Evidence map›Paper›PMID 21723825›Full record

ArticleBiophysical journal2011

Cofilin-linked changes in actin filament flexibility promote severing.

Brannon R McCullough, Elena E Grintsevich, Christine K Chen, Hyeran Kang, Alan L Hutchison, Arnon Henn, Wenxiang Cao, Cristian Suarez, Jean-Louis Martiel, Laurent Blanchoin and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

100 citing papers in PubMed, 149 citations in OpenAlex.

  1. Review
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  9. Article
  10. Article
  11. Principles and regulation of mechanosensing.Journal of cell science · 2024
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Twist response of actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Article
  18. Article
  19. Article
  20. Article

40 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

12 authors at 3 institutions in 2 countries.

Brannon R McCulloughDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, USA.
Elena E Grintsevich
Christine K Chen
Hyeran Kang
Alan L Hutchison
Arnon Henn
Wenxiang Cao
Cristian Suarez
Jean-Louis Martiel
Laurent Blanchoin
Emil Reisler
Enrique M De La Cruz
Yale University · USInstitut National de la Recherche Agronomique · MAUniversity of California, Los Angeles · US

Funding

Dynamic Events in Myosin and Actin and Their FunctionR01GM077190 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI REISLER, EMIL · 2006 to 2020
$6.2M
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 GM071688-03S1NIGMS NIH HHS R01 GM071688NIGMS NIH HHS R01 GM077190
6 · The paper itself

Abstract

The actin regulatory protein, cofilin, increases the bending and twisting elasticity of actin filaments and severs them. It has been proposed that filaments partially decorated with cofilin accumulate stress from thermally driven shape fluctuations at bare (stiff) and decorated (compliant) boundaries, thereby promoting severing. This mechanics-based severing model predicts that changes in actin filament compliance due to cofilin binding affect severing activity. Here, we test this prediction by evaluating how the severing activities of vertebrate and yeast cofilactin scale with the flexural rigidities determined from analysis of shape fluctuations. Yeast actin filaments are more compliant in bending than vertebrate actin filaments. Severing activities of cofilactin isoforms correlate with changes in filament flexibility. Vertebrate cofilin binds but does not increase the yeast actin filament flexibility, and does not sever them. Imaging of filament thermal fluctuations reveals that severing events are associated with local bending and fragmentation when deformations attain a critical angle. The critical severing angle at boundaries between bare and cofilin-decorated segments is smaller than in bare or fully decorated filaments. These measurements support a cofilin-severing mechanism in which mechanical asymmetry promotes local stress accumulation and fragmentation at boundaries of bare and cofilin-decorated segments, analogous to failure of some nonprotein materials.

Indexed as

Actin CytoskeletonActin Depolymerizing FactorsAnimalsElasticityHumansModels, MolecularMolecular ConformationPliabilityRabbitsSaccharomyces cerevisiaeSchizosaccharomycesActin Depolymerizing Factors

Identifiers

PMID21723825
PMCPMC3127193
OpenAlexW1974086731

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.