Evidence map›Paper›PMID 25806963›Full record

ArticlePloS one2015

Force dependent biotinylation of myosin IIA by α-catenin tagged with a promiscuous biotin ligase.

Shuji Ueda, Alexandra M Blee, Katherine G Macway, Derrick J Renner, Soichiro Yamada

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Review
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  7. Article
  8. E-cadherin and LGN align epithelial cell divisions with tissue tension independently of cell shape.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  9. Review
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  13. Review
  14. Identifying Protein-Protein Associations at the Nuclear Envelope with BioID.Methods in molecular biology (Clifton, N.J.) · 2016
    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

5 authors at 2 institutions in 2 countries.

Shuji UedaDepartment of Agrobioscience, Graduate School of Agricultural Science, Kobe University, Kobe, Japan.
Alexandra M BleeDepartment of Biomedical Engineering, University of California Davis, Davis, CA, 95616, United States of America.
Katherine G MacwayDepartment of Biomedical Engineering, University of California Davis, Davis, CA, 95616, United States of America.
Derrick J RennerDepartment of Biomedical Engineering, University of California Davis, Davis, CA, 95616, United States of America.
Soichiro YamadaDepartment of Biomedical Engineering, University of California Davis, Davis, CA, 95616, United States of America.
University of California, Davis · USKobe University · JP

Funding

Cell adhesion mediated self-recognitionR01GM094798 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI YAMADA, SOICHIRO · 2010 to 2013
$1.1M
NIGMS NIH HHS GM094798NIGMS NIH HHS R01 GM094798
6 · The paper itself

Abstract

Tissues and organs undergo constant physical perturbations and individual cells must respond to mechanical forces to maintain tissue integrity. However, molecular interactions underlying mechano-transduction are not fully defined at cell-cell junctions. This is in part due to weak and transient interactions that are likely prevalent in force-induced protein complexes. Using in situ proximal biotinylation by the promiscuous biotin ligase BirA tagged to α-catenin and a substrate stretch cell chamber, we sought to identify force-dependent molecular interactions surrounding α-catenin, an actin regulator at the sites of cadherin mediated cell-cell adhesion. While E-cadherin, β-catenin, vinculin and actin localize with α-catenin at cell-cell contacts in immuno-fluorescent staining, only β-catenin and plakoglobin were biotinylated, suggesting that this proximal biotinylation is limited to the molecules that are in the immediate vicinity of α-catenin. In mechanically stretched samples, increased biotinylation of non-muscle myosin IIA, but not myosin IIB, suggests close spatial proximity between α-catenin and myosin IIA during substrate stretching. This force-induced biotinylation diminished as myosin II activity was inhibited by blebbistatin. Taken together, this promising technique enables us to identify force sensitive complexes that may be essential for mechano-responses in force bearing cell adhesion.

Indexed as

Actinsalpha CateninAnimalsbeta CateninBiotinBiotinylationCarbon-Nitrogen LigasesDogsEscherichia coli Proteinsgamma CateninMadin Darby Canine Kidney CellsMicroscopy, ConfocalMutagenesis, Site-DirectedNonmuscle Myosin Type IIARepressor ProteinsStress, MechanicalActinsalpha Cateninbeta CateninBiotinbirA protein, E coliCarbon-Nitrogen LigasesEscherichia coli Proteinsgamma CateninNonmuscle Myosin Type IIARepressor Proteins

Identifiers

PMID25806963
PMCPMC4373798
OpenAlexW2091216980

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.