Evidence map›Paper›PMID 18228034›Full record

ReviewPflugers Archiv : European journal of physiology2009

The plant plasma membrane proton pump ATPase: a highly regulated P-type ATPase with multiple physiological roles.

Geoffrey Duby, Marc Boutry

Abstract readReview
PubMed Publisher
In one paragraph

Review in Pflugers Archiv : European journal of physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
5.1field-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

84 citing papers in PubMed, 213 citations in OpenAlex.

  1. Article
  2. bra-miR9569 Targets thePlants (Basel, Switzerland) · 2025
    Article
  3. Comparative translational reprogramming ofPhysiology and molecular biology of plants : an international journal of functional plant biology · 2025
    Article
  4. Article
  5. Article
  6. Identification and Analysis of the Plasma Membrane HPlants (Basel, Switzerland) · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Structural and Functional Diversity of Two ATP-Driven Plant Proton Pumps.International journal of molecular sciences · 2023
    Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Plasma membrane HiScience · 2022
    Article
  17. Article
  18. Article
  19. Article
  20. Plasma Membrane HInternational journal of molecular sciences · 2021
    Article

24 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Geoffrey DubyUnité de Biochimie Physiologique, Institut des Sciences de la Vie, Université Catholique de Louvain, 1348 Louvain-La-Neuve, Belgium.
Marc Boutry
UCLouvain · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Around 40 P-type ATPases have been identified in Arabidopsis and rice, for which the genomes are known. None seems to exchange sodium and potassium, as does the animal Na(+)/K(+)-ATPase. Instead, plants, together with fungi, possess a proton pumping ATPase (H(+)-ATPase), which couples ATP hydrolysis to proton transport out of the cell, and so establishes an electrochemical gradient across the plasma membrane, which is dissipated by secondary transporters using protons in symport or antiport, as sodium is used in animal cells. Additional functions, such as stomata opening, cell growth, and intracellular pH homeostasis, have been proposed. Crystallographic data and homology modeling suggest that the H(+)-ATPase has a broadly similar structure to the other P-type ATPases but has an extended C-terminal region, which is involved in enzyme regulation. Phosphorylation of the penultimate residue, a Thr, and the subsequent binding of regulatory 14-3-3 proteins result in the formation of a dodecamer (six H(+)-ATPase and six 14-3-3 molecules) and enzyme activation. This type of regulation is unique to the P-type ATPase family. However, the recent identification of additional phosphorylated residues suggests further regulatory features.

Indexed as

14-3-3 ProteinsAdenosine TriphosphatasesAmino Acid SequenceCell MembraneIsoenzymesModels, MolecularMolecular Sequence DataPlant ProteinsProtein Structure, QuaternaryProton PumpsSequence Alignment14-3-3 ProteinsAdenosine TriphosphatasesIsoenzymesPlant ProteinsProton Pumps

Identifiers

PMID18228034
OpenAlexW2011164920

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.