Evidence map›Paper›PMID 22547024›Full record

ArticleCell research2012

S-acylation-dependent association of the calcium sensor CBL2 with the vacuolar membrane is essential for proper abscisic acid responses.

Oliver Batistič, Marion Rehers, Amir Akerman, Kathrin Schlücking, Leonie Steinhorst, Shaul Yalovsky, Jörg Kudla

Open access · bronzeAbstract read
In one paragraph

Article in Cell research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
16.9field-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

48 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
  2. Global analysis of membrane protein S-acylation in the model plantbioRxiv : the preprint server for biology · 2025
    Article
  3. Algal origins of core land plant stress response subnetworks.The Plant journal : for cell and molecular biology · 2025
    Article
  4. Article
  5. An endogenous promoterFrontiers in plant science · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. The CBL-CIPK Pathway in Plant Response to Stress Signals.International journal of molecular sciences · 2020
    Review
  13. Article
  14. Dynamic Protein S-Acylation in Plants.International journal of molecular sciences · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Targeted Profiling ofThe Plant cell · 2018
    Article
  19. Article
  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

7 authors at 2 institutions in 2 countries.

Oliver BatističInstitut für Biologie und Biotechnologie der Pflanzen, Universität Münster, Schlossplatz 4, Münster 48149, Germany.
Marion Rehers
Amir Akerman
Kathrin Schlücking
Leonie Steinhorst
Shaul Yalovsky
Jörg Kudla
University of Münster · DETel Aviv University · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calcineurin B-like (CBL) proteins contribute to decoding calcium signals by interacting with CBL-interacting protein kinases (CIPKs). Currently, there is still very little information about the function and specific targeting mechanisms of CBL proteins that are localized at the vacuolar membrane. In this study, we focus on CBL2, an abundant vacuolar membrane-localized calcium sensor of unknown function from Arabidopsis thaliana. We show that vacuolar targeting of CBL2 is specifically brought about by S-acylation of three cysteine residues in its N-terminus and that CBL2 S-acylation and targeting occur by a Brefeldin A-insensitive pathway. Loss of CBL2 function renders plants hypersensitive to the phytohormone abscisic acid (ABA) during seed germination and only fully S-acylated and properly vacuolar-targeted CBL2 proteins can complement this mutant phenotype. These findings define an S-acylation-dependent vacuolar membrane targeting pathway for proteins and uncover a crucial role of vacuolar calcium sensors in ABA responses.

Indexed as

Abscisic AcidArabidopsisArabidopsis ProteinsCalciumCalcium-Binding ProteinsGene Expression Regulation, PlantIntracellular MembranesMicroscopy, FluorescencePlants, Genetically ModifiedProtein BindingVacuolesAbscisic AcidArabidopsis ProteinsAt5g55990 protein, ArabidopsisCalciumCalcium-Binding Proteins

Identifiers

PMID22547024
PMCPMC3391015
OpenAlexW2046945231

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.