Evidence map›Paper›PMID 27956608›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Self-organization of actin networks by a monomeric myosin.

Dario Saczko-Brack, Ewa Warchol, Benoit Rogez, Markus Kröss, Sarah M Heissler, James R Sellers, Christopher Batters, Claudia Veigel

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Arrested in Glass: Actin within Sophisticated Architectures of Biosilica in Sponges.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Article
  10. Trop-2, NaOncogene · 2022
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. 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

8 authors.

Dario Saczko-BrackDepartment of Cellular Physiology, Ludwig-Maximilians-Universität München, 80336 Munich, Germany.
Ewa WarcholDepartment of Cellular Physiology, Ludwig-Maximilians-Universität München, 80336 Munich, Germany.
Benoit RogezDepartment of Cellular Physiology, Ludwig-Maximilians-Universität München, 80336 Munich, Germany.
Markus KrössDepartment of Cellular Physiology, Ludwig-Maximilians-Universität München, 80336 Munich, Germany.
Sarah M HeisslerLaboratory of Molecular Physiology, National Heart, Lung and Blood Institute, NIH, Bethesda, MD 20892.
James R SellersLaboratory of Molecular Physiology, National Heart, Lung and Blood Institute, NIH, Bethesda, MD 20892.
Christopher BattersDepartment of Cellular Physiology, Ludwig-Maximilians-Universität München, 80336 Munich, Germany; claudia.veigel@med.uni-muenchen.de chris.batters@med.uni-muenchen.de.
Claudia VeigelDepartment of Cellular Physiology, Ludwig-Maximilians-Universität München, 80336 Munich, Germany; claudia.veigel@med.uni-muenchen.de chris.batters@med.uni-muenchen.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The organization of actomyosin networks lies at the center of many types of cellular motility, including cell polarization and collective cell migration during development and morphogenesis. Myosin-IXa is critically involved in these processes. Using total internal reflection fluorescence microscopy, we resolved actin bundles assembled by myosin-IXa. Electron microscopic data revealed that the bundles consisted of highly ordered lattices with parallel actin polarity. The myosin-IXa motor domains aligned across the network, forming cross-links at a repeat distance of precisely 36 nm, matching the helical repeat of actin. Single-particle image processing resolved three distinct conformations of myosin-IXa in the absence of nucleotide. Using cross-correlation of a modeled actomyosin crystal structure, we identified sites of additional mass, which can only be accounted for by the large insert in loop 2 exclusively found in the motor domain of class IX myosins. We show that the large insert in loop 2 binds calmodulin and creates two coordinated actin-binding sites that constrain the actomyosin interactions generating the actin lattices. The actin lattices introduce orientated tracks at specific sites in the cell, which might install platforms allowing Rho-GTPase-activating protein (RhoGAP) activity to be focused at a definite locus. In addition, the lattices might introduce a myosin-related, force-sensing mechanism into the cytoskeleton in cell polarization and collective cell migration.

Indexed as

Actin CytoskeletonActinsActomyosinAdenosine TriphosphatasesAdenosine TriphosphateCalmodulinCell MovementGTPase-Activating ProteinsHumansKineticsMicroscopy, ElectronMicrotubulesMolecular Dynamics SimulationMyosinsProtein BindingProtein ConformationActinsActomyosinAdenosine TriphosphatasesAdenosine TriphosphateCalmodulinGTPase-Activating ProteinsMYO9A protein, humanMyosinsactin networkelectron microscopyunconventional myosin

Identifiers

PMID27956608
PMCPMC5206537

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.