Evidence map›Paper›PMID 22174420›Full record

ArticleThe Journal of biological chemistry2012

Phosphosite mapping of P-type plasma membrane H+-ATPase in homologous and heterologous environments.

Elena L Rudashevskaya, Juanying Ye, Ole N Jensen, Anja T Fuglsang, Michael G Palmgren

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

39 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Unveiling FERONIA receptor kinase-mediated cellular mechanisms with a small-molecule inhibitor.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Molecular tipping points in plant cell surface HQuantitative plant biology · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Protein Phosphorylation Response to Abiotic Stress in Plants.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. The CaThe Plant cell · 2019
    Article
  16. Article
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  19. Review
  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.

Elena L RudashevskayaCentre for Membrane Pumps in Cells and Disease-PUMPkin, Department of Plant Biology and Biotechnology, University of Copenhagen, DK-1871 Frederiksberg C, Denmark. palmgren@life.ku.dk
Juanying Ye
Ole N Jensen
Anja T Fuglsang
Michael G Palmgren
University of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphorylation is an important posttranslational modification of proteins in living cells and primarily serves regulatory purposes. Several methods were employed for isolating phosphopeptides from proteolytically digested plasma membranes of Arabidopsis thaliana. After a mass spectrometric analysis of the resulting peptides we could identify 10 different phosphorylation sites in plasma membrane H(+)-ATPases AHA1, AHA2, AHA3, and AHA4/11, five of which have not been reported before, bringing the total number of phosphosites up to 11, which is substantially higher than reported so far for any other P-type ATPase. Phosphosites were almost exclusively (9 of 10) in the terminal regulatory domains of the pumps. The AHA2 isoform was subsequently expressed in the yeast Saccharomyces cerevisiae. The plant protein was phosphorylated at multiple sites in yeast, and surprisingly, seven of nine of the phosphosites identified in AHA2 were identical in the plant and fungal systems even though none of the target sequences in AHA2 show homology to proteins of the fungal host. These findings suggest an unexpected accessibility of the terminal regulatory domain of plasma membrane H(+)-ATPase to protein kinase action.

Indexed as

ArabidopsisArabidopsis ProteinsCell MembranePhosphorylationProtein Structure, TertiaryProton-Translocating ATPasesRecombinant ProteinsSaccharomyces cerevisiaeSequence Homology, Amino AcidArabidopsis ProteinsProton-Translocating ATPasesRecombinant Proteins

Identifiers

PMID22174420
PMCPMC3281613
OpenAlexW2053344734

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.