Evidence map›Paper›PMID 23676663›Full record

ArticleMolecular biology of the cell2013

Instantaneous inactivation of cofilin reveals its function of F-actin disassembly in lamellipodia.

Eric A Vitriol, Ariel L Wise, Mathew E Berginski, James R Bamburg, James Q Zheng

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

36 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. SiR-XActin: A Fluorescent Probe for Imaging Actin Dynamics in Live Cells.Angewandte Chemie (International ed. in English) · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Biochemical and mechanical regulation of actin dynamics.Nature reviews. Molecular cell biology · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. Control of actin polymerizationFrontiers in cell and developmental biology · 2022
    Review
  13. Article
  14. Article
  15. Article
  16. Optical manipulation of molecular function by chromophore-assisted light inactivation.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2021
    Review
  17. Article
  18. Article
  19. Dual role of cofilin in APP trafficking and amyloid-β clearance.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    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

5 authors at 3 institutions in 1 country.

Eric A VitriolDepartments of Cell Biology and Neurology, Center for Neurodegenerative Diseases, Emory University School of Medicine, Atlanta, GA 30322, USA.
Ariel L Wise
Mathew E Berginski
James R Bamburg
James Q Zheng
Emory University · USColorado State University · USUniversity of North Carolina at Chapel Hill · US

Funding

ENNCF - Viral Vector CoreP30NS055077 · NINDS · EMORY UNIVERSITY · PI SEYFRIED, NICHOLAS THOMAS · 2008 to 2018
$6.8M
Mechanisms of growth cone turning in diffusible gradientR01GM083889 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI ZHENG, JAMES Q · 2007 to 2021
$4.5M
Spatiotemporal Control of Cofilin Activity During Growth Cone MigrationF32NS077612 · NINDS · EMORY UNIVERSITY · PI VITRIOL, ERIC A · 2011 to 2013
$105k
NIGMS NIH HHS R01 GM083889NINDS NIH HHS P30 NS055077NINDS NIH HHS P30NS055077
6 · The paper itself

Abstract

Cofilin is a key regulator of the actin cytoskeleton. It can sever actin filaments, accelerate filament disassembly, act as a nucleation factor, recruit or antagonize other actin regulators, and control the pool of polymerization-competent actin monomers. In cells these actions have complex functional outputs. The timing and localization of cofilin activity are carefully regulated, and thus global, long-term perturbations may not be sufficient to probe its precise function. To better understand cofilin's spatiotemporal action in cells, we implemented chromophore-assisted laser inactivation (CALI) to instantly and specifically inactivate it. In addition to globally inhibiting actin turnover, CALI of cofilin generated several profound effects on the lamellipodia, including an increase of F-actin, a rearward expansion of the actin network, and a reduction in retrograde flow speed. These results support the hypothesis that the principal role of cofilin in lamellipodia at steady state is to break down F-actin, control filament turnover, and regulate the rate of retrograde flow.

Indexed as

Actin CytoskeletonActin Depolymerizing FactorsActinsAnimalsCell Line, TumorGene Expression RegulationGenes, ReporterGreen Fluorescent ProteinsHalf-LifeKineticsLasersMiceNeuronsPhotosensitizing AgentsProtein StabilityPseudopodiaActin Depolymerizing FactorsActinsGreen Fluorescent Proteinskiller red protein, AnthomedusaePhotosensitizing Agents

Identifiers

PMID23676663
PMCPMC3708729
OpenAlexW2168936544

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.