Evidence map›Paper›PMID 23086342›Full record

ArticlePlanta2013

Control of STN7 transcript abundance and transient STN7 dimerisation are involved in the regulation of STN7 activity.

Tobias Wunder, Qiuping Liu, Elena Aseeva, Vera Bonardi, Dario Leister, Mathias Pribil

Abstract read
PubMed Publisher
In one paragraph

Article in Planta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

23 citing papers in PubMed, 52 citations in OpenAlex.

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  7. STN7 is not essential for developmental acclimation of Arabidopsis to light intensity.The Plant journal : for cell and molecular biology · 2023
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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 1 institution in 1 country.

Tobias WunderDepartment Biology I, Ludwig-Maximilians-University Munich (LMU), Plant Molecular Biology (Botany), Großhaderner Strasse 2, Planegg-Martinsried, Germany.
Qiuping Liu
Elena Aseeva
Vera Bonardi
Dario Leister
Mathias Pribil
Ludwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reversible phosphorylation of LHCII, the light-harvesting complex of photosystem II, controls its migration between the two photosystems (state transitions), and serves to adapt the photosynthetic machinery of plants and green algae to short-term changes in ambient light conditions. The thylakoid kinase STN7 is required for LHCII phosphorylation and state transitions in vascular plants. Regulation of STN7 levels occurs at the post-translational level, depends on the thylakoid redox state, and might involve reversible autophosphorylation. Here, we have analysed the effects of different light conditions and chemical inhibitors on the abundance of STN7 transcripts and their products. This analysis was performed in wild-type Arabidopsis thaliana plants, in several photosynthetic mutants, and in lines overexpressing STN7 (oeSTN7) or expressing mutant variants of STN7 carrying single or double cysteine-serine exchanges. It was found that accumulation of the STN7 protein is also controlled at the level of transcript abundance. Under certain conditions, exposure to high light or far-red light treatment, the relative decreases in LHCII phosphorylation can be attributed to decreases in STN7 abundance. Nevertheless, inhibitor experiments showed that redox control of LHCII kinase activity persists in oeSTN7 plants. STN7 dimers were found in oeSTN7 plants and in lines with single cysteine-serine exchanges, indicating that dimerisation involves disulphide bridges. We speculate that transient STN7 dimerisation is required for STN7 activity, and that the altered dimerisation behaviour of oeSTN7 plants might be responsible for the unusually high phosphorylation of LHCII in the dark found in this genotype.

Indexed as

Protein MultimerizationArabidopsisArabidopsis ProteinsCysteineCytochrome b6f ComplexDisulfidesDithiothreitolDiuronEnzyme ActivationLightLight-Harvesting Protein ComplexesOxidation-ReductionPhosphorylationPhotosystem II Protein ComplexProtein Processing, Post-TranslationalProtein Serine-Threonine KinasesArabidopsis ProteinsCysteineCytochrome b6f ComplexDisulfidesDithiothreitolDiuronLight-Harvesting Protein ComplexesPhotosystem II Protein ComplexProtein Serine-Threonine KinasesRNA, MessengerSerineSTN7 protein, Arabidopsis

Identifiers

PMID23086342
OpenAlexW2083703354

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.