Evidence map›Paper›PMID 20081229›Full record

ArticleThe Journal of biological chemistry2010

Myosin X regulates sealing zone patterning in osteoclasts through linkage of podosomes and microtubules.

Brooke K McMichael, Richard E Cheney, Beth S Lee

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

34 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Review
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  10. Lack of Myosin X Enhances Osteoclastogenesis and Increases Cell Surface Unc5b in Osteoclast-Lineage Cells.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2019
    Article
  11. Article
  12. Induction of Krüppel-like factor 2 reduces K/BxN serum-induced arthritis.Journal of cellular and molecular medicine · 2019
    Article
  13. Review
  14. Article
  15. The Sealing Zone in Osteoclasts: A Self-Organized Structure on the Bone.International journal of molecular sciences · 2018
    Review
  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 1 country.

Brooke K McMichaelDepartment of Physiology and Cell Biology, The Ohio State University College of Medicine, Columbus, Ohio 43210.
Richard E CheneyDepartment of Cell and Molecular Physiology, University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599.
Beth S LeeDepartment of Physiology and Cell Biology, The Ohio State University College of Medicine, Columbus, Ohio 43210. Electronic address: lee.2076@osu.edu.
The Ohio State University · USUniversity of North Carolina at Chapel Hill · US

Funding

The Platelet-Leukocyte Switch in Vascular DiseaseP01HL080166 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI JACOBSON, KENNETH A · 2006 to 2010
$6.7M
Myosin-X: A Novel Myosin with PH DomainsR01DC003299 · NIDCD · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CHENEY, RICHARD E · 2002 to 2017
$4.4M
TRANSCRIPTIONAL CONTROL OF VACUOLAR H+-ATPASE EXPRESSIONR01DK052131 · NIDDK · WASHINGTON UNIVERSITY · PI LEE, BETH S. · 1997 to 2009
$2.7M
DYNAMICS OF THE ACTIN CYTOSKELETON IN OSTEOCLASTSR01AR051515 · NIAMS · OHIO STATE UNIVERSITY · PI LEE, BETH S. · 2006 to 2009
$1.0M
NHLBI NIH HHS P01 HL080166NIAMS NIH HHS R01 AR051515NIDCD NIH HHS R01 DC003299NIDCD NIH HHS R01 DC03299NIDDK NIH HHS R01 DK052131
6 · The paper itself

Abstract

Osteoclasts use actin-rich attachment structures in place of focal adhesions for adherence to bone and non-bone substrates. On glass, osteoclasts generate podosomes, foot-like processes containing a core of F-actin and regulatory proteins that undergo high turnover. To facilitate bone resorption, osteoclasts generate an actin-rich sealing zone composed of densely packed podosome-like units. Patterning of both podosomes and sealing zones is dependent upon an intact microtubule system. A role for unconventional myosin X (Myo10), which can bind actin, microtubules, and integrins, was examined in osteoclasts. Immunolocalization showed Myo10 to be associated with the outer edges of immature podosome rings and sealing zones, suggesting a possible role in podosome and sealing zone positioning. Further, complexes containing both Myo10 and beta-tubulin were readily precipitated from osteoclasts lysates. RNAi-mediated suppression of Myo10 led to decreased cell and sealing zone perimeter, along with decreased motility and resorptive capacity. Further, siRNA-treated cells could not properly position podosomes following microtubule disruption. Osteoclasts overexpressing dominant negative Myo10 microtubule binding domains (MyTH4) showed a similar phenotype. Conversely, overexpression of full-length Myo10 led to increased formation of podosome belts along with larger sealing zones and enhanced bone resorptive capacity. These studies suggest that Myo10 plays a role in osteoclast attachment and podosome positioning by direct linkage of actin to the microtubule network.

Indexed as

ActinsAnimalsBone ResorptionCell LineCytoskeletonGenes, DominantMiceMicrotubulesMyosinsOsteoclastsPhenotypeProtein Structure, TertiaryRNA InterferenceRNA, MessengerRNA, Small InterferingActinsMyo10 protein, mouseMyosinsRNA, MessengerRNA, Small Interfering

Identifiers

PMID20081229
PMCPMC2843201
OpenAlexW2168525527

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.