Evidence map›Paper›PMID 42749745›Full record

ArticleNature communications2026

Profilin promotes lamellipodium protrusion by tuning the antagonistic activities of capping protein and VASP.

Yubo Tang, Matthias Schaks, Xinqi Jiang, Marius Karger, Magdalena Mietkowska, Julian Kaltenhäuser, Jonas Scholz, Ruth Benavente-Naranjo, Sijian Hu, Sarah Körber and 9 more

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

19 authors.

Yubo TangDivision of Molecular Cell Biology, Institute for Cell- and Neurobiology, Technische Universität Braunschweig, Braunschweig, Germany.ORCID 0009-0000-8813-7121
Matthias SchaksDivision of Molecular Cell Biology, Institute for Cell- and Neurobiology, Technische Universität Braunschweig, Braunschweig, Germany.
Xinqi JiangDivision of Molecular Cell Biology, Institute for Cell- and Neurobiology, Technische Universität Braunschweig, Braunschweig, Germany.ORCID 0009-0008-8492-4898
Marius KargerDivision of Molecular Cell Biology, Institute for Cell- and Neurobiology, Technische Universität Braunschweig, Braunschweig, Germany.ORCID 0009-0003-4513-3923
Magdalena MietkowskaDivision of Molecular Cell Biology, Institute for Cell- and Neurobiology, Technische Universität Braunschweig, Braunschweig, Germany.
Julian KaltenhäuserDivision of Molecular Cell Biology, Institute for Cell- and Neurobiology, Technische Universität Braunschweig, Braunschweig, Germany.ORCID 0009-0002-7780-4771
Jonas ScholzInstitute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany.ORCID 0009-0000-4789-4249
Ruth Benavente-NaranjoDivision of Molecular Cell Biology, Institute for Cell- and Neurobiology, Technische Universität Braunschweig, Braunschweig, Germany.
Sijian HuDivision of Molecular Cell Biology, Institute for Cell- and Neurobiology, Technische Universität Braunschweig, Braunschweig, Germany.ORCID 0009-0008-9701-9723
Sarah KörberInstitute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany.ORCID 0000-0002-5077-9345
Zhilun LiDepartment of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, Stockholm, Sweden.
Christopher LambertDivision of Molecular Cell Biology, Institute for Cell- and Neurobiology, Technische Universität Braunschweig, Braunschweig, Germany.
Jessica L Henty-RidillaDepartment of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY, USA.ORCID 0000-0002-7203-8791
Theresia E B StradalDepartment of Cell Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany.ORCID 0000-0002-0352-9474
Roger KarlssonDepartment of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, Stockholm, Sweden.ORCID 0000-0001-9310-3233
Peter BielingDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID 0000-0002-7458-4358
Jan FaixInstitute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany.ORCID 0000-0003-1803-9192
Martin FalckeMax Delbrück Center for Molecular Medicine in the Helmholtz Association, Berlin, Germany. martin.falcke@mdc-berlin.de.ORCID 0000-0001-7137-1114
Klemens RottnerDivision of Molecular Cell Biology, Institute for Cell- and Neurobiology, Technische Universität Braunschweig, Braunschweig, Germany. k.rottner@tu-braunschweig.de.ORCID 0000-0003-4244-4198

Funding

Mechanisms of coordinated actin and microtubule dynamicsR35GM133485 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI Jessica L. Ridilla · 2019 to 2026
$3.3M
Deutsche Forschungsgemeinschaft (German Research Foundation) 2414/8-1Deutsche Forschungsgemeinschaft (German Research Foundation) BI 1998/2-1Deutsche Forschungsgemeinschaft (German Research Foundation) Fa330/12-3Deutsche Forschungsgemeinschaft (German Research Foundation) Fa350/19-1Deutsche Forschungsgemeinschaft (German Research Foundation) RO 2414/12-1NIGMS NIH HHS R35 GM133485U.S. Department of Health & Human Services | National Institutes of Health (NIH) GM133485
6 · The paper itself

Abstract

Cell migration frequently employs protrusions termed lamellipodia, constituting the prime model system for generation of branched actin filament networks. Here we utilize genome editing to explore the functional connections between the actin monomer-binding protein profilin (Pfn), the filament nucleating Arp2/3 complex, its co-factor heterodimeric capping protein (CP) and Ena/VASP family polymerases in lamellipodial actin assembly. We show that Pfn counters Ena/VASP but promotes Arp2/3 complex activity, while Ena/VASP and CP mutually antagonize each other. While Pfn promotes Arp2/3 complex activity irrespective of Ena/VASP, sensitivity of CP to Pfn removal vanishes in the absence of Ena/VASP. Our findings establish Pfn as master regulator of Arp2/3 complex-dependent actin network formation, differentially regulating VASP and its antagonizer CP. Mathematical modeling of our data suggest Ena/VASP and CP to compete for recruitment to lamellipodial edges. Our work provides critical insights into the molecular logic of branched actin network assembly in protrusion and force generation.

Indexed as

Actin Capping ProteinsCell Adhesion MoleculesMicrofilament ProteinsPhosphoproteinsProfilinsPseudopodiaActin CytoskeletonActin-Related Protein 2-3 ComplexActinsAnimalsCell MovementDNA-Binding ProteinsHumansVasodilator-Stimulated PhosphoproteinActin Capping ProteinsActin-Related Protein 2-3 ComplexActinsCell Adhesion MoleculesDNA-Binding ProteinsENA-VASP proteinsMicrofilament ProteinsPhosphoproteinsProfilins

Identifiers

PMID42749745
PMCPMC13582894

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.