Evidence map›Paper›PMID 14605223›Full record

ArticlePlant physiology2003

Blue-light- and phosphorylation-dependent binding of a 14-3-3 protein to phototropins in stomatal guard cells of broad bean.

Toshinori Kinoshita, Takashi Emi, Misumi Tominaga, Koji Sakamoto, Ayako Shigenaga, Michio Doi, Ken-ichiro Shimazaki

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
12.1field-weighted citation impact, top 2% 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

58 citing papers in PubMed, 150 citations in OpenAlex.

  1. Article
  2. Review
  3. Expression analysis of genes enriched in the pulvinus ofPlant biotechnology (Tokyo, Japan) · 2025
    Article
  4. Phosphorylation of plasma membrane HNature communications · 2024
    Article
  5. Light signaling as cellular integrator of multiple environmental cues in plants.Physiology and molecular biology of plants : an international journal of functional plant biology · 2023
    Review
  6. Article
  7. Review
  8. Article
  9. Stomatal Responses to Light, COFrontiers in plant science · 2021
    Article
  10. Review
  11. Article
  12. Ion Homeostasis and Metabolome Analysis ofFrontiers in plant science · 2021
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Blue light and CONature communications · 2017
    Article
  20. Review
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

7 authors at 2 institutions in 1 country.

Toshinori KinoshitaDepartment of Biology, Faculty of Science, Kyushu University, Ropponmatsu, Fukuoka, Japan 810-8560.
Takashi Emi
Misumi Tominaga
Koji Sakamoto
Ayako Shigenaga
Michio Doi
Ken-ichiro Shimazaki
Kyushu University · JPKomatsu University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phototropins are blue-light (BL) receptor serine (Ser)/threonine kinases, and contain two light, oxygen, and voltage (LOV) domains, and are members of the PAS domain superfamily. They mediate phototropism, chloroplast movement, leaf expansion, and stomatal opening of higher plants in response to BL. In stomatal guard cells, genetic analysis has revealed that phototropins mediate activation of the plasma membrane H+-ATPase by phosphorylation and drive stomatal opening. However, biochemical evidence for the involvement of phototropins in the BL response of stomata is lacking. Using guard cell protoplasts, we showed that broad bean (Vicia faba) phototropins (Vfphots) were phosphorylated by BL, and that this phosphorylation of Vfphots reached to the maximum level earlier than that of the H+-ATPase. Phosphorylation of both Vfphots and H+-ATPase showed similar sensitivity to BL and were similarly suppressed by protein kinase and flavoprotein inhibitors. We found that a 14-3-3 protein was bound to Vfphots upon phosphorylation, and this binding occurred earlier than the H+-ATPase phosphorylation. Vfphots (Vfphot1a and Vfphot1b) were expressed in Escherichia coli, and phosphorylation sites were determined to be Ser-358 for Vfphot1a and Ser-344 for Vfphot1b, which are localized between LOV1 and LOV2. We conclude that Vfphots act as BL receptors in guard cells and that phosphorylation of a Ser residue between LOV1 and LOV2 and subsequent 14-3-3 protein binding are likely to be key steps of BL response in stomata. The binding of a 14-3-3 protein to Vfphot was found in etiolated seedlings and leaves in response to BL, suggesting that this event was common to phototropin-mediated responses.

Indexed as

14-3-3 ProteinsBase SequenceCell MembraneCloning, MolecularDNA PrimersPhosphorylationPhototropismPlant LeavesPlant ProteinsProton-Translocating ATPasesTyrosine 3-MonooxygenaseVicia faba14-3-3 ProteinsDNA PrimersPlant ProteinsProton-Translocating ATPasesTyrosine 3-Monooxygenase

Identifiers

PMID14605223
PMCPMC300702
OpenAlexW2148376740

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.