Evidence map›Paper›PMID 25896806›Full record

ArticleNature communications2015

A STIM2 splice variant negatively regulates store-operated calcium entry.

Anna-Maria Miederer, Dalia Alansary, Gertrud Schwär, Po-Hsien Lee, Martin Jung, Volkhard Helms, Barbara A Niemeyer

Abstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
–field-weighted citation impact
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

68 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. STIM2β is a CaThe FEBS journal · 2025
    Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. The Molecular Heterogeneity of Store-Operated CaInternational journal of molecular sciences · 2023
    Review
  13. Review
  14. Review
  15. Review
  16. Review
  17. Identification of a STIM1 Splicing Variant that Promotes Glioblastoma Growth.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Article
  18. Article
  19. Functional communication between IPProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  20. Review

8 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

7 authors.

Anna-Maria MiedererMolecular Biophysics, Center for Integrative Physiology and Molecular Medicine (CIPMM), School of Medicine, Saarland University, Building 48, Homburg 66421, Germany.
Dalia AlansaryMolecular Biophysics, Center for Integrative Physiology and Molecular Medicine (CIPMM), School of Medicine, Saarland University, Building 48, Homburg 66421, Germany.
Gertrud SchwärMolecular Biophysics, Center for Integrative Physiology and Molecular Medicine (CIPMM), School of Medicine, Saarland University, Building 48, Homburg 66421, Germany.
Po-Hsien LeeCenter for Bioinformatics, Saarland University, Campus E2 1, R. 315, PO Box 151150, Saarbrücken 66041, Germany.
Martin JungDepartment of Medical Biochemistry and Molecular Biology, Saarland University, Building 44, Homburg 66421, Germany.
Volkhard HelmsCenter for Bioinformatics, Saarland University, Campus E2 1, R. 315, PO Box 151150, Saarbrücken 66041, Germany.
Barbara A NiemeyerMolecular Biophysics, Center for Integrative Physiology and Molecular Medicine (CIPMM), School of Medicine, Saarland University, Building 48, Homburg 66421, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellular homeostasis relies upon precise regulation of Ca(2+) concentration. Stromal interaction molecule (STIM) proteins regulate store-operated calcium entry (SOCE) by sensing Ca(2+) concentration in the ER and forming oligomers to trigger Ca(2+) entry through plasma membrane-localized Orai1 channels. Here we characterize a STIM2 splice variant, STIM2.1, which retains an additional exon within the region encoding the channel-activating domain. Expression of STIM2.1 is ubiquitous but its abundance relative to the more common STIM2.2 variant is dependent upon cell type and highest in naive T cells. STIM2.1 knockdown increases SOCE in naive CD4(+) T cells, whereas knockdown of STIM2.2 decreases SOCE. Conversely, overexpression of STIM2.1, but not STIM2.2, decreases SOCE, indicating its inhibitory role. STIM2.1 interaction with Orai1 is impaired and prevents Orai1 activation, but STIM2.1 shows increased affinity towards calmodulin. Our results imply STIM2.1 as an additional player tuning Orai1 activation in vivo.

Indexed as

Biological TransportCalciumCalcium ChannelsCalmodulinCell Adhesion MoleculesGene Expression RegulationHEK293 CellsHumansJurkat CellsORAI1 ProteinProtein IsoformsStromal Interaction Molecule 2CalciumCalcium ChannelsCalmodulinCell Adhesion MoleculesORAI1 ProteinORAI1 protein, humanProtein IsoformsSTIM2 protein, humanStromal Interaction Molecule 2

Identifiers

PMID25896806
PMCPMC4411291

What OpenQuestion holds

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Registered trials

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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.