Evidence map›Paper›PMID 21940796›Full record

ArticleJournal of cell science2011

Cofilin cooperates with fascin to disassemble filopodial actin filaments.

Dennis Breitsprecher, Stefan A Koestler, Igor Chizhov, Maria Nemethova, Jan Mueller, Bruce L Goode, J Victor Small, Klemens Rottner, Jan Faix

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

97 citing papers in PubMed, 158 citations in OpenAlex.

  1. Article
  2. Myosin II-independent contraction of actin filaments in membrane nanotubes.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Review
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  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023
    Review
  17. Article
  18. Article
  19. Disassembly of bundled F-actin and cellular remodeling via an interplay of Mical, cofilin, and F-actin crosslinkers.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  20. Review

37 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

9 authors at 6 institutions in 3 countries.

Dennis BreitsprecherInstitute for Biophysical Chemistry, Hannover Medical School, Carl-Neuberg-Str. 1, D-30625 Hannover, Germany.
Stefan A Koestler
Igor Chizhov
Maria Nemethova
Jan Mueller
Bruce L Goode
J Victor Small
Klemens Rottner
Jan Faix
Medizinische Hochschule Hannover · DEAustrian Academy of Sciences · ATBrandeis University · USHelmholtz Centre for Infection Research · DEInstitute of Molecular Biotechnology · ATUniversity of Bonn · DE

Funding

MECHNISMS REGULATING ACTIN ASSEMBLYR01GM063691 · NIGMS · BRANDEIS UNIVERSITY · PI GOODE, BRUCE L · 2002 to 2019
$7.5M
Austrian Science Fund FWF I 516Austrian Science Fund FWF P 21292NIGMS NIH HHS R01 GM063691
6 · The paper itself

Abstract

Cells use a large repertoire of proteins to remodel the actin cytoskeleton. Depending on the proteins involved, F-actin is organized in specialized protrusions such as lamellipodia or filopodia, which serve diverse functions in cell migration and sensing. Although factors responsible for directed filament assembly in filopodia have been extensively characterized, the mechanisms of filament disassembly in these structures are mostly unknown. We investigated how the actin-depolymerizing factor cofilin-1 affects the dynamics of fascincrosslinked actin filaments in vitro and in live cells. By multicolor total internal reflection fluorescence microscopy and fluorimetric assays, we found that cofilin-mediated severing is enhanced in fascin-crosslinked bundles compared with isolated filaments, and that fascin and cofilin act synergistically in filament severing. Immunolabeling experiments demonstrated for the first time that besides its known localization in lamellipodia and membrane ruffles, endogenous cofilin can also accumulate in the tips and shafts of filopodia. Live-cell imaging of fluorescently tagged proteins revealed that cofilin is specifically targeted to filopodia upon stalling of protrusion and during their retraction. Subsequent electron tomography established filopodial actin filament and/or bundle fragmentation to precisely correlate with cofilin accumulation. These results identify a new mechanism of filopodium disassembly involving both fascin and cofilin.

Indexed as

Protein MultimerizationActin CytoskeletonActin Depolymerizing FactorsAnimalsCarrier ProteinsCell LineGreen Fluorescent ProteinsHumansKineticsMiceMicrofilament ProteinsMicroscopy, FluorescencePhalloidinePseudopodiaRecombinant Fusion ProteinsTime-Lapse ImagingActin Depolymerizing FactorsCarrier ProteinsfascinGreen Fluorescent ProteinsMicrofilament ProteinsPhalloidineRecombinant Fusion Proteins

Identifiers

PMID21940796
PMCPMC4074248
OpenAlexW2078801891

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.