Evidence map›Paper›PMID 23589853›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Direct real-time detection of the actin-activated power stroke within the myosin catalytic domain.

Joseph M Muretta, Karl J Petersen, David D Thomas

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

33 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Heart failure drug changes the mechanoenzymology of the cardiac myosin powerstroke.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  20. How Myosin Generates Force on Actin Filaments.Trends in biochemical sciences · 2016
    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

3 authors at 1 institution in 1 country.

Joseph M MurettaDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
Karl J Petersen
David D Thomas
University of Minnesota · US

Funding

TRAINING PROGRAM IN MUSCLE RESEARCHT32AR007612 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI JAMES M ERVASTI, DAWN A LOWE · 2001 to 2026
$11.3M
Structural Dynamics of Muscle ContractionR01AR032961 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID D · 1986 to 2018
$8.0M
Use of specific transcription factors to promote limb regeneration capacityP30AR057220 · NIAMS · UNIVERSITY OF MINNESOTA · PI KARACHUNSKI, PETER ISAAK · 2009 to 2013
$3.0M
MOLECULAR DYNAMICS OF MUSCLE CONTRACTIONR37AR032961 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID DALE · 1994 to 2003
$2.1M
Spectroscopic Probes of Smooth Muscle Functional DynamicsF32AR056191 · NIAMS · UNIVERSITY OF MINNESOTA · PI MURETTA, JOSEPH M. · 2008 to 2010
$145k
NIAMS NIH HHS AR032961NIAMS NIH HHS AR056191NIAMS NIH HHS AR057220NIAMS NIH HHS F32 AR056191NIAMS NIH HHS P30 AR057220NIAMS NIH HHS R01 AR032961NIAMS NIH HHS R37 AR032961NIAMS NIH HHS T32 AR007612
6 · The paper itself

Abstract

We have used transient kinetics, nanosecond time-resolved fluorescence resonance energy transfer (FRET), and kinetics simulations to resolve a structural transition in the Dictyostelium myosin II relay helix during the actin-activated power stroke. The relay helix plays a critical role in force generation in myosin, coupling biochemical changes in the ATPase site with the force-transducing rotation of the myosin light-chain domain. Previous research in the absence of actin showed that ATP binding to myosin induces a dynamic equilibrium between a bent prepower stroke state of the relay helix and a straight postpower stroke state, which dominates in the absence of ATP or when ADP is bound. We now ask whether actin binding reverses this transition and if so, how this reversal is coordinated with actin-activated phosphate release. We labeled a Cys-lite Dictyostelium myosin II motor domain with donor and acceptor probes at two engineered Cys residues designed to detect relay helix bending. We then performed transient time-resolved FRET following stopped-flow mixing of actin with labeled myosin, preincubated with ATP. We determined the kinetics of actin-activated phosphate release, using fluorescent phosphate-binding protein. The results show that actin binding to the myosin.ADP.P complex straightens the relay helix before phosphate dissociation. This actin-activated relay helix straightening is reversible, but phosphate irreversibly dissociates from the postpower stroke state, preventing reversal of the power stroke. Thus, relay helix straightening gates phosphate dissociation, whereas phosphate dissociation provides the thermodynamic driving force underlying force production.

Indexed as

Catalytic DomainComputer SystemsActinsAnimalsBiomechanical PhenomenaCrystallography, X-RayDictyosteliumElectron Spin Resonance SpectroscopyFluorescence Resonance Energy TransferKineticsMyosin Type IIPhosphatesProtein Structure, SecondaryRabbitsTime FactorsActinsMyosin Type IIPhosphates

Identifiers

PMID23589853
PMCPMC3645529
OpenAlexW1973899575

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.