Evidence map›Paper›PMID 31757941›Full record

ArticleNature communications2019

Mechanism of synergistic actin filament pointed end depolymerization by cyclase-associated protein and cofilin.

Tommi Kotila, Hugo Wioland, Giray Enkavi, Konstantin Kogan, Ilpo Vattulainen, Antoine Jégou, Guillaume Romet-Lemonne, Pekka Lappalainen

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
6.5field-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

80 citing papers in PubMed, 114 citations in OpenAlex.

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  19. Journal of virology · 2025
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20 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

8 authors at 2 institutions in 2 countries.

Tommi KotilaHiLIFE Institute of Biotechnology, University of Helsinki, FI-00014, Helsinki, Finland.ORCID http://orcid.org/0000-0002-9046-5834
Hugo WiolandUniversité de Paris, CNRS, Institut Jacques Monod, 75013, Paris, France.ORCID http://orcid.org/0000-0001-5254-9642
Giray EnkaviDepartment of Physics, University of Helsinki, FI-00014, Helsinki, Finland.ORCID http://orcid.org/0000-0001-5033-8649
Konstantin KoganHiLIFE Institute of Biotechnology, University of Helsinki, FI-00014, Helsinki, Finland.
Ilpo VattulainenDepartment of Physics, University of Helsinki, FI-00014, Helsinki, Finland.ORCID http://orcid.org/0000-0001-7408-3214
Antoine JégouUniversité de Paris, CNRS, Institut Jacques Monod, 75013, Paris, France.ORCID http://orcid.org/0000-0003-0356-3127
Guillaume Romet-LemonneUniversité de Paris, CNRS, Institut Jacques Monod, 75013, Paris, France.
Pekka LappalainenHiLIFE Institute of Biotechnology, University of Helsinki, FI-00014, Helsinki, Finland. pekka.lappalainen@helsinki.fi.
University of Helsinki · FICentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ability of cells to generate forces through actin filament turnover was an early adaptation in evolution. While much is known about how actin filaments grow, mechanisms of their disassembly are incompletely understood. The best-characterized actin disassembly factors are the cofilin family proteins, which increase cytoskeletal dynamics by severing actin filaments. However, the mechanism by which severed actin filaments are recycled back to monomeric form has remained enigmatic. We report that cyclase-associated-protein (CAP) works in synergy with cofilin to accelerate actin filament depolymerization by nearly 100-fold. Structural work uncovers the molecular mechanism by which CAP interacts with actin filament pointed end to destabilize the interface between terminal actin subunits, and subsequently recycles the newly-depolymerized actin monomer for the next round of filament assembly. These findings establish CAP as a molecular machine promoting rapid actin filament depolymerization and monomer recycling, and explain why CAP is critical for actin-dependent processes in all eukaryotes.

Indexed as

Actin CytoskeletonActinsAnimalsCarrier ProteinsCofilin 1Crystallography, X-RayMiceMolecular Dynamics SimulationProtein BindingProtein Interaction Domains and MotifsRabbitsActinsCAP1 cyclase-associated protein, mouseCarrier ProteinsCfl1 protein, mouseCofilin 1

Identifiers

PMID31757941
PMCPMC6876575
OpenAlexW2991078116

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.