Evidence map›Paper›PMID 22090438›Full record

ArticleJournal of experimental botany2012

Phosphorylation of serine residues in the N-terminus modulates the activity of ACA8, a plasma membrane Ca2+-ATPase of Arabidopsis thaliana.

Sonia Giacometti, Claudia Adriana Marrano, Maria Cristina Bonza, Laura Luoni, Margherita Limonta, Maria Ida De Michelis

Open access · bronzeAbstract read
In one paragraph

Article in Journal of experimental botany, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

26 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
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  3. Evolutionarily conserved BON1 regulates the basal cytosolic CaProceedings of the National Academy of Sciences of the United States of America · 2025
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  15. Tonoplast-localized CaProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Mapping proteome-wide targets of protein kinases in plant stress responses.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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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

6 authors at 1 institution in 1 country.

Sonia GiacomettiDipartimento di Biologia L. Gorini, Università degli Studi di Milano, Istituto di Biofisica del CNR, Sezione di Milano, via G. Celoria 26, 20133 Milano, Italy.
Claudia Adriana Marrano
Maria Cristina Bonza
Laura Luoni
Margherita Limonta
Maria Ida De Michelis
Istituto Nazionale di Fisica Nucleare, Sezione di Milano · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ACA8 is a plasma membrane-localized isoform of calmodulin (CaM)-regulated Ca(2+)-ATPase of Arabidopsis thaliana. Several phosphopeptides corresponding to portions of the regulatory N-terminus of ACA8 have been identified in phospho-proteomic studies. To mimic phosphorylation of the ACA8 N-terminus, each of the serines found to be phosphorylated in those studies (Ser19, Ser22, Ser27, Ser29, Ser57, and Ser99) has been mutated to aspartate. Mutants have been expressed in Saccharomyces cerevisiae and characterized: mutants S19D and S57D--and to a lesser extent also mutants S22D and S27D--are deregulated, as shown by their low activation by CaM and by tryptic cleavage of the N-terminus. The His-tagged N-termini of wild-type and mutant ACA8 (6His-(1)M-I(116)) were expressed in Escherichia coli, affinity-purified, and used to analyse the kinetics of CaM binding by surface plasmon resonance. All the analysed mutations affect the kinetics of interaction with CaM to some extent: in most cases, the altered kinetics result in marginal changes in affinity, with the exception of mutants S57D (K(D) ≈ 10-fold higher than wild-type ACA8) and S99D (K(D) about half that of wild-type ACA8). The ACA8 N-terminus is phosphorylated in vitro by two isoforms of A. thaliana calcium-dependent protein kinase (CPK1 and CPK16); phosphorylation of mutant 6His-(1)M-I(116) peptides shows that CPK16 is able to phosphorylate the ACA8 N-terminus at Ser19 and at Ser22. The possible physiological implications of the subtle modulation of ACA8 activity by phosphorylation of its N-terminus are discussed.

Indexed as

ArabidopsisArabidopsis ProteinsCalcium-Transporting ATPasesCalmodulinCell MembranePhosphorylationPlants, Genetically ModifiedSerineAca8 protein, ArabidopsisArabidopsis ProteinsCalcium-Transporting ATPasesCalmodulinSerine

Identifiers

PMID22090438
PMCPMC3276087
OpenAlexW2145991260

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.