Evidence map›Paper›PMID 24591646›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Myosin lever arm directs collective motion on cellular actin network.

Rizal F Hariadi, Mario Cale, Sivaraj Sivaramakrishnan

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
6.6field-weighted citation impact, top 3% 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

28 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The right shoe for the job.Science (New York, N.Y.) · 2022
    Article
  5. Review
  6. Review
  7. Article
  8. Active cargo positioning in antiparallel transport networks.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Patterning protein complexes on DNA nanostructures using a GFP nanobody.Protein science : a publication of the Protein Society · 2016
    Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Rizal F HariadiDepartment of Cell and Developmental Biology, Department of Biophysics, and Department of Biomedical Engineering, University of Michigan, Ann Arbor, MI 48109.
Mario Cale
Sivaraj Sivaramakrishnan
University of Michigan–Ann Arbor · US

Funding

The kinase toolbox: Mapping the spatial and temporal regulation of cell signalingDP2CA186752 · NCI · UNIVERSITY OF MINNESOTA · PI SIVARAMAKRISHNAN, SIVARAJ · 2013 to 2013
$2.3M
NCI NIH HHS 1DP2CA186752-01NCI NIH HHS DP2 CA186752
6 · The paper itself

Abstract

The molecular motor myosin teams up to drive muscle contraction, membrane traffic, and cell division in biological cells. Myosin function in cells emerges from the interaction of multiple motors tethered to a scaffold, with surrounding actin filaments organized into 3D networks. Despite the importance of myosin function, the influence of intermotor interactions on collective motion remains poorly understood. In this study, we used precisely engineered myosin assemblies to examine emergence in collective myosin movement. We report that tethering multiple myosin VI motors, but not myosin V motors, modifies their movement trajectories on keratocyte actin networks. Single myosin V and VI dimers display similar skewed trajectories, albeit in opposite directions, when traversing the keratocyte actin network. In contrast, tethering myosin VI motors, but not myosin V motors, progressively straightens the trajectories with increasing myosin number. Trajectory shape of multimotor scaffolds positively correlates with the stiffness of the myosin lever arm. Swapping the flexible myosin VI lever arm for the relatively rigid myosin V lever increases trajectory skewness, and vice versa. A simplified model of coupled motor movement demonstrates that the differences in flexural rigidity of the two myosin lever arms is sufficient to account for the differences in observed behavior of groups of myosin V and VI motors. In accordance with this model trajectory, shapes for scaffolds containing both myosin V and VI are dominated by the myosin with a stiffer lever arm. Our findings suggest that structural features unique to each myosin type may confer selective advantages in cellular functions.

Indexed as

Models, BiologicalActin CytoskeletonBioengineeringBiomimeticsBiophysicsMolecular Dynamics SimulationMovementMyosinsNanotechnologyMyosinscollective decision-makingDNA nanotechnologymotor proteinssingle molecule biophysicssynthetic biology

Identifiers

PMID24591646
PMCPMC3964131
OpenAlexW1990381237

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.