Evidence map›Paper›PMID 23911787›Full record

ArticleBiochemical and biophysical research communications2013

Competitive displacement of cofilin can promote actin filament severing.

W Austin Elam, Hyeran Kang, Enrique M De La Cruz

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.8field-weighted citation impact, top 11% 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

35 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Torsional stress generated by ADF/cofilin on cross-linked actin filaments boosts their severing.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

W Austin ElamDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
Hyeran Kang
Enrique M De La Cruz
Yale University · US

Funding

R25 IMSD Minority Biomedical Research Support Program (MBRS)R25GM096161 · NIGMS · RUTGERS THE STATE UNIV OF NJ NEWARK · PI KOMISARUK, BARRY RICHARD · 2011 to 2020
$6.2M
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 GM097348NIGMS NIH HHS R01-GM097348NIGMS NIH HHS R25 GM096161
6 · The paper itself

Abstract

Cofilin is an essential actin filament severing protein that functions in the dynamic remodeling of the actin cytoskeleton. Filament severing activity is most efficient at sub-stoichiometric cofilin binding densities (i.e. <1 cofilin per actin filament subunit), and peaks when the number density of boundaries (i.e. junctions) between bare and cofilin-decorated segments is maximal. A model in which local topological and mechanical discontinuities lead to preferential fragmentation at boundaries accounts for available experimental data, including direct visualization of cofilin and actin during real-time severing events. The boundary-severing model predicts that ligands (e.g. other actin-binding proteins) that compete with cofilin for actin filament binding and modulate cofilin occupancy on filaments will alter the bare-decorated segment boundary density, and thus, the filament severing activity of cofilin. Here, we directly test this model prediction by evaluating the effects of phalloidin and myosin, two ligands that compete with cofilin for filament binding, on the actin filament binding and severing activities of cofilin. Our experiments demonstrate that competitive displacement of cofilin lowers cofilin occupancy and promotes severing when initial cofilin occupancy is high (i.e. >50%). Even in the presence of competitive ligands, maximum severing activity occurs when cofilin-decorated boundary density is highest, consistent with preferential fragmentation at boundaries. We propose a general "severodyne" framework for the modulation of cofilin-mediated actin filament severing by small molecule or actin-binding protein ligands that compete with cofilin for actin filament binding.

Indexed as

Actin CytoskeletonActinsAnimalsCofilin 1HumansMyosinsPhalloidineProtein BindingRabbitsRecombinant ProteinsActinsCofilin 1MyosinsPhalloidineRecombinant ProteinsActin binding proteinaverage filament lengthcofilin binding densityCompetitionCytoskeletonL(avg)MyosinNEMN-ethylmaleimidePhalloidinS1subfragment 1XAip1Xenopus Actin-interacting protein 1ν(cof)

Identifiers

PMID23911787
PMCPMC3785092
OpenAlexW1975313456

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.