Evidence map›Paper›PMID 25468977›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Site-specific cation release drives actin filament severing by vertebrate cofilin.

Hyeran Kang, Michael J Bradley, Wenxiang Cao, Kaifeng Zhou, Elena E Grintsevich, Alphée Michelot, Charles V Sindelar, Mark Hochstrasser, Enrique M De La Cruz

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

39 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023
    Review
  8. Article
  9. Article
  10. Twist response of actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Molecular and structural basis of actin filament severing by ADF/cofilin.Computational and structural biotechnology journal · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Force and phosphate release from Arp2/3 complex promote dissociation of actin filament branches.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  19. Article
  20. Structures of cofilin-induced structural changes reveal local and asymmetric perturbations of actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

9 authors at 3 institutions in 2 countries.

Hyeran KangDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520;
Michael J BradleyDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520;
Wenxiang CaoDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520;
Kaifeng ZhouDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520;
Elena E GrintsevichDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095; and.
Alphée MichelotPhysics of the Cytoskeleton and Morphogenesis Group, Institut de Recherches en Technologies et Sciences pour le Vivant, Laboratoire de Physiologie Cellulaire Végétale, CNRS, Commissariat à l'Énergie Atomique et aux Énergies Alternatives, Institut National de la Recherche Agronomique, Université Joseph Fourier, Grenoble 38054, France.
Charles V SindelarDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520;
Mark HochstrasserDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520;
Enrique M De La CruzDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520; enrique.delacruz@yale.edu.
Yale University · USLaboratoire Physiologie Cellulaire & Végétale · FRUniversity of California, Los Angeles · US

Funding

FUNCTIONS AND MECHANISMS OF DEUBIQUITINATING ENZYMESR01GM053756 · NIGMS · YALE UNIVERSITY · PI HOCHSTRASSER, MARK W · 1996 to 2019
$6.5M
Actin filament elasticity and actin-binding protein functionR01GM097348 · NIGMS · YALE UNIVERSITY · PI DE LA CRUZ, ENRIQUE M · 2011 to 2018
$3.1M
Structural basis of motility by dimeric kinesin motor proteinsR01GM110530 · NIGMS · YALE UNIVERSITY · PI SINDELAR, CHARLES VAUGHN · 2014 to 2023
$3.0M
NIGMS NIH HHS GM053756NIGMS NIH HHS GM11053001NIGMS NIH HHS R01 GM053756NIGMS NIH HHS R01 GM097348NIGMS NIH HHS R01-GM097348NIGMS NIH HHS R01 GM110530PHS HHS NIGMS 077190
6 · The paper itself

Abstract

Actin polymerization powers the directed motility of eukaryotic cells. Sustained motility requires rapid filament turnover and subunit recycling. The essential regulatory protein cofilin accelerates network remodeling by severing actin filaments and increasing the concentration of ends available for elongation and subunit exchange. Although cofilin effects on actin filament assembly dynamics have been extensively studied, the molecular mechanism of cofilin-induced filament severing is not understood. Here we demonstrate that actin filament severing by vertebrate cofilin is driven by the linked dissociation of a single cation that controls filament structure and mechanical properties. Vertebrate cofilin only weakly severs Saccharomyces cerevisiae actin filaments lacking this "stiffness cation" unless a stiffness cation-binding site is engineered into the actin molecule. Moreover, vertebrate cofilin rescues the viability of a S. cerevisiae cofilin deletion mutant only when the stiffness cation site is simultaneously introduced into actin, demonstrating that filament severing is the essential function of cofilin in cells. This work reveals that site-specific interactions with cations serve a key regulatory function in actin filament fragmentation and dynamics.

Indexed as

Models, MolecularActin CytoskeletonCationsCell MovementChromatography, AffinityCofilin 1Cryoelectron MicroscopyHumansSaccharomyces cerevisiaeCationsCFL1 protein, humanCofilin 1cytoskeletonelectron cryomicroscopymechanicspersistence length

Identifiers

PMID25468977
PMCPMC4273407
OpenAlexW2073120749

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.