Evidence map›Paper›PMID 18617188›Full record

ArticleJournal of molecular biology2008

Cofilin increases the bending flexibility of actin filaments: implications for severing and cell mechanics.

Brannon R McCullough, Laurent Blanchoin, Jean-Louis Martiel, Enrique M De la Cruz

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 131 papers.

0numbers the graph read from it
0cells of the map it votes in
131citing papers in PubMed
5.0field-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

131 citing papers in PubMed, 234 citations in OpenAlex.

  1. Article
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  5. Core-sheath coupling controls flagellar curvature and motility inbioRxiv : the preprint server for biology · 2026
    Article
  6. Sensing the shape of a surface by tightly surface-bound filaments.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. SurFlex microscopy: Measuring flexibility of surface-tethered biomolecules.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  15. Reducing Cofilin dosage makes embryos resilient to heat stress.bioRxiv : the preprint server for biology · 2025
    Article
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71 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

4 authors at 3 institutions in 2 countries.

Brannon R McCulloughYale University, Department of Molecular Biophysics and Biochemistry, 260 Whitney Avenue, New Haven, CT 06520, USA.
Laurent Blanchoin
Jean-Louis Martiel
Enrique M De la Cruz
Yale University · USInstitut de Recherches en Technologies et Sciences pour le Vivant · FRTranslational Innovation in Medicine and Complexity · FR

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
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 GM071688NIGMS NIH HHS T32 GM007223NIGMS NIH HHS T32GM007223
6 · The paper itself

Abstract

We determined the flexural (bending) rigidities of actin and cofilactin filaments from a cosine correlation function analysis of their thermally driven, two-dimensional fluctuations in shape. The persistence length of actin filaments is 9.8 microm, corresponding to a flexural rigidity of 0.040 pN microm(2). Cofilin binding lowers the persistence length approximately 5-fold to a value of 2.2 microm and the filament flexural rigidity to 0.0091 pN microm(2). That cofilin-decorated filaments are more flexible than native filaments despite an increased mass indicates that cofilin binding weakens and redistributes stabilizing subunit interactions of filaments. We favor a mechanism in which the increased flexibility of cofilin-decorated filaments results from the linked dissociation of filament-stabilizing ions and reorganization of actin subdomain 2 and as a consequence promotes severing due to a mechanical asymmetry. Knowledge of the effects of cofilin on actin filament bending mechanics, together with our previous analysis of torsional stiffness, provide a quantitative measure of the mechanical changes in actin filaments associated with cofilin binding, and suggest that the overall mechanical and force-producing properties of cells can be modulated by cofilin activity.

Indexed as

Actin CytoskeletonAnimalsBiomechanical PhenomenaCofilin 2Computer SimulationCytoskeletonMicrofilament ProteinsPliabilityRabbitsCofilin 2Microfilament Proteins

Identifiers

PMID18617188
PMCPMC2753234
OpenAlexW1974329525

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.