Evidence map›Paper›PMID 18599791›Full record

ArticleScience (New York, N.Y.)2008

Myosin I can act as a molecular force sensor.

Joseph M Laakso, John H Lewis, Henry Shuman, E Michael Ostap

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 147 papers.

0numbers the graph read from it
0cells of the map it votes in
147citing papers in PubMed
10.5field-weighted citation impact, top 1% 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

147 citing papers in PubMed, 254 citations in OpenAlex.

  1. Article
  2. Article
  3. A local solution to local load: Myo1E as a tension-responsive actuator in clathrin-mediated endocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Motor-Assisted Co-Migration of Intracellular Organelles and Microtubules as a Mechanism for Directed Cargo Transport.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Coupling between the lever arm and active site via an N-terminal extension tunes force sensitivity in the myosin-1 family.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

87 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Joseph M LaaksoPennsylvania Muscle Institute and Department of Physiology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.
John H Lewis
Henry Shuman
E Michael Ostap
University of Pennsylvania · US

Funding

Regulation and Mechano-Chemistry of Myosins V and VIP01AR051174 · NIAMS · UNIVERSITY OF PENNSYLVANIA · PI HOLZBAUR, ERIKA L · 2004 to 2008
$7.1M
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
NIAMS NIH HHS AR051174NIAMS NIH HHS P01 AR051174NIGMS NIH HHS GM057247NIGMS NIH HHS R01 GM057247NIGMS NIH HHS R37 GM057247
6 · The paper itself

Abstract

The ability to sense molecular tension is crucial for a wide array of cellular processes, including the detection of auditory stimuli, control of cell shape, and internalization and transport of membranes. We show that myosin I, a motor protein that has been implicated in powering key steps in these processes, dramatically alters its motile properties in response to tension. We measured the displacement generated by single myosin I molecules, and we determined the actin-attachment kinetics with varying tensions using an optical trap. The rate of myosin I detachment from actin decreases >75-fold under tension of 2 piconewtons or less, resulting in myosin I transitioning from a low (<0.2) to a high (>0.9) duty-ratio motor. This impressive tension sensitivity supports a role for myosin I as a molecular force sensor.

Indexed as

ActinsActomyosinAdenosine DiphosphateAdenosine TriphosphateAmino Acid MotifsAnimalsBiophysical PhenomenaBiophysicsKineticsLikelihood FunctionsModels, BiologicalMolecular Motor ProteinsMonte Carlo MethodMyosin Type IOptical TweezersProtein Structure, TertiaryActinsActomyosinAdenosine DiphosphateAdenosine TriphosphateMolecular Motor ProteinsMyosin Type I

Identifiers

PMID18599791
PMCPMC2493443
OpenAlexW2069314092

What OpenQuestion holds

Textmetadata
LicenceTDM
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.