Evidence map›Paper›PMID 27173885›Full record

ArticleNature communications2016

Evidence that phytochrome functions as a protein kinase in plant light signalling.

Ah-Young Shin, Yun-Jeong Han, Ayoung Baek, Taeho Ahn, Soo Young Kim, Thai Son Nguyen, Minky Son, Keun Woo Lee, Yu Shen, Pill-Soon Song and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
29.5field-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

61 citing papers in PubMed, 121 citations in OpenAlex.

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  8. A circadian clock output functions independently of phyB to sustain daytime PIF3 degradation.Proceedings of the National Academy of Sciences of the United States of America · 2024
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1 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

11 authors at 4 institutions in 2 countries.

Ah-Young ShinDepartment of Biotechnology and Kumho Life Science Laboratory, Chonnam National University, Gwangju 500-757, Korea.
Yun-Jeong HanDepartment of Biotechnology and Kumho Life Science Laboratory, Chonnam National University, Gwangju 500-757, Korea.
Ayoung BaekDivision of Applied Life Science (BK21 Plus Program), Systems and Synthetic Agrobiotech Center (SSAC), Plant Molecular Biology and Biotechnology Research Center (PMBBRC), Research Institute of Natural Science (RINS), Gyeongsang National University, Jinju 660-701, Korea.
Taeho AhnCollege of Veterinary Medicine, Chonnam National University, Gwangju 500-757, Korea.
Soo Young KimDepartment of Biotechnology and Kumho Life Science Laboratory, Chonnam National University, Gwangju 500-757, Korea.
Thai Son NguyenDepartment of Biotechnology and Kumho Life Science Laboratory, Chonnam National University, Gwangju 500-757, Korea.
Minky SonDivision of Applied Life Science (BK21 Plus Program), Systems and Synthetic Agrobiotech Center (SSAC), Plant Molecular Biology and Biotechnology Research Center (PMBBRC), Research Institute of Natural Science (RINS), Gyeongsang National University, Jinju 660-701, Korea.
Keun Woo LeeDivision of Applied Life Science (BK21 Plus Program), Systems and Synthetic Agrobiotech Center (SSAC), Plant Molecular Biology and Biotechnology Research Center (PMBBRC), Research Institute of Natural Science (RINS), Gyeongsang National University, Jinju 660-701, Korea.
Yu ShenBioVision Inc., Milpitas, California 95035, USA.
Pill-Soon SongFaculty of Biotechnology and Subtropical Horticulture Research Institute, Jeju National University, Jeju 690-756, Korea.
Jeong-Il KimDepartment of Biotechnology and Kumho Life Science Laboratory, Chonnam National University, Gwangju 500-757, Korea.
Chonnam National University · KRGyeongsang National University · KRBioInVision (United States) · USJeju National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

It has been suggested that plant phytochromes are autophosphorylating serine/threonine kinases. However, the biochemical properties and functional roles of putative phytochrome kinase activity in plant light signalling are largely unknown. Here, we describe the biochemical and functional characterization of Avena sativa phytochrome A (AsphyA) as a potential protein kinase. We provide evidence that phytochrome-interacting factors (PIFs) are phosphorylated by phytochromes in vitro. Domain mapping of AsphyA shows that the photosensory core region consisting of PAS-GAF-PHY domains in the N-terminal is required for the observed kinase activity. Moreover, we demonstrate that transgenic plants expressing mutant versions of AsphyA, which display reduced activity in in vitro kinase assays, show hyposensitive responses to far-red light. Further analysis reveals that far-red light-induced phosphorylation and degradation of PIF3 are significantly reduced in these transgenic plants. Collectively, these results suggest a positive relationship between phytochrome kinase activity and photoresponses in plants.

Indexed as

AvenaBasic Helix-Loop-Helix ProteinsLight Signal TransductionMutationPhosphorylationPhytochrome APlants, Genetically ModifiedProtein DomainsBasic Helix-Loop-Helix ProteinsPhytochrome A

Identifiers

PMID27173885
PMCPMC4869175
OpenAlexW2363808666

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.