Evidence map›Paper›PMID 27602732›Full record

ArticleBiophysical journal2016

Sustained α-catenin Activation at E-cadherin Junctions in the Absence of Mechanical Force.

Kabir H Biswas, Kevin L Hartman, Ronen Zaidel-Bar, Jay T Groves

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

17 citing papers in PubMed, 44 citations in OpenAlex.

  1. Mimicking Cellular Membranes With Micropatterned Lipid Bilayers.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026
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  4. BRET-based biosensors for SARS-CoV-2 oligonucleotide detection.Frontiers in bioengineering and biotechnology · 2024
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  6. A genetically encoded BRET-based SARS-CoV-2 MCommunications chemistry · 2022
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  9. Intracellular Ionic Strength Sensing Using NanoLuc.International journal of molecular sciences · 2021
    Article
  10. Topography design in model membranes: Where biology meets physics.Experimental biology and medicine (Maywood, N.J.) · 2019
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Supported lipid bilayer platforms to probe cell mechanobiology.Biochimica et biophysica acta. Biomembranes · 2017
    Review
  17. Force Bistability in Adhesion Switch.Biophysical journal · 2016
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Kabir H BiswasMechanobiology Institute, National University of Singapore, Singapore, Singapore. Electronic address: mbikhb@nus.edu.sg.
Kevin L HartmanMechanobiology Institute, National University of Singapore, Singapore, Singapore; Department of Chemistry, University of California, Berkeley, Berkeley, California.
Ronen Zaidel-BarMechanobiology Institute, National University of Singapore, Singapore, Singapore; Department of Biomedical Engineering, National University of Singapore, Singapore, Singapore. Electronic address: zaidelbar@gmail.com.
Jay T GrovesMechanobiology Institute, National University of Singapore, Singapore, Singapore; Department of Chemistry, University of California, Berkeley, Berkeley, California; Department of Biomedical Engineering, National University of Singapore, Singapore, Singapore. Electronic address: jtgroves@lbl.gov.
National University of Singapore · SGUniversity of California, Berkeley · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mechanotransduction at E-cadherin junctions has been postulated to be mediated in part by a force-dependent conformational activation of α-catenin. Activation of α-catenin allows it to interact with vinculin in addition to F-actin, resulting in a strengthening of junctions. Here, using E-cadherin adhesions reconstituted on synthetic, nanopatterned membranes, we show that activation of α-catenin is dependent on E-cadherin clustering, and is sustained in the absence of mechanical force or association with F-actin or vinculin. Adhesions were formed by filopodia-mediated nucleation and micron-scale assembly of E-cadherin clusters, which could be distinguished as either peripheral or central assemblies depending on their relative location at the cell-bilayer adhesion. Whereas F-actin, vinculin, and phosphorylated myosin light chain associated only with the peripheral assemblies, activated α-catenin was present in both peripheral and central assemblies, and persisted in the central assemblies in the absence of actomyosin tension. Impeding filopodia-mediated nucleation and micron-scale assembly of E-cadherin adhesion complexes by confining the movement of bilayer-bound E-cadherin on nanopatterned substrates reduced the levels of activated α-catenin. Taken together, these results indicate that although the initial activation of α-catenin requires micron-scale clustering that may allow the development of mechanical forces, sustained force is not required for maintaining α-catenin in the active state.

Indexed as

Actinsalpha CateninAntigens, CDCadherinsCell AdhesionCell Culture TechniquesCell Line, TumorGreen Fluorescent ProteinsHumansLipid BilayersMechanotransduction, CellularMicroscopy, ConfocalMicroscopy, FluorescenceMyosin Light Chainsrho-Associated KinasesStress, MechanicalActinsalpha CateninAntigens, CDCadherinsCDH1 protein, humanGreen Fluorescent ProteinsLipid BilayersMyosin Light Chainsrho-Associated KinasesVinculin

Identifiers

PMID27602732
PMCPMC5018127
OpenAlexW2512061829

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.