Evidence map›Paper›PMID 34836783›Full record

ReviewTrends in cell biology2022

Nucleation, stabilization, and disassembly of branched actin networks.

Alexis M Gautreau, Fred E Fregoso, Gleb Simanov, Roberto Dominguez

Open access · bronzeAbstract readReview
In one paragraph

Review in Trends in cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
11.1field-weighted citation impact, top 1% 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

89 citing papers in PubMed, 147 citations in OpenAlex.

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  17. Arp2/3-mediated bidirectional actin assembly by SPIN90 dimers.Nature structural & molecular biology · 2025
    Article
  18. Article
  19. Article
  20. Article

29 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

4 authors at 3 institutions in 2 countries.

Alexis M GautreauLaboratoire de Biologie Structurale de la Cellule, CNRS, École Polytechnique, Institut Polytechnique de Paris, 91128 Palaiseau, France. Electronic address: alexis.gautreau@polytechnique.edu.
Fred E FregosoDepartment of Physiology and Biochemistry and Molecular Biophysics Graduate Group, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
Gleb SimanovLaboratoire de Biologie Structurale de la Cellule, CNRS, École Polytechnique, Institut Polytechnique de Paris, 91128 Palaiseau, France.
Roberto DominguezDepartment of Physiology and Biochemistry and Molecular Biophysics Graduate Group, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. Electronic address: droberto@pennmedicine.upenn.edu.
University of Pennsylvania · USCentre National de la Recherche Scientifique · FRÉcole Polytechnique · FR

Funding

Integrative mechanisms of organelle dynamics from the atomic-to-cellular levelRM1GM136511 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DOMINGUEZ, ROBERTO, HOLZBAUR, ERIKA L · 2020 to 2024
$7.4M
Structural-Functional Basis of Actin Cytoskeleton DynamicsR01GM073791 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DOMINGUEZ, ROBERTO · 2005 to 2025
$7.0M
Structural biology and molecular biophysics training programT32GM132039 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Ben E. Black, Elizabeth Rhoades · 2019 to 2026
$3.3M
NIGMS NIH HHS R01 GM073791NIGMS NIH HHS RM1 GM136511NIGMS NIH HHS T32 GM132039
6 · The paper itself

Abstract

Arp2/3 complex is an actin filament nucleation and branching machinery conserved in all eukaryotes from yeast to human. Arp2/3 complex branched networks generate pushing forces that drive cellular processes ranging from membrane remodeling to cell and organelle motility. Several molecules regulate these processes by directly inhibiting or activating Arp2/3 complex and by stabilizing or disassembling branched networks. Here, we review recent advances in our understanding of Arp2/3 complex regulation, including high-resolution cryoelectron microscopy (cryo-EM) structures that illuminate the mechanisms of Arp2/3 complex activation and branch formation, and novel cellular pathways of branch formation, stabilization, and debranching. We also identify major gaps in our understanding of Arp2/3 complex inhibition and branch stabilization and disassembly.

Indexed as

Actin CytoskeletonActinsActin-Related Protein 2-3 ComplexCryoelectron MicroscopyHumansProtein BindingSaccharomyces cerevisiaeActin-Related Protein 2-3 ComplexActinsArp2/3 complexbranched network stabilization and disassemblyinhibitorsmechanosensationnucleation-promoting factors

Identifiers

PMID34836783
PMCPMC9018471
OpenAlexW3216754170

What OpenQuestion holds

Textmetadata
LicenceTDM
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.