Evidence map›Paper›PMID 30967504›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Myosin Va transport of liposomes in three-dimensional actin networks is modulated by actin filament density, position, and polarity.

Andrew T Lombardo, Shane R Nelson, Guy G Kennedy, Kathleen M Trybus, Sam Walcott, David M Warshaw

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.0field-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

18 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
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  5. Review
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  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Roles and regulation of myosin V interaction with cargo.Advances in biological regulation · 2021
    Review
  14. Article
  15. Article
  16. Article
  17. The role of the Arp2/3 complex in shaping the dynamics and structures of branched actomyosin networks.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. 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 at 2 institutions in 1 country.

Andrew T LombardoDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405.
Shane R NelsonDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405.
Guy G KennedyInstrumentation and Model Facility, University of Vermont, Burlington, VT 05405.
Kathleen M TrybusDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405.ORCID 0000-0002-5583-8500
Sam WalcottDepartment of Mathematics, University of California, Davis, CA 95616.
David M WarshawDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405; David.Warshaw@med.uvm.edu.
University of Vermont · USUniversity of California, Davis · US

Funding

Multidisciplinary Training in Lung BiologyT32HL076122 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI IRVIN, CHARLES G, POYNTER, MATTHEW E · 2004 to 2023
$6.1M
MUTATIONAL STUDIES OF PROCESSIVE MYOSIN MOTORSR01GM078097 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI TRYBUS, KATHLEEN M · 2007 to 2019
$4.8M
Myosin Va Cargo Transport: In Vitro Model SystemsR01GM094229 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI WARSHAW, DAVID M · 2011 to 2020
$2.7M
NHLBI NIH HHS T32 HL076122NIGMS NIH HHS R01 GM078097NIGMS NIH HHS R01 GM094229
6 · The paper itself

Abstract

The cell's dense 3D actin filament network presents numerous challenges to vesicular transport by teams of myosin Va (MyoVa) molecular motors. These teams must navigate their cargo through diverse actin structures ranging from Arp2/3-branched lamellipodial networks to the dense, unbranched cortical networks. To define how actin filament network organization affects MyoVa cargo transport, we created two different 3D actin networks in vitro. One network was comprised of randomly oriented, unbranched actin filaments; the other was comprised of Arp2/3-branched actin filaments, which effectively polarized the network by aligning the actin filament plus-ends. Within both networks, we defined each actin filament's 3D spatial position using superresolution stochastic optical reconstruction microscopy (STORM) and its polarity by observing the movement of single fluorescent reporter MyoVa. We then characterized the 3D trajectories of fluorescent, 350-nm fluid-like liposomes transported by MyoVa teams (∼10 motors) moving within each of the two networks. Compared with the unbranched network, we observed more liposomes with directed and fewer with stationary motion on the Arp2/3-branched network. This suggests that the modes of liposome transport by MyoVa motors are influenced by changes in the local actin filament polarity alignment within the network. This mechanism was supported by an in silico 3D model that provides a broader platform to understand how cellular regulation of the actin cytoskeletal architecture may fine tune MyoVa-based intracellular cargo transport.

Indexed as

ActinsLiposomesMyosinsBiological TransportIntracellular SpaceModels, BiologicalActinsLiposomesMyosinsactinintracellular transportmyosinpolaritysingle molecule

Identifiers

PMID30967504
PMCPMC6486769
OpenAlexW2913127398

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.