Evidence map›Paper›PMID 35524157›Full record

ArticleNature communications2022

Calcium bursts allow rapid reorganization of EFhD2/Swip-1 cross-linked actin networks in epithelial wound closure.

Franziska Lehne, Thomas Pokrant, Sabnam Parbin, Gabriela Salinas, Jörg Großhans, Katja Rust, Jan Faix, Sven Bogdan

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

23 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Physical models of embryonic epithelial healing.PLoS computational biology · 2026
    Review
  5. Excessive CabioRxiv : the preprint server for biology · 2026
    Article
  6. Stress transmission towards the nucleus of the cell.Frontiers in cell and developmental biology · 2026
    Review
  7. Article
  8. Electrochemical Detection of NO and CaPlasma chemistry and plasma processing · 2026
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Calcium signaling in mitochondrial intermembrane space.Biochemical Society transactions · 2024
    Review
  18. 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

8 authors at 3 institutions in 1 country.

Franziska LehneInstitute of Physiology and Pathophysiology, Department of Molecular Cell Physiology, Philipps-University Marburg, Marburg, Germany.ORCID 0000-0002-6102-2487
Thomas PokrantInstitute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany.
Sabnam ParbinNGS-Integrative Genomics Core Unit, Department of Human Genetics, University Medical Center Göttingen, Göttingen, Germany.
Gabriela SalinasNGS-Integrative Genomics Core Unit, Department of Human Genetics, University Medical Center Göttingen, Göttingen, Germany.
Jörg GroßhansDepartment of Biology, Philipps-University Marburg, Marburg, Germany.
Katja RustInstitute of Physiology and Pathophysiology, Department of Molecular Cell Physiology, Philipps-University Marburg, Marburg, Germany.
Jan FaixInstitute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany.ORCID 0000-0003-1803-9192
Sven BogdanInstitute of Physiology and Pathophysiology, Department of Molecular Cell Physiology, Philipps-University Marburg, Marburg, Germany. sven.bogdan@staff.uni-marburg.de.ORCID 0000-0002-8753-9855
Philipps University of Marburg · DEMedizinische Hochschule Hannover · DEUniversitätsmedizin Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Changes in cell morphology require the dynamic remodeling of the actin cytoskeleton. Calcium fluxes have been suggested as an important signal to rapidly relay information to the actin cytoskeleton, but the underlying mechanisms remain poorly understood. Here, we identify the EF-hand domain containing protein EFhD2/Swip-1 as a conserved lamellipodial protein strongly upregulated in Drosophila macrophages at the onset of metamorphosis when macrophage behavior shifts from quiescent to migratory state. Loss- and gain-of-function analysis confirm a critical function of EFhD2/Swip-1 in lamellipodial cell migration in fly and mouse melanoma cells. Contrary to previous assumptions, TIRF-analyses unambiguously demonstrate that EFhD2/Swip-1 proteins efficiently cross-link actin filaments in a calcium-dependent manner. Using a single-cell wounding model, we show that EFhD2/Swip-1 promotes wound closure in a calcium-dependent manner. Mechanistically, our data suggest that transient calcium bursts reduce EFhD2/Swip-1 cross-linking activity and thereby promote rapid reorganization of existing actin networks to drive epithelial wound closure.

Indexed as

ActinsCalciumCalcium-Binding ProteinsWound HealingAnimalsCell MovementDrosophilaDrosophila ProteinsMiceSignal TransductionActinsCalciumCalcium-Binding ProteinsDrosophila ProteinsEFHD2 protein, mouseSwip-1 protein, Drosophila

Identifiers

PMID35524157
PMCPMC9076686
OpenAlexW4229061110

What OpenQuestion holds

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LicenceCC BY
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.