Evidence map›Paper›PMID 23378619›Full record

ArticleThe Plant cell2013

Phosphorylation of phytochrome B inhibits light-induced signaling via accelerated dark reversion in Arabidopsis.

Mátyás Medzihradszky, János Bindics, Éva Ádám, András Viczián, Éva Klement, Séverine Lorrain, Péter Gyula, Zsuzsanna Mérai, Christian Fankhauser, Katalin F Medzihradszky and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
14.8field-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

69 citing papers in PubMed, 124 citations in OpenAlex.

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  13. International journal of molecular sciences · 2023
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9 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 5 institutions in 4 countries.

Mátyás MedzihradszkyFaculty of Biology, University of Freiburg, D-79104, Freiburg Germany.
János Bindics
Éva Ádám
András Viczián
Éva Klement
Séverine Lorrain
Péter Gyula
Zsuzsanna Mérai
Christian Fankhauser
Katalin F Medzihradszky
Tim Kunkel
Eberhard Schäfer
Ferenc Nagy
HUN-REN Szegedi Biológiai Kutatóközpont · HUUniversity of Freiburg · DEInstitute of Plant Biology · HUUniversity of Lausanne · CHUniversity of Edinburgh · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The photoreceptor phytochrome B (phyB) interconverts between the biologically active Pfr (λmax = 730 nm) and inactive Pr (λmax = 660 nm) forms in a red/far-red-dependent fashion and regulates, as molecular switch, many aspects of light-dependent development in Arabidopsis thaliana. phyB signaling is launched by the biologically active Pfr conformer and mediated by specific protein-protein interactions between phyB Pfr and its downstream regulatory partners, whereas conversion of Pfr to Pr terminates signaling. Here, we provide evidence that phyB is phosphorylated in planta at Ser-86 located in the N-terminal domain of the photoreceptor. Analysis of phyB-9 transgenic plants expressing phospho-mimic and nonphosphorylatable phyB-yellow fluorescent protein (YFP) fusions demonstrated that phosphorylation of Ser-86 negatively regulates all physiological responses tested. The Ser86Asp and Ser86Ala substitutions do not affect stability, photoconversion, and spectral properties of the photoreceptor, but light-independent relaxation of the phyB(Ser86Asp) Pfr into Pr, also termed dark reversion, is strongly enhanced both in vivo and in vitro. Faster dark reversion attenuates red light-induced nuclear import and interaction of phyB(Ser86Asp)-YFP Pfr with the negative regulator PHYTOCHROME INTERACTING FACTOR3 compared with phyB-green fluorescent protein. These data suggest that accelerated inactivation of the photoreceptor phyB via phosphorylation of Ser-86 represents a new paradigm for modulating phytochrome-controlled signaling.

Indexed as

Signal TransductionArabidopsisArabidopsis ProteinsBacterial ProteinsBasic Helix-Loop-Helix ProteinsDarknessLightLuminescent ProteinsPhosphorylationPhytochrome BPlants, Genetically ModifiedProtein StabilityProtein Structure, TertiarySeedlingsSerineSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationArabidopsis ProteinsBacterial ProteinsBasic Helix-Loop-Helix ProteinsLuminescent ProteinsPHYB protein, ArabidopsisPhytochrome BPIF3 protein, ArabidopsisSerineyellow fluorescent protein, Bacteria

Identifiers

PMID23378619
PMCPMC3608776
OpenAlexW2117193029

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.