Evidence map›Paper›PMID 27156719›Full record

ArticleScientific reports2016

Force Generation by Membrane-Associated Myosin-I.

Serapion Pyrpassopoulos, Göker Arpağ, Elizabeth A Feeser, Henry Shuman, Erkan Tüzel, E Michael Ostap

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Devising a divisome for synthetic cells.Nature reviews. Chemistry · 2026
    Review
  2. Switch-2 determines MgFrontiers in physiology · 2024
    Article
  3. Article
  4. Endocytic myosin-1 is a force-insensitive, power-generating motor.bioRxiv : the preprint server for biology · 2023
    Article
  5. Article
  6. Article
  7. Myosin 1b is an actin depolymerase.Nature communications · 2019
    Article
  8. Article
  9. Article
  10. Intracellular cargo transport by single-headed kinesin motors.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Article
  12. Article
  13. Membrane bending by actin polymerization.Current opinion in cell biology · 2018
    Review
  14. Review
  15. Article
  16. Supported lipid bilayer platforms to probe cell mechanobiology.Biochimica et biophysica acta. Biomembranes · 2017
    Review
  17. Article
  18. Article
  19. 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.

Serapion PyrpassopoulosThe Pennsylvania Muscle Institute and Department of Physiology, Perelman School of Medicine at the University of Pennsylvania, Philadelphia PA 19104-6085, USA.
Göker ArpağDepartment of Physics, Worcester Polytechnic Institute, Worcester MA 01609, USA.
Elizabeth A FeeserThe Pennsylvania Muscle Institute and Department of Physiology, Perelman School of Medicine at the University of Pennsylvania, Philadelphia PA 19104-6085, USA.
Henry ShumanThe Pennsylvania Muscle Institute and Department of Physiology, Perelman School of Medicine at the University of Pennsylvania, Philadelphia PA 19104-6085, USA.
Erkan TüzelDepartment of Physics, Worcester Polytechnic Institute, Worcester MA 01609, USA.
E Michael OstapThe Pennsylvania Muscle Institute and Department of Physiology, Perelman School of Medicine at the University of Pennsylvania, Philadelphia PA 19104-6085, USA.
University of Pennsylvania · USWorcester Polytechnic Institute · US

Funding

Molecular function of Myosin-lR37GM057247 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 2016 to 2025
$5.3M
Molecular function of myosin-IR01GM057247 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 1998 to 2014
$4.4M
NIGMS NIH HHS R01 GM057247
6 · The paper itself

Abstract

Vertebrate myosin-IC (Myo1c) is a type-1 myosin that links cell membranes to the cytoskeleton via its actin-binding motor domain and its phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2)-binding tail domain. While it is known that Myo1c bound to PtdIns(4,5)P2 in fluid-lipid bilayers can propel actin filaments in an unloaded motility assay, its ability to develop forces against external load on actin while bound to fluid bilayers has not been explored. Using optical tweezers, we measured the diffusion coefficient of single membrane-bound Myo1c molecules by force-relaxation experiments, and the ability of ensembles of membrane-bound Myo1c molecules to develop and sustain forces. To interpret our results, we developed a computational model that recapitulates the basic features of our experimental ensemble data and suggests that Myo1c ensembles can generate forces parallel to lipid bilayers, with larger forces achieved when the myosin works away from the plane of the membrane or when anchored to slowly diffusing regions.

Indexed as

Actin CytoskeletonActinsAnimalsBiomechanical PhenomenaCell MembraneComputer SimulationDiffusionLipidsMiceModels, MolecularMyosin Type IOptical TweezersProtein TransportActinsLipidsMyo1c protein, mouseMyosin Type I

Identifiers

PMID27156719
PMCPMC4860596
OpenAlexW2346113605

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.