Evidence map›Paper›PMID 32365328›Full record

ArticleBiophysical journal2020

Bond Type and Discretization of Nonmuscle Myosin II Are Critical for Simulated Contractile Dynamics.

Daniel B Cortes, Max Gordon, Francois Nédélec, Amy S Maddox

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

15 citing papers in PubMed, 30 citations in OpenAlex.

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  15. Tools for computational analysis of moving boundary problems in cellular mechanobiology.Wiley interdisciplinary reviews. Systems biology and medicine · 2020
    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

4 authors at 2 institutions in 2 countries.

Daniel B CortesDepartment of Biology, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina.
Max GordonDepartment of Biology, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina.
Francois NédélecSainsbury Laboratory, University of Cambridge, Cambridge, United Kingdom.
Amy S MaddoxDepartment of Biology, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina. Electronic address: asm@unc.edu.
University of North Carolina at Chapel Hill · USUniversity of Cambridge · GB

Funding

Super-resolution of the Mechanisms of Cell Shape Change in Cytokinesis - the Zeiss LSM800/AiryscanR01GM102390 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI MADDOX, AMY SHAUB · 2012 to 2020
$2.9M
NIGMS NIH HHS R01 GM102390
6 · The paper itself

Abstract

Molecular motors drive cytoskeletal rearrangements to change cell shape. Myosins are the motors that move, cross-link, and modify the actin cytoskeleton. The primary force generator in contractile actomyosin networks is nonmuscle myosin II (NMMII), a molecular motor that assembles into ensembles that bind, slide, and cross-link actin filaments (F-actin). The multivalence of NMMII ensembles and their multiple roles have confounded the resolution of crucial questions, including how the number of NMMII subunits affects dynamics and what affects the relative contribution of ensembles' cross-linking versus motoring activities. Because biophysical measurements of ensembles are sparse, modeling of actomyosin networks has aided in discovering the complex behaviors of NMMII ensembles. Myosin ensembles have been modeled via several strategies with variable discretization or coarse graining and unbinding dynamics, and although general assumptions that simplify motor ensembles result in global contractile behaviors, it remains unclear which strategies most accurately depict cellular activity. Here, we used an agent-based platform, Cytosim, to implement several models of NMMII ensembles. Comparing the effects of bond type, we found that ensembles of catch-slip and catch motors were the best force generators and binders of filaments. Slip motor ensembles were capable of generating force but unbound frequently, resulting in slower contractile rates of contractile networks. Coarse graining of these ensemble types from two sets of 16 motors on opposite ends of a stiff rod to two binders, each representing 16 motors, reduced force generation, contractility, and the total connectivity of filament networks for all ensemble types. A parallel cluster model, previously used to describe ensemble dynamics via statistical mechanics, allowed better contractility with coarse graining, though connectivity was still markedly reduced for this ensemble type with coarse graining. Together, our results reveal substantial tradeoffs associated with the process of coarse graining NMMII ensembles and highlight the robustness of discretized catch-slip ensembles in modeling actomyosin networks.

Indexed as

ActomyosinMyosin Type IIActin CytoskeletonActinsMuscle ContractionMyosinsActinsActomyosinMyosinsMyosin Type II

Identifiers

PMID32365328
PMCPMC7264813
OpenAlexW3018788015

What OpenQuestion holds

Textmetadata
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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.