Evidence map›Paper›PMID 26941194›Full record

ArticlePlant physiology2016

Activation of the Stt7/STN7 Kinase through Dynamic Interactions with the Cytochrome b6f Complex.

Alexey Shapiguzov, Xin Chai, Geoffrey Fucile, Paolo Longoni, Lixin Zhang, Jean-David Rochaix

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

42 citing papers in PubMed, 81 citations in OpenAlex.

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  17. ROS production and signalling in chloroplasts: cornerstones and evolving concepts.The Plant journal : for cell and molecular biology · 2022
    Review
  18. Article
  19. STN7 Kinase Is Essential forInternational journal of molecular sciences · 2022
    Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 2 countries.

Alexey ShapiguzovDepartments of Molecular Biology and Plant Biology, University of Geneva, Geneva, Switzerland (A.S.); and Photosynthesis Research Center, Institute of Botany, Chinese Academy of Sciences, Beijing, China (X.C., G.F., P.L., L.Z., J.-D.R.).
Xin ChaiDepartments of Molecular Biology and Plant Biology, University of Geneva, Geneva, Switzerland (A.S.); and Photosynthesis Research Center, Institute of Botany, Chinese Academy of Sciences, Beijing, China (X.C., G.F., P.L., L.Z., J.-D.R.).
Geoffrey FucileDepartments of Molecular Biology and Plant Biology, University of Geneva, Geneva, Switzerland (A.S.); and Photosynthesis Research Center, Institute of Botany, Chinese Academy of Sciences, Beijing, China (X.C., G.F., P.L., L.Z., J.-D.R.).
Paolo LongoniDepartments of Molecular Biology and Plant Biology, University of Geneva, Geneva, Switzerland (A.S.); and Photosynthesis Research Center, Institute of Botany, Chinese Academy of Sciences, Beijing, China (X.C., G.F., P.L., L.Z., J.-D.R.).
Lixin ZhangDepartments of Molecular Biology and Plant Biology, University of Geneva, Geneva, Switzerland (A.S.); and Photosynthesis Research Center, Institute of Botany, Chinese Academy of Sciences, Beijing, China (X.C., G.F., P.L., L.Z., J.-D.R.).
Jean-David RochaixDepartments of Molecular Biology and Plant Biology, University of Geneva, Geneva, Switzerland (A.S.); and Photosynthesis Research Center, Institute of Botany, Chinese Academy of Sciences, Beijing, China (X.C., G.F., P.L., L.Z., J.-D.R.) jean-david.rochaix@unige.ch.ORCID 0000-0001-8483-777X
University of Geneva · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photosynthetic organisms have the ability to adapt to changes in light quality by readjusting the cross sections of the light-harvesting systems of photosystem II (PSII) and photosystem I (PSI). This process, called state transitions, maintains the redox poise of the photosynthetic electron transfer chain and ensures a high photosynthetic yield when light is limiting. It is mediated by the Stt7/STN7 protein kinase, which is activated through the cytochrome b6f complex upon reduction of the plastoquinone pool. Its probable major substrate, the light-harvesting complex of PSII, once phosphorylated, dissociates from PSII and docks to PSI, thereby restoring the balance of absorbed light excitation energy between the two photosystems. Although the kinase is known to be inactivated under high-light intensities, the molecular mechanisms governing its regulation remain unknown. In this study we monitored the redox state of a conserved and essential Cys pair of the Stt7/STN7 kinase and show that it forms a disulfide bridge. We could not detect any change in the redox state of these Cys during state transitions and high-light treatment. It is only after prolonged anaerobiosis that this disulfide bridge is reduced. It is likely to be mainly intramolecular, although kinase activation may involve a transient covalently linked kinase dimer with two intermolecular disulfide bonds. Using the yeast two-hybrid system, we have mapped one interaction site of the kinase on the Rieske protein of the cytochrome b6f complex.

Indexed as

ArabidopsisArabidopsis ProteinsChlamydomonasChlorophyllCytochrome b6f ComplexLightLight-Harvesting Protein ComplexesMutagenesis, Site-DirectedOxidation-ReductionPhosphorylationPhotosynthesisPhotosystem II Protein ComplexPhotosystem I Protein ComplexPlant ProteinsPlastoquinoneProtein KinasesArabidopsis ProteinsChlorophyllCytochrome b6f ComplexLight-Harvesting Protein ComplexesPhotosystem II Protein ComplexPhotosystem I Protein ComplexPlant ProteinsPlastoquinoneProtein Kinases

Identifiers

PMID26941194
PMCPMC4854690
OpenAlexW2288799968

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.