Evidence map›Paper›PMID 31181075›Full record

ArticlePLoS biology2019

Sizes of actin networks sharing a common environment are determined by the relative rates of assembly.

Adrien Antkowiak, Audrey Guillotin, Micaela Boiero Sanders, Jessica Colombo, Renaud Vincentelli, Alphée Michelot

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Biochemical and mechanical regulation of actin dynamics.Nature reviews. Molecular cell biology · 2022
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review
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 at 1 institution in 1 country.

Adrien AntkowiakAix Marseille Univ, CNRS, IBDM, Turing Centre for Living Systems, Marseille, France.ORCID 0000-0002-3711-5544
Audrey GuillotinAix Marseille Univ, CNRS, IBDM, Turing Centre for Living Systems, Marseille, France.
Micaela Boiero SandersAix Marseille Univ, CNRS, IBDM, Turing Centre for Living Systems, Marseille, France.
Jessica ColomboAix Marseille Univ, CNRS, IBDM, Turing Centre for Living Systems, Marseille, France.ORCID 0000-0002-3462-6373
Renaud VincentelliUnité Mixte de Recherche (UMR) 7257, Centre National de la Recherche Scientifique (CNRS) Aix-Marseille Université, Architecture et Fonction des Macromolécules Biologiques (AFMB), Marseille, France.
Alphée MichelotAix Marseille Univ, CNRS, IBDM, Turing Centre for Living Systems, Marseille, France.ORCID 0000-0003-2023-8094
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Within the cytoplasm of a single cell, several actin networks can coexist with distinct sizes, geometries, and protein compositions. These actin networks assemble in competition for a limited pool of proteins present in a common cellular environment. To predict how two distinct networks of actin filaments control this balance, the simultaneous assembly of actin-related protein 2/3 (Arp2/3)-branched networks and formin-linear networks of actin filaments around polystyrene microbeads was investigated with a range of actin accessory proteins (profilin, capping protein, actin-depolymerizing factor [ADF]/cofilin, and tropomyosin). Accessory proteins generally affected actin assembly rates for the distinct networks differently. These effects at the scale of individual actin networks were surprisingly not always correlated with corresponding loss-of-function phenotypes in cells. However, our observations agreed with a global interpretation, which compared relative actin assembly rates of individual actin networks. This work supports a general model in which the size of distinct actin networks is determined by their relative capacity to assemble in a common and competing environment.

Indexed as

Actin CytoskeletonActin Depolymerizing FactorsActin-Related Protein 2-3 ComplexActinsAnimalsHumansKineticsMicrofilament ProteinsProfilinsProtein Interaction MapsTropomyosinActin Depolymerizing FactorsActin-Related Protein 2-3 ComplexActinsMicrofilament ProteinsProfilinsTropomyosin

Identifiers

PMID31181075
PMCPMC6586355
OpenAlexW2949875351

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.