Evidence map›Paper›PMID 24958883›Full record

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

Single-molecule imaging and kinetic analysis of cooperative cofilin-actin filament interactions.

Kimihide Hayakawa, Shotaro Sakakibara, Masahiro Sokabe, Hitoshi Tatsumi

Open access · bronzeAbstract 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 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
10.0field-weighted citation impact, top 2% 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

40 citing papers in PubMed, 72 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. A Hierarchical Mechanotransduction System: From Macro to Micro.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Review
  8. Article
  9. Vascular mechanotransduction.Physiological reviews · 2023
    Review
  10. Twist response of actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Article
  12. Single-molecule analysis of actin filament debranching by cofilin and GMF.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Cofilin-induced structural changes in actin filaments stay local.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

4 authors at 2 institutions in 1 country.

Kimihide HayakawaCell Mechanosensing Project, International Cooperative Research Project/Solution-Oriented Research for Science and Technology, Japan Science and Technology Agency, Nagoya 466-8550, Japan; and.
Shotaro SakakibaraDepartment of Physiology, Nagoya University Graduate School of Medicine, Nagoya 466-8550, Japan.
Masahiro SokabeCell Mechanosensing Project, International Cooperative Research Project/Solution-Oriented Research for Science and Technology, Japan Science and Technology Agency, Nagoya 466-8550, Japan; andDepartment of Physiology, Nagoya University Graduate School of Medicine, Nagoya 466-8550, Japan.
Hitoshi TatsumiDepartment of Physiology, Nagoya University Graduate School of Medicine, Nagoya 466-8550, Japan tatsumi@med.nagoya-u.ac.jp.
Nagoya University · JPJapan Science and Technology Agency · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The actin filament-severing protein actin depolymerizing factor (ADF)/cofilin is ubiquitously distributed among eukaryotes and modulates actin dynamics. The cooperative binding of cofilin to actin filaments is crucial for the concentration-dependent unconventional modulation of actin dynamics by cofilin. In this study, the kinetic parameters associated with the cooperative binding of cofilin to actin filaments were directly evaluated using a single-molecule imaging technique. The on-rate of cofilin binding to the actin filament was estimated to be 0.06 µM(-1)⋅s(-1) when the cofilin concentration was in the range of 30 nM to 1 µM. A dwell time histogram of cofilin bindings decays exponentially to give an off-rate of 0.6 s(-1). During long-term cofilin binding events (>0.4 s), additional cofilin bindings were observed in the vicinity of the initial binding site. The on-rate for these events was 2.3-fold higher than that for noncontiguous bindings. Super-high-resolution image analysis of the cofilin binding location showed that the on-rate enhancement occurred within 65 nm of the original binding event. By contrast, the cofilin off-rate was not affected by the presence of prebound cofilin. Neither decreasing the temperature nor increasing the viscosity of the test solution altered the on-rates, off-rates, or the cooperative parameter (ω) of the binding. These results indicate that cofilin binding enhances additional cofilin binding in the vicinity of the initial binding site (ca. 24 subunits), but it does not affect the off-rate, which could be the molecular mechanism of the cooperative binding of cofilin to actin filaments.

Indexed as

ActinsCofilin 1Cofilin 2DestrinKineticsProtein BindingTemperatureViscosityActinsCofilin 1Cofilin 2Destrincooperativityfluctuationsnon-Arrheniusnon--nearest-neighborsuperresolution

Identifiers

PMID24958883
PMCPMC4103329
OpenAlexW1966086467

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.