Evidence map›Paper›PMID 28625781›Full record

ArticleCurrent biology : CB2017

ADF/Cofilin Accelerates Actin Dynamics by Severing Filaments and Promoting Their Depolymerization at Both Ends.

Hugo Wioland, Berengere Guichard, Yosuke Senju, Sarah Myram, Pekka Lappalainen, Antoine Jégou, Guillaume Romet-Lemonne

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 147 papers.

0numbers the graph read from it
0cells of the map it votes in
147citing papers in PubMed
11.2field-weighted citation impact, top 1% 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

147 citing papers in PubMed, 251 citations in OpenAlex.

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  13. ATP-dependent actin barbed-end fluctuations at steady state.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Cofilin Inhibition Ameliorates PIEZO2 and AMPA Dysfunction in a Mouse Model of Angelman Syndrome.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025
    Article
  15. Article
  16. Review
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87 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

7 authors at 4 institutions in 2 countries.

Hugo WiolandInstitut Jacques Monod, CNRS, Université Paris Diderot, 75013 Paris, France.
Berengere GuichardInstitut Jacques Monod, CNRS, Université Paris Diderot, 75013 Paris, France.
Yosuke SenjuInstitute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland.
Sarah MyramInstitut Jacques Monod, CNRS, Université Paris Diderot, 75013 Paris, France.
Pekka LappalainenInstitute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland.
Antoine JégouInstitut Jacques Monod, CNRS, Université Paris Diderot, 75013 Paris, France. Electronic address: antoine.jegou@ijm.fr.
Guillaume Romet-LemonneInstitut Jacques Monod, CNRS, Université Paris Diderot, 75013 Paris, France. Electronic address: romet@ijm.fr.
Université Paris Cité · FRUniversity of Helsinki · FICentre National de la Recherche Scientifique · FRInstitut Jacques Monod · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Actin-depolymerizing factor (ADF)/cofilins contribute to cytoskeletal dynamics by promoting rapid actin filament disassembly. In the classical view, ADF/cofilin sever filaments, and capping proteins block filament barbed ends whereas pointed ends depolymerize, at a rate that is still debated. Here, by monitoring the activity of the three mammalian ADF/cofilin isoforms on individual skeletal muscle and cytoplasmic actin filaments, we directly quantify the reactions underpinning filament severing and depolymerization from both ends. We find that, in the absence of monomeric actin, soluble ADF/cofilin can associate with bare filament barbed ends to accelerate their depolymerization. Compared to bare filaments, ADF/cofilin-saturated filaments depolymerize faster from their pointed ends and slower from their barbed ends, resulting in similar depolymerization rates at both ends. This effect is isoform specific because depolymerization is faster for ADF- than for cofilin-saturated filaments. We also show that, unexpectedly, ADF/cofilin-saturated filaments qualitatively differ from bare filaments: their barbed ends are very difficult to cap or elongate, and consequently undergo depolymerization even in the presence of capping protein and actin monomers. Such depolymerizing ADF/cofilin-decorated barbed ends are produced during 17% of severing events. They are also the dominant fate of filament barbed ends in the presence of capping protein, because capping allows growing ADF/cofilin domains to reach the barbed ends, thereby promoting their uncapping and subsequent depolymerization. Our experiments thus reveal how ADF/cofilin, together with capping protein, control the dynamics of actin filament barbed and pointed ends. Strikingly, our results propose that significant barbed-end depolymerization may take place in cells.

Indexed as

Actin CytoskeletonActinsAnimalsCattleCofilin 1Cofilin 2DestrinHumansPolymerizationRabbitsActinsCofilin 1Cofilin 2Destrinactin-depolymerizing factoractin dynamicsbarbed-end depolymerizationcapping proteincofilinmicrofluidicsnon-muscle actinsingle filaments

Identifiers

PMID28625781
PMCPMC5505867
OpenAlexW2626922536

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.