Evidence map›Paper›PMID 26476298›Full record

ReviewCurrent opinion in plant biology2015

Regulation of the plasma membrane proton pump (H(+)-ATPase) by phosphorylation.

Miyoshi Haruta, William M Gray, Michael R Sussman

Open access · bronzeAbstract readReview
In one paragraph

Review in Current opinion in plant biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
17.6field-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

90 citing papers in PubMed, 199 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. bra-miR9569 Targets thePlants (Basel, Switzerland) · 2025
    Article
  6. Article
  7. Silicon-Mediated Mitigation of Salt Stress in Maize Plants.Plant-environment interactions (Hoboken, N.J.) · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Molecular tipping points in plant cell surface HQuantitative plant biology · 2025
    Review
  13. Article
  14. Article
  15. Review
  16. Structure and growth of plant cell walls.Nature reviews. Molecular cell biology · 2024
    Review
  17. Article
  18. Article
  19. Phosphorylation of plasma membrane HNature communications · 2024
    Article
  20. Article

30 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

3 authors at 2 institutions in 1 country.

Miyoshi HarutaBiotechnology Center and Department of Biochemistry, University of Wisconsin-Madison, United States.
William M GrayDepartment of Plant Biology, University of Minnesota, United States.
Michael R SussmanBiotechnology Center and Department of Biochemistry, University of Wisconsin-Madison, United States. Electronic address: msussman@wisc.edu.
University of Minnesota · USUniversity of Wisconsin–Madison · US

Funding

Molecular mechanisms of auxin response in ArabidopsisR01GM067203 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI GRAY, WILLIAM M · 2003 to 2020
$3.5M
NIGMS NIH HHS GM067203NIGMS NIH HHS R01 GM067203
6 · The paper itself

Abstract

In plants and fungi, energetics at the plasma membrane is provided by a large protonmotive force (PMF) generated by the family of P-type ATPases specialized for proton transport (commonly called PM H(+)-ATPases or, in Arabidopsis, AHAs for Arabidopsis H(+)-ATPases). Studies have demonstrated that this 100-kDa protein is essential for plant growth and development. Posttranslational modifications of the H(+)-ATPase play crucial roles in its regulation. Phosphorylation of several Thr and Ser residues within the carboxy terminal regulatory domain composed of ∼100 amino acids change in response to environmental stimuli, endogenous hormones, and nutrient conditions. Recently developed mass spectrometric technologies provide a means to carefully quantify these changes in H(+)-ATPase phosphorylation at the different sites. These chemical modifications can then be genetically tested in planta by complementing the loss-of-function aha mutants with phosphomimetic mutations. Interestingly, recent data suggest that phosphatase-mediated changes in PM H(+)-ATPase phosphorylation are important in mediating auxin-regulated growth. Thus, as with another hormone (abscisic acid), dephosphorylation by phosphatases, rather than kinase mediated phosphorylation, may be an important focal point for regulation during plant signal transduction. Although interactions with other proteins have also been implicated in ATPase regulation, the very hydrophobic nature and high concentration of this polytopic protein presents special challenges in evaluating the biological significance of these interactions. Only by combining biochemical and genetic experiments can we attempt to meet these challenges to understand the essential molecular details by which this protein functions in planta.

Indexed as

ArabidopsisArabidopsis ProteinsCell MembranePhosphorylationProton-Translocating ATPasesSignal TransductionArabidopsis ProteinsProton-Translocating ATPases

Identifiers

PMID26476298
PMCPMC4679459
OpenAlexW1877310556

What OpenQuestion holds

Textmetadata
LicenceTDM
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.