Evidence map›Paper›PMID 33558729›Full record

ArticleNature cell biology2021

Twinfilin uncaps filament barbed ends to promote turnover of lamellipodial actin networks.

Markku Hakala, Hugo Wioland, Mari Tolonen, Tommi Kotila, Antoine Jegou, Guillaume Romet-Lemonne, Pekka Lappalainen

Erratum issuedOpen access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Nature cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
6.9field-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

53 citing papers in PubMed, 74 citations in OpenAlex.

  1. RHAMM drives formation of polyploid cancer cells and confers resistance to ER-targeted therapy in breast cancer.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  9. Regulation of actin dynamics by Twinfilin.Current opinion in cell biology · 2025
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Markku HakalaInstitute of Biotechnology and Helsinki Institute of Life Sciences, University of Helsinki, Helsinki, Finland.ORCID http://orcid.org/0000-0002-3485-6080
Hugo WiolandUniversité de Paris, CNRS, Institut Jacques Monod, Paris, France.ORCID http://orcid.org/0000-0001-5254-9642
Mari TolonenInstitute of Biotechnology and Helsinki Institute of Life Sciences, University of Helsinki, Helsinki, Finland.
Tommi KotilaInstitute of Biotechnology and Helsinki Institute of Life Sciences, University of Helsinki, Helsinki, Finland.ORCID http://orcid.org/0000-0002-9046-5834
Antoine JegouUniversité de Paris, CNRS, Institut Jacques Monod, Paris, France.ORCID http://orcid.org/0000-0003-0356-3127
Guillaume Romet-LemonneUniversité de Paris, CNRS, Institut Jacques Monod, Paris, France.ORCID http://orcid.org/0000-0002-4938-1065
Pekka LappalainenInstitute of Biotechnology and Helsinki Institute of Life Sciences, University of Helsinki, Helsinki, Finland. pekka.lappalainen@helsinki.fi.ORCID http://orcid.org/0000-0001-6227-0354
University of Helsinki · FICentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Coordinated polymerization of actin filaments provides force for cell migration, morphogenesis and endocytosis. Capping protein (CP) is a central regulator of actin dynamics in all eukaryotes. It binds to actin filament (F-actin) barbed ends with high affinity and slow dissociation kinetics to prevent filament polymerization and depolymerization. However, in cells, CP displays remarkably rapid dynamics within F-actin networks, but the underlying mechanism remains unclear. Here, we report that the conserved cytoskeletal regulator twinfilin is responsible for CP's rapid dynamics and specific localization in cells. Depletion of twinfilin led to stable association between CP and cellular F-actin arrays, as well as to its retrograde movement throughout leading-edge lamellipodia. These were accompanied by diminished F-actin turnover rates. In vitro single-filament imaging approaches revealed that twinfilin directly promotes dissociation of CP from filament barbed ends, while enabling subsequent filament depolymerization. These results uncover a bipartite mechanism that controls how actin cytoskeleton-mediated forces are generated in cells.

Indexed as

Actin CytoskeletonActinsAdenosine DiphosphateAnimalsFluorescence Recovery After PhotobleachingGreen Fluorescent ProteinsMiceMice, KnockoutMicrofilament ProteinsMutationPolymerizationPseudopodiaActinsAdenosine DiphosphateGreen Fluorescent ProteinsMicrofilament ProteinsTwf1 protein, mouse

Identifiers

PMID33558729
OpenAlexW3126944731

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.