling an active phot1-NPH3 complex at the plasma membrane, the mechanisms driving NPH3 dephosphorylation remain unclear. Here, we show that clade L TYPE 2C PROTEIN PHOSPHATASES (PP2C19 and PP2C35) regulate S744 phosphorylation and NPH3 function. Mutants lacking PP2C19 exhibit sustained S744 phosphorylation and reduced phototropism, with greater defects observed in pp2c19 pp2c35 double mutants, indicating functional redundancy between these phosphatases. Moreover, clade L pp2c mutants display altered RPT2 phosphorylation and abundance and modulate the phosphorylation status of NRL PROTEIN FOR CHLOROPLAST MOVEMENT 1 (NCH1), suggesting broader regulatory control over phot1-NRL targets. Consistent with this, phototropin-dependent chloroplast accumulation is impaired in both Arabidopsis and Marchantia pp2c19 mutants. These findings identify clade L PP2Cs as key regulators of auxin-dependent (phototropism) and auxin-independent (chloroplast accumulation movement) light responses, which, together with their additional role in regulating hypocotyl gravitropism, are particularly important for seedling emergence and establishment from beneath the soil surface.

Indexed as

ArabidopsisArabidopsis ProteinsGene Expression Regulation, PlantHypocotylMutationPhosphoprotein PhosphatasesPhosphorylationPhototropismSignal TransductionArabidopsis ProteinsNPH3 protein, ArabidopsisPhosphoprotein PhosphatasesRPT2 protein, Arabidopsis

Identifiers

PMID41719245
PMCPMC13017905

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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.