Evidence map›Paper›PMID 21768351›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Comparative phosphoproteome profiling reveals a function of the STN8 kinase in fine-tuning of cyclic electron flow (CEF).

Sonja Reiland, Giovanni Finazzi, Anne Endler, Adrian Willig, Katja Baerenfaller, Jonas Grossmann, Bertran Gerrits, Dorothea Rutishauser, Wilhelm Gruissem, Jean-David Rochaix and 1 more

Abstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing 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

75 citing papers in PubMed.

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  18. Regulation of Light Harvesting inPlant physiology · 2020
    Article
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15 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.

Sonja ReilandDepartment of Biology, Eidgenössische Technische Hochschule Zurich, 8092 Zurich, Switzerland.
Giovanni Finazzi
Anne Endler
Adrian Willig
Katja Baerenfaller
Jonas Grossmann
Bertran Gerrits
Dorothea Rutishauser
Wilhelm Gruissem
Jean-David Rochaix
Sacha Baginsky

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Important aspects of photosynthetic electron transport efficiency in chloroplasts are controlled by protein phosphorylation. Two thylakoid-associated kinases, STN7 and STN8, have distinct roles in short- and long-term photosynthetic acclimation to changes in light quality and quantity. Although some substrates of STN7 and STN8 are known, the complexity of this regulatory kinase system implies that currently unknown substrates connect photosynthetic performance with the regulation of metabolic and regulatory functions. We performed an unbiased phosphoproteome-wide screen with Arabidopsis WT and stn8 mutant plants to identify unique STN8 targets. The phosphorylation status of STN7 was not affected in stn8, indicating that kinases other than STN8 phosphorylate STN7 under standard growth conditions. Among several putative STN8 substrates, PGRL1-A is of particular importance because of its possible role in the modulation of cyclic electron transfer. The STN8 phosphorylation site on PGRL1-A is absent in both monocotyledonous plants and algae. In dicots, spectroscopic measurements with Arabidopsis WT, stn7, stn8, and stn7/stn8 double-mutant plants indicate a STN8-mediated slowing down of the transition from cyclic to linear electron flow at the onset of illumination. This finding suggests a possible link between protein phosphorylation by STN8 and fine-tuning of cyclic electron flow during this critical step of photosynthesis, when the carbon assimilation is not commensurate to the electron flow capacity of the chloroplast.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsChromatography, Ion ExchangeChromatography, LiquidElectron TransportLightMembrane ProteinsMolecular Sequence DataMutationPhosphoproteinsPhosphorylationPhotosynthesisPhotosystem II Protein ComplexPhotosystem I Protein ComplexProtein KinasesArabidopsis ProteinsMembrane ProteinsPGRL1 protein, ArabidopsisPhosphoproteinsPhotosystem II Protein ComplexPhotosystem I Protein ComplexProtein KinasesProtein Serine-Threonine KinasesSTN7 protein, ArabidopsisSTN8 protein, Arabidopsis

Identifiers

PMID21768351
PMCPMC3150903

What OpenQuestion holds

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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.