Evidence map›Paper›PMID 31301801›Full record

ArticleBiophysical journal2019

Plastic Deformation and Fragmentation of Strained Actin Filaments.

Anthony C Schramm, Glen M Hocky, Gregory A Voth, Jean-Louis Martiel, Enrique M De La Cruz

Abstract read
In one paragraph

Article in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Adaptive nonequilibrium design of actin-based metamaterials: Fundamental and practical limits of control.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. Twist response of actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. LIM domain proteins in cell mechanobiology.Cytoskeleton (Hoboken, N.J.) · 2021
    Review
  13. Article
  14. Article
  15. 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
  16. 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.

Anthony C SchrammDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut.
Glen M HockyDepartment of Chemistry, New York University, New York, New York.
Gregory A VothDepartment of Chemistry, Institute for Biophysical Dynamics, and James Franck Institute, University of Chicago, Chicago, Illinois.
Jean-Louis MartielTIMC-IMAG Lab, UMR 5525, Inserm/CNRS/Université Grenoble-Alpes, Tronche, France. Electronic address: jean-louis.martiel@univ-grenoble-alpes.fr.
Enrique M De La CruzDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut. Electronic address: enrique.delacruz@yale.edu.

Funding

Actin filament elasticity and actin-binding protein functionR01GM097348 · NIGMS · YALE UNIVERSITY · PI DE LA CRUZ, ENRIQUE M · 2011 to 2018
$3.1M
NIGMS NIH HHS R01 GM097348
6 · The paper itself

Abstract

The assembly of actin filaments and filament networks generate forces that drive cell and vesicle movement. These structures and the comprising actin filaments must be mechanically stable to sustain these forces and maintain their structural integrity. Filaments in these dynamic structures must also be disassembled to recycle and replenish the pool of actin monomers available for polymerization. Actin-severing proteins such as cofilin and contractile myosin motor proteins fragment these nominally stable structures. We developed a mesoscopic-length-scale actin filament model to investigate force-induced filament fragmentation. We show that fragmentation in our model occurs at curvatures similar to previous measurements of fragmentation within (cofil)actin and actin-cofilactin boundaries. Boundaries between bare and cofilin-decorated segments are brittle and fragment at small bending and twisting deformations. Extending filaments disperses strain uniformly over subunit interfaces, and filaments fragment with no detectable partial rupture or plastic deformation. In contrast, bending or twisting filaments imposes nonuniform interface strain and leads to partial interface rupture, accelerating filament fragmentation. As a result, the rupture force under compressive loads is an order of magnitude lower than under tensile loads. Partial interface rupture may be a primary mechanism of accelerating actin filament fragmentation by other actin-destabilizing proteins.

Indexed as

Stress, MechanicalActin CytoskeletonActinsBiomechanical PhenomenaKineticsProtein BindingProtein SubunitsActinsProtein Subunits

Identifiers

PMID31301801
PMCPMC6697348

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.