Evidence map›Paper›PMID 21530260›Full record

ArticleCurrent biology : CB2011

Cofilin tunes the nucleotide state of actin filaments and severs at bare and decorated segment boundaries.

Cristian Suarez, Jérémy Roland, Rajaa Boujemaa-Paterski, Hyeran Kang, Brannon R McCullough, Anne-Cécile Reymann, Christophe Guérin, Jean-Louis Martiel, Enrique M De la Cruz, Laurent Blanchoin

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 150 papers.

0numbers the graph read from it
0cells of the map it votes in
150citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

150 citing papers in PubMed, 230 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
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  9. Review
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  13. ADPact: A versatile sensor for ADP-F-actin.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
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  20. Article

90 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

10 authors at 5 institutions in 2 countries.

Cristian SuarezLaboratoire de Physiologie Cellulaire et Végétale, Institut de Recherches en Sciences et Technologies pour le Vivant, CEA/CNRS/INRA/UJF, F-38054 Grenoble, France.
Jérémy Roland
Rajaa Boujemaa-Paterski
Hyeran Kang
Brannon R McCullough
Anne-Cécile Reymann
Christophe Guérin
Jean-Louis Martiel
Enrique M De la Cruz
Laurent Blanchoin
Centre National de la Recherche Scientifique · FRYale University · USCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRCEA Grenoble · FRLaboratoire de Physiologie Cellulaire

Funding

Functional diversity of myosin VIIR01GM071688 · NIGMS · YALE UNIVERSITY · PI DE LA CRUZ, ENRIQUE M · 2007 to 2010
$1.2M
NIGMS NIH HHS GM071688NIGMS NIH HHS R01 GM071688
6 · The paper itself

Abstract

Actin-based motility demands the spatial and temporal coordination of numerous regulatory actin-binding proteins (ABPs), many of which bind with affinities that depend on the nucleotide state of actin filament. Cofilin, one of three ABPs that precisely choreograph actin assembly and organization into comet tails that drive motility in vitro, binds and stochastically severs aged ADP actin filament segments of de novo growing actin filaments. Deficiencies in methodologies to track in real time the nucleotide state of actin filaments, as well as cofilin severing, limit the molecular understanding of coupling between actin filament chemical and mechanical states and severing. We engineered a fluorescently labeled cofilin that retains actin filament binding and severing activities. Because cofilin binding depends strongly on the actin-bound nucleotide, direct visualization of fluorescent cofilin binding serves as a marker of the actin filament nucleotide state during assembly. Bound cofilin allosterically accelerates P(i) release from unoccupied filament subunits, which shortens the filament ATP/ADP-P(i) cap length by nearly an order of magnitude. Real-time visualization of filament severing indicates that fragmentation scales with and occurs preferentially at boundaries between bare and cofilin-decorated filament segments, thereby controlling the overall filament length, depending on cofilin binding density.

Indexed as

ActinsCofilin 1Escherichia coliImage Processing, Computer-AssistedLeast-Squares AnalysisMicroscopy, FluorescenceModels, BiologicalMovementNucleotidesProtein EngineeringSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsActinsCOF1 protein, S cerevisiaeCofilin 1NucleotidesSaccharomyces cerevisiae Proteins

Identifiers

PMID21530260
PMCPMC3100394
OpenAlexW2033926605

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.