Evidence map›Paper›PMID 22908250›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Myosin IC generates power over a range of loads via a new tension-sensing mechanism.

Michael J Greenberg, Tianming Lin, Yale E Goldman, Henry Shuman, E Michael Ostap

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
3.8field-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

66 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
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  6. Review
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  10. Article
  11. Switch-2 determines MgFrontiers in physiology · 2024
    Article
  12. Review
  13. Article
  14. Endocytic myosin-1 is a force-insensitive, power-generating motor.bioRxiv : the preprint server for biology · 2023
    Article
  15. Article
  16. Article
  17. Actomyosin Complex.Sub-cellular biochemistry · 2022
    Article
  18. Article
  19. Article
  20. Article

6 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

5 authors at 1 institution in 1 country.

Michael J GreenbergThe Pennsylvania Muscle Institute and Department of Physiology, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA 19104-6085, USA.
Tianming Lin
Yale E Goldman
Henry Shuman
E Michael Ostap
University of Pennsylvania · US

Funding

Role of Myosin-l in Membrane Dynamics and TransportP01GM087253 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI HOLZBAUR, ERIKA L · 2009 to 2018
$15.3M
Training in Muscle Biology and Muscle DiseaseT32AR053461 · NIAMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 2006 to 2025
$4.9M
Regulation of Myosin Ic MechanochemistryF32GM097889 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GREENBERG, MICHAEL J · 2011 to 2012
$101k
NIAMS NIH HHS T32 AR053461NIGMS NIH HHS F32 GM097889NIGMS NIH HHS P01 GM087253
6 · The paper itself

Abstract

Myosin IC (myo1c), a widely expressed motor protein that links the actin cytoskeleton to cell membranes, has been associated with numerous cellular processes, including insulin-stimulated transport of GLUT4, mechanosensation in sensory hair cells, endocytosis, transcription of DNA in the nucleus, exocytosis, and membrane trafficking. The molecular role of myo1c in these processes has not been defined, so to better understand myo1c function, we utilized ensemble kinetic and single-molecule techniques to probe myo1c's biochemical and mechanical properties. Utilizing a myo1c construct containing the motor and regulatory domains, we found the force dependence of the actin-attachment lifetime to have two distinct regimes: a force-independent regime at forces < 1 pN, and a highly force-dependent regime at higher loads. In this force-dependent regime, forces that resist the working stroke increase the actin-attachment lifetime. Unexpectedly, the primary force-sensitive transition is the isomerization that follows ATP binding, not ADP release as in other slow myosins. This force-sensing behavior is unique amongst characterized myosins and clearly demonstrates mechanochemical diversity within the myosin family. Based on these results, we propose that myo1c functions as a slow transporter rather than a tension-sensitive anchor.

Indexed as

ActinsAdenosine DiphosphateAdenosine TriphosphateAnimalsBiomechanical PhenomenaCalmodulinCarrier ProteinsChromatography, LiquidLikelihood FunctionsMiceMuscle TonusMyosin Type IOptical TweezersActinsAdenosine DiphosphateAdenosine TriphosphateCalmodulinCarrier ProteinsMyo1c protein, mouseMyosin Type I

Identifiers

PMID22908250
PMCPMC3443183
OpenAlexW2022378428

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.