Evidence map›Paper›PMID 32354995›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

The role of the Arp2/3 complex in shaping the dynamics and structures of branched actomyosin networks.

James Liman, Carlos Bueno, Yossi Eliaz, Nicholas P Schafer, M Neal Waxham, Peter G Wolynes, Herbert Levine, Margaret S Cheung

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

16 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
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  3. Frustration in physiology and molecular medicine.Molecular aspects of medicine · 2025
    Review
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  11. Article
  12. Understanding cytoskeletal avalanches using mechanical stability analysis.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. A strong nonequilibrium bound for sorting of cross-linkers on growing biopolymers.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Review
  15. Article
  16. 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

8 authors at 3 institutions in 1 country.

James LimanDepartment of Bioengineering, Rice University, Houston, TX 77030.ORCID 0000-0002-5861-9004
Carlos BuenoCenter for Theoretical Biological Physics, Rice University, Houston, TX 77030.ORCID 0000-0001-9494-6128
Yossi EliazCenter for Theoretical Biological Physics, Rice University, Houston, TX 77030.
Nicholas P SchaferCenter for Theoretical Biological Physics, Rice University, Houston, TX 77030.
M Neal WaxhamDepartment of Neurobiology and Anatomy, McGovern Medical School at the University of Texas Health Science Center at Houston, Houston, TX 77030.
Peter G WolynesCenter for Theoretical Biological Physics, Rice University, Houston, TX 77030; pwolynes@rice.edu h.levine@northeastern.edu mscheung@uh.edu.ORCID 0000-0001-7975-9287
Herbert LevineCenter for Theoretical Biological Physics, Rice University, Houston, TX 77030; pwolynes@rice.edu h.levine@northeastern.edu mscheung@uh.edu.
Margaret S CheungDepartment of Bioengineering, Rice University, Houston, TX 77030; pwolynes@rice.edu h.levine@northeastern.edu mscheung@uh.edu.
Center for Theoretical Biological Physics · USNortheastern University · USThe University of Texas Health Science Center at Houston · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Actomyosin networks give cells the ability to move and divide. These networks contract and expand while being driven by active energy-consuming processes such as motor protein walking and actin polymerization. Actin dynamics is also regulated by actin-binding proteins, such as the actin-related protein 2/3 (Arp2/3) complex. This complex generates branched filaments, thereby changing the overall organization of the network. In this work, the spatiotemporal patterns of dynamical actin assembly accompanying the branching-induced reorganization caused by Arp2/3 were studied using a computational model (mechanochemical dynamics of active networks [MEDYAN]); this model simulates actomyosin network dynamics as a result of chemical reactions whose rates are modulated by rapid mechanical equilibration. We show that branched actomyosin networks relax significantly more slowly than do unbranched networks. Also, branched networks undergo rare convulsive movements, "avalanches," that release strain in the network. These avalanches are associated with the more heterogeneous distribution of mechanically linked filaments displayed by branched networks. These far-from-equilibrium events arising from the marginal stability of growing actomyosin networks provide a possible mechanism of the "cytoquakes" recently seen in experiments.

Indexed as

Actin-Related Protein 2-3 ComplexActomyosinAnimalsMolecular Dynamics SimulationActin-Related Protein 2-3 ComplexActomyosinactin reorganizationavalanchemarginal stability

Identifiers

PMID32354995
PMCPMC7245093
OpenAlexW3022732381

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.