Evidence map›Paper›PMID 10823962›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

A calcium-dependent protein kinase can inhibit a calmodulin-stimulated Ca2+ pump (ACA2) located in the endoplasmic reticulum of Arabidopsis.

I Hwang, H Sze, J F Harper

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
22.6field-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

64 citing papers in PubMed, 175 citations in OpenAlex.

  1. Article
  2. Article
  3. Evolutionarily conserved BON1 regulates the basal cytosolic CaProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Structure, Function, and Applications of Soybean Calcium Transporters.International journal of molecular sciences · 2022
    Review
  9. Article
  10. Review
  11. Article
  12. Guard cell endomembrane CaNature plants · 2021
    Article
  13. Article
  14. Review
  15. Comparative Transcriptome Analysis of TwoInternational journal of molecular sciences · 2020
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

4 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.

I HwangDepartment of Cell Biology and Molecular Genetics, and Maryland Agricultural Experiment Station, University of Maryland, College Park, MD 20742, USA.
H Sze
J F Harper
University of Maryland, College Park · USScripps Research Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The magnitude and duration of a cytosolic Ca(2+) release can potentially be altered by changing the rate of Ca(2+) efflux. In plant cells, Ca(2+) efflux from the cytoplasm is mediated by H(+)/Ca(2+)-antiporters and two types of Ca(2+)-ATPases. ACA2 was recently identified as a calmodulin-regulated Ca(2+)-pump located in the endoplasmic reticulum. Here, we show that phosphorylation of its N-terminal regulatory domain by a Ca(2+)-dependent protein kinase (CDPK isoform CPK1), inhibits both basal activity ( approximately 10%) and calmodulin stimulation ( approximately 75%), as shown by Ca(2+)-transport assays with recombinant enzyme expressed in yeast. A CDPK phosphorylation site was mapped to Ser(45) near a calmodulin binding site, using a fusion protein containing the N-terminal domain as an in vitro substrate for a recombinant CPK1. In a full-length enzyme, an Ala substitution for Ser(45) (S45/A) completely blocked the observed CDPK inhibition of both basal and calmodulin-stimulated activities. An Asp substitution (S45/D) mimicked phosphoinhibition, indicating that a negative charge at this position is sufficient to account for phosphoinhibition. Interestingly, prior binding of calmodulin blocked phosphorylation. This suggests that, once ACA2 binds calmodulin, its activation state becomes resistant to phosphoinhibition. These results support the hypothesis that ACA2 activity is regulated as the balance between the initial kinetics of calmodulin stimulation and CDPK inhibition, providing an example in plants for a potential point of crosstalk between two different Ca(2+)-signaling pathways.

Indexed as

Calcium SignalingAmino Acid SequenceAmino Acid SubstitutionArabidopsisCalciumCalcium-Calmodulin-Dependent Protein KinasesCalcium-Transporting ATPasesCalmodulinEndoplasmic ReticulumIon TransportMolecular Sequence DataMutagenesis, Site-DirectedPhosphorylationPhosphoserinePlant ProteinsProtein KinasesCalciumCalcium-Calmodulin-Dependent Protein KinasesCalcium-Transporting ATPasesCalmodulinPhosphoserinePlant ProteinsProtein KinasesRecombinant Fusion ProteinsNASA Discipline Plant BiologyNASA Program Fundamental Space BiologyNon-NASA Center

Identifiers

PMID10823962
PMCPMC18586
OpenAlexW2017672977

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.