Evidence map›Paper›PMID 25948416›Full record

ReviewCellular and molecular life sciences : CMLS2015

Control of polarized assembly of actin filaments in cell motility.

Marie-France Carlier, Julien Pernier, Pierre Montaville, Shashank Shekhar, Sonja Kühn, Cytoskeleton Dynamics and Motility group

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing 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

49 citing papers in PubMed.

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  13. Unconventional Secretion, Gate to Homeoprotein Intercellular Transfer.Frontiers in cell and developmental biology · 2022
    Review
  14. Article
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  20. Myosin 1b is an actin depolymerase.Nature communications · 2019
    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

6 authors.

Marie-France CarlierInstitut de Biologie Intégrative de la Cellule, CNRS, 91198, Gif-sur Yvette, France, carlier@lebs.cnrs-gif.fr.
Julien Pernier
Pierre Montaville
Shashank Shekhar
Sonja Kühn
Cytoskeleton Dynamics and Motility group

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Actin cytoskeleton remodeling, which drives changes in cell shape and motility, is orchestrated by a coordinated control of polarized assembly of actin filaments. Signal responsive, membrane-bound protein machineries initiate and regulate polarized growth of actin filaments by mediating transient links with their barbed ends, which elongate from polymerizable actin monomers. The barbed end of an actin filament thus stands out as a hotspot of regulation of filament assembly. It is the target of both soluble and membrane-bound agonists as well as antagonists of filament assembly. Here, we review the molecular mechanisms by which various regulators of actin dynamics bind, synergize or compete at filament barbed ends. Two proteins can compete for the barbed end via a mutually exclusive binding scheme. Alternatively, two regulators acting individually at barbed ends may be bound together transiently to terminal actin subunits at barbed ends, leading to the displacement of one by the other. The kinetics of these reactions is a key in understanding how filament length and membrane-filament linkage are controlled. It is also essential for understanding how force is produced to shape membranes by mechano-sensitive, processive barbed end tracking machineries like formins and by WASP-Arp2/3 branched filament arrays. A combination of biochemical and biophysical approaches, including bulk solution assembly measurements using pyrenyl-actin fluorescence, single filament dynamics, single molecule fluorescence imaging and reconstituted self-organized filament assemblies, have provided mechanistic insight into the role of actin polymerization in motile processes.

Indexed as

Models, BiologicalModels, MolecularActin CytoskeletonActin-Related Protein 2-3 ComplexCell MovementCell PolarityMicrofilament ProteinsOptical ImagingProtein BindingProtein ConformationActin-Related Protein 2-3 ComplexMicrofilament Proteins

Identifiers

PMID25948416
PMCPMC4506460

What OpenQuestion holds

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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.