Evidence map›Paper›PMID 25902812›Full record

ArticlePlant physiology2015

Plants Actively Avoid State Transitions upon Changes in Light Intensity: Role of Light-Harvesting Complex II Protein Dephosphorylation in High Light.

Nageswara Rao Mekala, Marjaana Suorsa, Marjaana Rantala, Eva-Mari Aro, Mikko Tikkanen

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

38 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Red-Light Transmittance Changes in VariegatedInternational journal of molecular sciences · 2023
    Article
  8. STN7 is not essential for developmental acclimation of Arabidopsis to light intensity.The Plant journal : for cell and molecular biology · 2023
    Article
  9. Article
  10. Article
  11. Review
  12. STN7 Kinase Is Essential forInternational journal of molecular sciences · 2022
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Composition, phosphorylation and dynamic organization of photosynthetic protein complexes in plant thylakoid membrane.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2020
    Review
  19. Article
  20. Article
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

5 authors at 1 institution in 1 country.

Nageswara Rao MekalaMolecular Plant Biology, Department of Biochemistry, University of Turku, 20014 Turku, Finland.ORCID http://orcid.org/0000-0002-6309-5532
Marjaana SuorsaMolecular Plant Biology, Department of Biochemistry, University of Turku, 20014 Turku, Finland.
Marjaana RantalaMolecular Plant Biology, Department of Biochemistry, University of Turku, 20014 Turku, Finland.
Eva-Mari AroMolecular Plant Biology, Department of Biochemistry, University of Turku, 20014 Turku, Finland evaaro@utu.fi misati@utu.fi.
Mikko TikkanenMolecular Plant Biology, Department of Biochemistry, University of Turku, 20014 Turku, Finland evaaro@utu.fi misati@utu.fi.ORCID http://orcid.org/0000-0002-2753-9597
University of Turku · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photosystem II (PSII) core and light-harvesting complex II (LHCII) proteins in plant chloroplasts undergo reversible phosphorylation upon changes in light intensity (being under control of redox-regulated STN7 and STN8 kinases and TAP38/PPH1 and PSII core phosphatases). Shift of plants from growth light to high light results in an increase of PSII core phosphorylation, whereas LHCII phosphorylation concomitantly decreases. Exactly the opposite takes place when plants are shifted to lower light intensity. Despite distinct changes occurring in thylakoid protein phosphorylation upon light intensity changes, the excitation balance between PSII and photosystem I remains unchanged. This differs drastically from the canonical-state transition model induced by artificial states 1 and 2 lights that concomitantly either dephosphorylate or phosphorylate, respectively, both the PSII core and LHCII phosphoproteins. Analysis of the kinase and phosphatase mutants revealed that TAP38/PPH1 phosphatase is crucial in preventing state transition upon increase in light intensity. Indeed, tap38/pph1 mutant revealed strong concomitant phosphorylation of both the PSII core and LHCII proteins upon transfer to high light, thus resembling the wild type under state 2 light. Coordinated function of thylakoid protein kinases and phosphatases is shown to secure balanced excitation energy for both photosystems by preventing state transitions upon changes in light intensity. Moreover, proton gradient regulation5 (PGR5) is required for proper regulation of thylakoid protein kinases and phosphatases, and the pgr5 mutant mimics phenotypes of tap38/pph1. This shows that there is a close cooperation between the redox- and proton gradient-dependent regulatory mechanisms for proper function of the photosynthetic machinery.

Indexed as

LightAcclimatizationArabidopsisArabidopsis ProteinsHydrogen-Ion ConcentrationImmunoblottingLight-Harvesting Protein ComplexesModels, BiologicalMultiprotein ComplexesMutationPhosphorylationPhotosystem II Protein ComplexPhotosystem I Protein ComplexProtonsThylakoidsArabidopsis ProteinsLight-Harvesting Protein ComplexesMultiprotein ComplexesPhotosystem II Protein ComplexPhotosystem I Protein ComplexProtons

Identifiers

PMID25902812
PMCPMC4453798
OpenAlexW2048357508

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.