Evidence map›Paper›PMID 18931255›Full record

ArticleBiophysical journal2008

Twirling of actin by myosins II and V observed via polarized TIRF in a modified gliding assay.

John F Beausang, Harry W Schroeder, Philip C Nelson, Yale E Goldman

Abstract read
In one paragraph

Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
–field-weighted citation impact
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

40 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Twist response of actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Article
  11. CYK-1/Formin activation in cortical RhoA signaling centers promotes organismal left-right symmetry breaking.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Working stroke of the kinesin-14, ncd, comprises two substeps of different direction.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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

4 authors.

John F BeausangDepartment of Physics and Astronomy, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Harry W Schroeder
Philip C Nelson
Yale E Goldman

Funding

Regulation and Mechano-Chemistry of Myosins V and VIP01AR051174 · NIAMS · UNIVERSITY OF PENNSYLVANIA · PI HOLZBAUR, ERIKA L · 2004 to 2008
$7.1M
STRUCTURAL DYNAMICS OF ACTOMYOSIN MOTILITYR01AR026846 · NIAMS · UNIVERSITY OF PENNSYLVANIA · PI GOLDMAN, YALE E · 1986 to 2007
$2.3M
NIAMS NIH HHS P01 AR051174NIAMS NIH HHS P01AR051174-05NIAMS NIH HHS R01 AR026846NIAMS NIH HHS R01-AR026846
6 · The paper itself

Abstract

The force generated between actin and myosin acts predominantly along the direction of the actin filament, resulting in relative sliding of the thick and thin filaments in muscle or transport of myosin cargos along actin tracks. Previous studies have also detected lateral forces or torques that are generated between actin and myosin, but the origin and biological role of these sideways forces is not known. Here we adapt an actin gliding filament assay to measure the rotation of an actin filament about its axis ("twirling") as it is translocated by myosin. We quantify the rotation by determining the orientation of sparsely incorporated rhodamine-labeled actin monomers, using polarized total internal reflection microscopy. To determine the handedness of the filament rotation, linear incident polarizations in between the standard s- and p-polarizations were generated, decreasing the ambiguity of our probe orientation measurement fourfold. We found that whole myosin II and myosin V both twirl actin with a relatively long (approximately 1 microm), left-handed pitch that is insensitive to myosin concentration, filament length, and filament velocity.

Indexed as

MovementActin CytoskeletonActinsAnimalsBiomechanical PhenomenaCattleMicroscopy, FluorescenceMyosin Type IIMyosin Type VRabbitsActinsMyosin Type IIMyosin Type V

Identifiers

PMID18931255
PMCPMC2599829

What OpenQuestion holds

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Registered trials

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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.