Evidence map›Paper›PMID 31940262›Full record

ArticleMolecular biology of the cell2020

Formins specify membrane patterns generated by propagating actin waves.

Mary Ecke, Jana Prassler, Patrick Tanribil, Annette Müller-Taubenberger, Sarah Körber, Jan Faix, Günther Gerisch

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Review
  2. Review
  3. Signaling and actin waves at a glance.Journal of cell science · 2025
    Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Competition and Synergy of Arp2/3 and Formins in Nucleating Actin Waves.bioRxiv : the preprint server for biology · 2023
    Article
  10. Article
  11. Article
  12. Convergence of Ras- and Rac-regulated formin pathways is pivotal for phagosome formation and particle uptake inProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Article
  14. Article
  15. Review
  16. Three-dimensional organization of the cytoskeleton: A cryo-electron tomography perspective.Protein science : a publication of the Protein Society · 2020
    Review
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.

Mary EckeMax Planck Institute of Biochemistry, D-82152 Martinsried, Munich, Germany.
Jana PrasslerMax Planck Institute of Biochemistry, D-82152 Martinsried, Munich, Germany.
Patrick TanribilMax Planck Institute of Biochemistry, D-82152 Martinsried, Munich, Germany.
Annette Müller-TaubenbergerDepartment of Cell Biology (Anatomy III), Ludwig Maximilian University of Munich, D-82152 Planegg-Martinsried, Munich, Germany.
Sarah KörberInstitute of Biophysical Chemistry, Hannover Medical School, D-30625 Hannover, Germany.
Jan FaixInstitute of Biophysical Chemistry, Hannover Medical School, D-30625 Hannover, Germany.
Günther GerischMax Planck Institute of Biochemistry, D-82152 Martinsried, Munich, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Circular actin waves separate two distinct areas on the substrate-attached cell surface from each other: an external area from an inner territory that is circumscribed by the wave. These areas differ in composition of actin-associated proteins and of phosphoinositides in the membrane. At the propagating wave, one area is converted into the other. By photo-conversion of Eos-actin and analysis of actin network structures we show that both in the inner territory and the external area the actin network is subject to continuous turnover. To address the question of whether areas in the wave pattern are specified by particular actin polymerizing machines, we locate five members of the formin family to specific regions of the wave landscape using TIRF microscopy and constitutively active formin constructs tagged with fluorescent protein. Formin ForB favors the actin wave and ForG the inner territory, whereas ForA, ForE, and ForH are more strongly recruited to the external area. Fluctuations of membrane binding peculiar to ForB indicate transient states in the specification of membrane domains before differentiation into ForB decorated and depleted ones. Annihilation of the patterns by 1 µM of the formin inhibitor SMIFH2 supports the implication of formins in their generation.

Indexed as

Actin-Related Protein 2-3 ComplexActinsCell Adhesion MoleculesCell MembraneDictyosteliumForminsMicrofilament ProteinsPhosphoproteinsPolymerizationProtozoan ProteinsThionesUracilVasodilator-Stimulated PhosphoproteinActin-Related Protein 2-3 ComplexActinsCell Adhesion MoleculesForminsMicrofilament ProteinsPhosphoproteinsProtozoan ProteinsSMIFH2 compoundThionesUracilVasodilator-Stimulated Phosphoprotein

Identifiers

PMID31940262
PMCPMC7183788

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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.