Evidence map›Paper›PMID 29057977›Full record

ArticleScientific reports2017

Myosin X is recruited to nascent focal adhesions at the leading edge and induces multi-cycle filopodial elongation.

Kangmin He, Tsuyoshi Sakai, Yoshikazu Tsukasaki, Tomonobu M Watanabe, Mitsuo Ikebe

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.3field-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

32 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Modulation of Filopodial Myosin Function.bioRxiv : the preprint server for biology · 2025
    Article
  3. The filopodial myosin DdMyo7 is a slow, calcium-regulated motor.The Journal of biological chemistry · 2025
    Article
  4. Article
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  8. Article
  9. Article
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  13. Article
  14. Lysyl hydroxylase 2 deficiency promotes filopodia formation and fibroblast migration.Biochemical and biophysical research communications · 2022
    Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Functional Role of Class III Myosins in Hair Cells.Frontiers in cell and developmental biology · 2021
    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 4 institutions in 3 countries.

Kangmin HeInstitute of Vascular Medicine, Peking University Third Hospital and Academy for Advanced Interdisciplinary Studies, Peking University, Key Laboratory of Cardiovascular Molecular Biology and Regulatory Peptides, Ministry of Health, Key Laboratory of Molecular Cardiovascular Sciences, Ministry of Education and Beijing Key Laboratory of Cardiovascular Receptors Research, Beijing, 100191, China.
Tsuyoshi SakaiDepartment of Cellular and Molecular Biology, University of Texas Health Science Center at Tyler, Tyler, TX75708, USA.
Yoshikazu TsukasakiDepartment of Cellular and Molecular Biology, University of Texas Health Science Center at Tyler, Tyler, TX75708, USA.
Tomonobu M WatanabeGraduate School of Frontier Biosciences, Osaka University, Osaka, 5650871, Japan. tomowatanabe@riken.jp.
Mitsuo IkebeDepartment of Cellular and Molecular Biology, University of Texas Health Science Center at Tyler, Tyler, TX75708, USA. mitsuo.Ikebe@uthct.edu.
The University of Texas Health Science Center at Tyler · USOsaka University · JPPeking University Third Hospital · CNQuantitative BioSciences · US

Funding

Regulation of Mammalian Class VI MyosinR01AR048526 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IKEBE, MITSUO · 2003 to 2007
$1.8M
Function of Small G-Protein Binding MyosinR01AR048898 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IKEBE, MITSUO · 2003 to 2007
$1.8M
Motor Function and Regulation of Myosin VIIR01DC006103 · NIDCD · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IKEBE, MITSUO · 2003 to 2007
$1.5M
NIAMS NIH HHS R01 AR048526NIAMS NIH HHS R01 AR048898NIDCD NIH HHS R01 DC006103
6 · The paper itself

Abstract

Filopodia protrude from the leading edge of cells and play important roles in cell motility. Here we report the mechanism of myosin X (encoded by Myo10)-induced multi-cycle filopodia extension. We found that actin, Arp2/3, vinculin and integrin-β first accumulated at the cell's leading edge. Myosin X was then gathered at these sites, gradually clustered by lateral movement, and subsequently initiated filopodia formation. During filopodia extension, we found the translocation of Arp2/3 and integrin-β along filopodia. Arp2/3 and integrin-β then became localized at the tip of filopodia, from where myosin X initiated the second extension of filopodia with a change in extension direction, thus producing long filopodia. Elimination of integrin-β, Arp2/3 and vinculin by siRNA significantly attenuated the myosin-X-induced long filopodia formation. We propose the following mechanism. Myosin X accumulates at nascent focal adhesions at the cell's leading edge, where myosin X promotes actin convergence to create the base of filopodia. Then myosin X moves to the filopodia tip and attracts integrin-β and Arp2/3 for further actin nucleation. The tip-located myosin X then initiates the second cycle of filopodia elongation to produce the long filopodia.

Indexed as

ActinsAnimalsCattleCell MovementChlorocebus aethiopsCOS CellsFocal AdhesionsHumansIntegrin beta ChainsMyosinsPseudopodiaVinculinActinsIntegrin beta ChainsMyosinsVinculin

Identifiers

PMID29057977
PMCPMC5651867
OpenAlexW2765332071

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.