Evidence map›Paper›PMID 21613547›Full record

ArticleMolecular biology of the cell2011

Turnover of branched actin filament networks by stochastic fragmentation with ADF/cofilin.

Anne-Cécile Reymann, Cristian Suarez, Christophe Guérin, Jean-Louis Martiel, Christopher J Staiger, Laurent Blanchoin, Rajaa Boujemaa-Paterski

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

32 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Actin Turnover in Lamellipodial Fragments.Current biology : CB · 2017
    Article
  16. Article
  17. Article
  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

7 authors at 2 institutions in 2 countries.

Anne-Cécile ReymannLaboratoire de Physiologie Cellulaire & Végétale, Institut de Recherches en Technologies et Sciences pour le Vivant, Centre National de la Recherche Scientifique/Commissariat à l'énergie atomique et aux énergies alternatives/Institut National de la Recherche Agronomique/Université Joseph Fourier, Grenoble 38054, France.
Cristian Suarez
Christophe Guérin
Jean-Louis Martiel
Christopher J Staiger
Laurent Blanchoin
Rajaa Boujemaa-Paterski
Centre National de la Recherche Scientifique · FRPurdue University West Lafayette · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell motility depends on the rapid assembly, aging, severing, and disassembly of actin filaments in spatially distinct zones. How a set of actin regulatory proteins that sustains actin-based force generation during motility work together in space and time remains poorly understood. We present our study of the distribution and dynamics of Arp2/3 complex, capping protein (CP), and actin-depolymerizing factor (ADF)/cofilin in actin "comet tails," using a minimal reconstituted system with nucleation-promoting factor (NPF)-coated beads. The Arp2/3 complex concentrates at nucleation sites near the beads as well as in the first actin shell. CP colocalizes with actin and is homogeneously distributed throughout the comet tail; it serves to constrain the spatial distribution of ATP/ADP-P(i) filament zones to areas near the bead. The association of ADF/cofilin with the actin network is therefore governed by kinetics of actin assembly, actin nucleotide state, and CP binding. A kinetic simulation accurately validates these observations. Following its binding to the actin networks, ADF/cofilin is able to break up the dense actin filament array of a comet tail. Stochastic severing by ADF/cofilin loosens the tight entanglement of actin filaments inside the comet tail and facilitates turnover through the macroscopic release of large portions of the aged actin network.

Indexed as

Actin Capping ProteinsActin CytoskeletonActin-Related Protein 2-3 ComplexAnimalsCattleCell MovementDestrinFluorescence Recovery After PhotobleachingKineticsMicrospheresRabbitsActin Capping ProteinsActin-Related Protein 2-3 ComplexDestrin

Identifiers

PMID21613547
PMCPMC3135479
OpenAlexW2018824068

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.