Evidence map›Paper›PMID 34504078›Full record

ArticleNature communications2021

A barbed end interference mechanism reveals how capping protein promotes nucleation in branched actin networks.

Johanna Funk, Felipe Merino, Matthias Schaks, Klemens Rottner, Stefan Raunser, Peter Bieling

Abstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing 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

59 citing papers in PubMed.

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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

6 authors.

Johanna Funk *Department of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Felipe Merino *Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Matthias SchaksDivision of Molecular Cell Biology, Zoological Institute, Technische Universität Braunschweig, Braunschweig, Germany.
Klemens RottnerDivision of Molecular Cell Biology, Zoological Institute, Technische Universität Braunschweig, Braunschweig, Germany.ORCID 0000-0003-4244-4198
Stefan RaunserDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany. Stefan.Raunser@mpi-dortmund.mpg.de.ORCID 0000-0001-9373-3016
Peter BielingDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany. Peter.Bieling@mpi-dortmund.mpg.de.ORCID 0000-0002-7458-4358

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heterodimeric capping protein (CP/CapZ) is an essential factor for the assembly of branched actin networks, which push against cellular membranes to drive a large variety of cellular processes. Aside from terminating filament growth, CP potentiates the nucleation of actin filaments by the Arp2/3 complex in branched actin networks through an unclear mechanism. Here, we combine structural biology with in vitro reconstitution to demonstrate that CP not only terminates filament elongation, but indirectly stimulates the activity of Arp2/3 activating nucleation promoting factors (NPFs) by preventing their association to filament barbed ends. Key to this function is one of CP's C-terminal "tentacle" extensions, which sterically masks the main interaction site of the terminal actin protomer. Deletion of the β tentacle only modestly impairs capping. However, in the context of a growing branched actin network, its removal potently inhibits nucleation promoting factors by tethering them to capped filament ends. End tethering of NPFs prevents their loading with actin monomers required for activation of the Arp2/3 complex and thus strongly inhibits branched network assembly both in cells and reconstituted motility assays. Our results mechanistically explain how CP couples two opposed processes-capping and nucleation-in branched actin network assembly.

Indexed as

Actin Capping ProteinsActin CytoskeletonActin-Related Protein 2-3 ComplexActinsAnimalsBinding SitesCattleCytoskeletonGelsolinGene Expression RegulationHumansIntercellular Signaling Peptides and ProteinsKineticsMelanocytesMelanoma, ExperimentalMiceActin Capping ProteinsActin-Related Protein 2-3 ComplexActinsGelsolinIntercellular Signaling Peptides and ProteinsmyotrophinProfilinsRecombinant ProteinsWASL protein, humanWiskott-Aldrich Syndrome Protein, Neuronal

Identifiers

PMID34504078
PMCPMC8429771

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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.