Evidence map›Paper›PMID 22735530›Full record

ArticleBiophysical journal2012

Calcium regulation of myosin-I tension sensing.

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

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

22 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Switch-2 determines MgFrontiers in physiology · 2024
    Article
  5. Article
  6. Actomyosin Complex.Sub-cellular biochemistry · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. N-terminal splicing extensions of the humanThe Journal of biological chemistry · 2017
    Article
  13. Article
  14. Review
  15. Article
  16. Mechanochemical tuning of myosin-I by the N-terminal region.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  17. Article
  18. A vertebrate myosin-I structure reveals unique insights into myosin mechanochemical tuning.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  19. Review
  20. Review
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.

John H LewisPennsylvania Muscle Institute and Department of Physiology, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, Pennsylvania, USA.
Michael J Greenberg
Joseph M Laakso
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 GM097889NIGMS NIH HHS P01 GM087253
6 · The paper itself

Abstract

Myo1b is a myosin that is exquisitely sensitive to tension. Its actin-attachment lifetime increases > 50-fold when its working stroke is opposed by 1 pN of force. The long attachment lifetime of myo1b under load raises the question: how are actin attachments that last >50 s in the presence of force regulated? Like most myosins, forces are transmitted to the myo1b motor through a light-chain binding domain that is structurally stabilized by calmodulin, a calcium-binding protein. Thus, we examined the effect of calcium on myo1b motility using ensemble and single-molecule techniques. Calcium accelerates key biochemical transitions on the ATPase pathway, decreases the working-stroke displacement, and greatly reduces the ability of myo1b to sense tension. Thus, calcium provides an effective mechanism for inhibiting motility and terminating long-duration attachments.

Indexed as

Mechanical PhenomenaActinsAnimalsBiomechanical PhenomenaCalciumMovementMyosin Type IRabbitsActinsCalciumMyosin Type I

Identifiers

PMID22735530
PMCPMC3379621
OpenAlexW2015017468

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.