Evidence map›Paper›PMID 19362000›Full record

ArticleCurrent biology : CB2009

Cofilin dissociates Arp2/3 complex and branches from actin filaments.

Chikio Chan, Christopher C Beltzner, Thomas D Pollard

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.

0numbers the graph read from it
0cells of the map it votes in
121citing papers in PubMed
7.9field-weighted citation impact, top 2% 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

121 citing papers in PubMed, 194 citations in OpenAlex.

  1. Article
  2. Review
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  7. Article
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  9. Review
  10. Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023
    Review
  11. Article
  12. Biochemical and mechanical regulation of actin dynamics.Nature reviews. Molecular cell biology · 2022
    Review
  13. Article
  14. Review
  15. Single-molecule analysis of actin filament debranching by cofilin and GMF.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Celebrating 20 years of live single-actin-filament studies with five golden rules.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  20. Review

61 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

3 authors at 1 institution in 1 country.

Chikio ChanDepartment of Molecular Cellular, Yale University, PO Box 208103, New Haven, CT 06520-8103, USA.
Christopher C Beltzner
Thomas D Pollard
Yale University · US

Funding

MOLECULAR MECHANISMS OF CELLULAR MOTILITYR01GM026338 · NIGMS · YALE UNIVERSITY · PI POLLARD, THOMAS D. · 1985 to 2020
$9.8M
NIGMS NIH HHS GM-026338NIGMS NIH HHS R01 GM026338
6 · The paper itself

Abstract

backgroundActin-based cellular motility requires spatially and temporally coordinated remodeling of a network of branched actin filaments. This study investigates how cofilin and Arp2/3 complex, two main players in the dendritic nucleation model, interact to produce sharp spatial transitions between densely branched filaments and long, unbranched filaments.

resultsWe found that cofilin binding reduces both the affinity of actin filaments for Arp2/3 complex and the stability of branches. We used fluorescence spectroscopy to measure the kinetics of cofilin association with filaments and the resulting dissociation of Arp2/3 complex and TIRF microscopy to visualize filament severing and the loss of actin filament branches. Cofilin severs filaments optimally when few actin subunits are occupied but dissociates branches rapidly only at higher occupancies. Effective debranching is nevertheless achieved, as a result of cooperative binding and reduced affinity of Arp2/3 complex for the filament, at cofilin concentrations below those required for direct competition.

conclusionsCofilin rapidly dissociates Arp2/3 complex and branches by direct competition for binding sites on the actin filament and by propagation of structural changes in the actin filament that reduce affinity for Arp2/3 complex.

Indexed as

Actin Depolymerizing FactorsActin-Related Protein 2-3 ComplexActinsAdenosine DiphosphateAnimalsCell MovementChickensProtein BindingSchizosaccharomycesSchizosaccharomyces pombe ProteinsActin Depolymerizing FactorsActin-Related Protein 2-3 ComplexActinsAdenosine DiphosphateSchizosaccharomyces pombe Proteins

Identifiers

PMID19362000
PMCPMC3711486
OpenAlexW2063065938

What OpenQuestion holds

Textmetadata
LicenceTDM
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.