Evidence map›Paper›PMID 25997445›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Calcium sensor kinase activates potassium uptake systems in gland cells of Venus flytraps.

Sönke Scherzer, Jennifer Böhm, Elzbieta Krol, Lana Shabala, Ines Kreuzer, Christina Larisch, Felix Bemm, Khaled A S Al-Rasheid, Sergey Shabala, Heinz Rennenberg and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
18.1field-weighted citation impact, top 1% 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

44 citing papers in PubMed, 121 citations in OpenAlex.

  1. Article
  2. Article
  3. Arabidopsis HAK5 under low KNature communications · 2024
    Article
  4. Article
  5. Resveratrol enhances the tolerance ofFrontiers in plant science · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. STOP1 RegulatesInternational journal of molecular sciences · 2021
    Article
  13. An endoplasmic reticulum-localized cytochromeProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Review
  15. Regulation of Cytosolic pH: The Contributions of Plant Plasma Membrane HInternational journal of molecular sciences · 2021
    Review
  16. Review
  17. Article
  18. 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

12 authors at 6 institutions in 3 countries.

Sönke ScherzerInstitute for Molecular Plant Physiology and Biophysics, University of Wuerzburg, D-97082 Würzburg, Germany;
Jennifer BöhmInstitute for Molecular Plant Physiology and Biophysics, University of Wuerzburg, D-97082 Würzburg, Germany;
Elzbieta KrolInstitute for Molecular Plant Physiology and Biophysics, University of Wuerzburg, D-97082 Würzburg, Germany;
Lana ShabalaSchool of Land and Food, University of Tasmania, Hobart TAS 7001, Australia;
Ines KreuzerInstitute for Molecular Plant Physiology and Biophysics, University of Wuerzburg, D-97082 Würzburg, Germany;
Christina LarischInstitute for Molecular Plant Physiology and Biophysics, University of Wuerzburg, D-97082 Würzburg, Germany;
Felix BemmDepartment of Molecular Biology, Max Planck Institute for Developmental Biology, 72076 Tübingen, Germany;
Khaled A S Al-RasheidZoology Department, College of Science, King Saud University, Riyadh 11451, Saudi Arabia;
Sergey ShabalaSchool of Land and Food, University of Tasmania, Hobart TAS 7001, Australia;
Heinz RennenbergInstitute of Forest Sciences, University of Freiburg, 79085 Freiburg, Germany;
Erwin NeherDepartment for Membrane Biophysics, Max Planck Institute for Biophysical Chemistry, D-37077 Goettingen, Germany eneher@gwdg.de hedrich@botanik.uni-wuerzburg.de.
Rainer HedrichInstitute for Molecular Plant Physiology and Biophysics, University of Wuerzburg, D-97082 Würzburg, Germany; eneher@gwdg.de hedrich@botanik.uni-wuerzburg.de.
University of Würzburg · DEUniversity of Tasmania · AUKing Saud University · SAMax Planck Institute for Biophysical Chemistry · DEMax Planck Institute for Developmental Biology · DEUniversity of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Darwin plant Dionaea muscipula is able to grow on mineral-poor soil, because it gains essential nutrients from captured animal prey. Given that no nutrients remain in the trap when it opens after the consumption of an animal meal, we here asked the question of how Dionaea sequesters prey-derived potassium. We show that prey capture triggers expression of a K(+) uptake system in the Venus flytrap. In search of K(+) transporters endowed with adequate properties for this role, we screened a Dionaea expressed sequence tag (EST) database and identified DmKT1 and DmHAK5 as candidates. On insect and touch hormone stimulation, the number of transcripts of these transporters increased in flytraps. After cRNA injection of K(+)-transporter genes into Xenopus oocytes, however, both putative K(+) transporters remained silent. Assuming that calcium sensor kinases are regulating Arabidopsis K(+) transporter 1 (AKT1), we coexpressed the putative K(+) transporters with a large set of kinases and identified the CBL9-CIPK23 pair as the major activating complex for both transporters in Dionaea K(+) uptake. DmKT1 was found to be a K(+)-selective channel of voltage-dependent high capacity and low affinity, whereas DmHAK5 was identified as the first, to our knowledge, proton-driven, high-affinity potassium transporter with weak selectivity. When the Venus flytrap is processing its prey, the gland cell membrane potential is maintained around -120 mV, and the apoplast is acidified to pH 3. These conditions in the green stomach formed by the closed flytrap allow DmKT1 and DmHAK5 to acquire prey-derived K(+), reducing its concentration from millimolar levels down to trace levels.

Indexed as

AnimalsCalciumDroseraceaeExpressed Sequence TagsGenes, PlantHydrogen-Ion ConcentrationIon TransportPotassiumProtein KinasesSignal TransductionXenopusCalciumPotassiumProtein KinasesAKTCIPKDionaea muscipulaHAK5transporter

Identifiers

PMID25997445
PMCPMC4466697
OpenAlexW2145416677

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.