Evidence map›Paper›PMID 16571671›Full record

ArticleMolecular biology of the cell2006

Myosin VI stabilizes an actin network during Drosophila spermatid individualization.

Tatsuhiko Noguchi, Marta Lenartowska, Kathryn G Miller

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

56 citing papers in PubMed, 91 citations in OpenAlex.

  1. Review
  2. Myosin VI is expressed in developing ovarian follicles inFrontiers in cell and developmental biology · 2025
    Article
  3. Article
  4. Article
  5. Myosin VI powers self-organization of branched contractile actin network.Biochemical and biophysical research communications · 2024
    Article
  6. Article
  7. Article
  8. Diverse functions of myosin VI in spermiogenesis.Histochemistry and cell biology · 2021
    Review
  9. Article
  10. Article
  11. Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019
    Review
  12. Article
  13. Myosin 1b is an actin depolymerase.Nature communications · 2019
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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 2 institutions in 2 countries.

Tatsuhiko NoguchiDepartment of Biology, Washington University in St. Louis, St. Louis, MO 63130, USA. noguchi@biology2.wustl.edu
Marta Lenartowska
Kathryn G Miller
Washington University in St. Louis · USNicolaus Copernicus University · PL

Funding

Myosin VI in Intracellular Transport/LocalizationR01GM060494 · NIGMS · WASHINGTON UNIVERSITY · PI MILLER, KATHRYN G · 2000 to 2011
$4.1M
NIGMS NIH HHS GM-60494NIGMS NIH HHS R01 GM060494
6 · The paper itself

Abstract

Here, we demonstrate a new function of myosin VI using observations of Drosophila spermatid individualization in vivo. We find that myosin VI stabilizes a branched actin network in actin structures (cones) that mediate the separation of the syncytial spermatids. In a myosin VI mutant, the cones do not accumulate F-actin during cone movement, whereas overexpression of myosin VI leads to bigger cones with more F-actin. Myosin subfragment 1-fragment decoration demonstrated that the actin cone is made up of two regions: a dense meshwork at the front and parallel bundles at the rear. The majority of the actin filaments were oriented with their pointed ends facing in the direction of cone movement. Our data also demonstrate that myosin VI binds to the cone front using its motor domain. Fluorescence recovery after photobleach experiments using green fluorescent protein-myosin VI revealed that myosin VI remains bound to F-actin for minutes, suggesting its role is tethering, rather than transporting cargo. We hypothesize that myosin VI protects the actin cone structure either by cross-linking actin filaments or anchoring regulatory molecules at the cone front. These observations uncover a novel mechanism mediated by myosin VI for stabilizing long-lived actin structures in cells.

Indexed as

ActinsAnimalsCell MovementDrosophilaDrosophila ProteinsGenes, ReporterMaleMicroscopy, ElectronMyosin Heavy ChainsRecombinant Fusion ProteinsSpermatidsTestisActinsDrosophila ProteinsMyosin Heavy Chainsmyosin VIRecombinant Fusion Proteins

Identifiers

PMID16571671
PMCPMC1474903
OpenAlexW2099771391

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.