Evidence map›Paper›PMID 42789714›Full record

ArticleScience advances2026

Distinct Arp2/3 isocomplexes drive axonal actin ring assembly and integrity.

Ana Rita Costa, Teresa Lopes, Luís P Rodrigues, João M Rocha, José C Mateus, Maria Leonor Moura, Christoph Spahn, Marko Lampe, Naoko Kogata, António J Pereira and 5 more

Abstract read
In one paragraph

Article in Science advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

15 authors.

Ana Rita Costai3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal.ORCID 0000-0002-2855-0472
Teresa Lopesi3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal.
Luís P Rodriguesi3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal.ORCID 0009-0000-2589-212X
João M Rochai3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal.ORCID 0009-0007-7016-6259
José C Mateusi3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal.ORCID 0000-0001-8058-5093
Maria Leonor Mourai3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal.ORCID 0009-0000-8107-5167
Christoph SpahnRudolf Virchow Center-Center for Integrative and Translational Bioimaging, Julius-Maximilians-University Würzburg, Würzburg, Germany.ORCID 0000-0001-9886-2263
Marko LampeAdvanced Light Microscopy Facility, European Molecular Biology Laboratory, Heidelberg, Germany.ORCID 0000-0002-4510-9048
Naoko KogataThe Francis Crick Institute, London, UK.ORCID 0000-0002-7777-0797
António J Pereirai3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal.
Paulo Aguiari3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal.ORCID 0000-0003-4164-5713
Pedro Britesi3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal.
Paula Sampaioi3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal.ORCID 0000-0003-1148-2159
Michael WayThe Francis Crick Institute, London, UK.ORCID 0000-0001-7207-2722
Monica M Sousai3S-Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Porto, Portugal.ORCID 0000-0002-4524-2260

Funding

Wellcome Trust CC2096
6 · The paper itself

Abstract

The actin-related protein 2/3 (Arp2/3) complex is a central nucleator of branched actin filaments, essential for numerous cellular processes. Using superresolution imaging, we demonstrate that Arp2/3 is a component of the membrane periodic skeleton (MPS)-a highly ordered actin ring-spectrin lattice in the submembrane axonal cytoskeleton. While generally viewed as a single entity, functional specialization of the Arp2/3 complex arises from isoform diversity of three of its seven subunits. Moreover, isoform-specific perturbations revealed that distinct Arp2/3 isocomplexes orchestrate successive stages of MPS actin ring development. While Arp2/3 isocomplexes containing ARPC1A and ARPC5 are essential for actin ring assembly during early MPS formation, those with ARPC1B and ARPC5L are key to maintaining actin rings in mature axons. These findings demonstrate that beyond linear actin, branched actin filaments contribute to the MPS nanoarchitecture and uncover a switch in Arp2/3 isocomplex composition that is required to ensure actin ring assembly and stability.

Indexed as

Actin CytoskeletonActin-Related Protein 2-3 ComplexActinsAxonsAnimalsMiceActin-Related Protein 2-3 ComplexActins

Identifiers

PMID42789714
PMCPMC13614374

What OpenQuestion holds

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Registered trials

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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.