Evidence map›Paper›PMID 27992406›Full record

ArticleNature cell biology2017

Nanoscale architecture of cadherin-based cell adhesions.

Cristina Bertocchi, Yilin Wang, Andrea Ravasio, Yusuke Hara, Yao Wu, Talgat Sailov, Michelle A Baird, Michael W Davidson, Ronen Zaidel-Bar, Yusuke Toyama and 3 more

Open access · greenAbstract read
In one paragraph

Article in Nature cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
11.6field-weighted citation impact, top 1% 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

93 citing papers in PubMed, 180 citations in OpenAlex.

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  18. Review
  19. Cell-Material Interplay in Focal Adhesion Points.ACS applied materials & interfaces · 2024
    Article
  20. Review

33 more citing papers are in PubMed but not listed here.

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

13 authors at 4 institutions in 3 countries.

Cristina BertocchiMechanobiology Institute, Singapore 117411, Republic of Singapore.
Yilin WangMechanobiology Institute, Singapore 117411, Republic of Singapore.
Andrea RavasioMechanobiology Institute, Singapore 117411, Republic of Singapore.
Yusuke HaraMechanobiology Institute, Singapore 117411, Republic of Singapore.ORCID http://orcid.org/0000-0002-2005-7704
Yao WuMechanobiology Institute, Singapore 117411, Republic of Singapore.
Talgat SailovMechanobiology Institute, Singapore 117411, Republic of Singapore.
Michelle A BairdNational High Magnetic Field Laboratory, The Florida State University, Tallahassee, Florida 32310, USA.
Michael W DavidsonNational High Magnetic Field Laboratory, The Florida State University, Tallahassee, Florida 32310, USA.
Ronen Zaidel-BarMechanobiology Institute, Singapore 117411, Republic of Singapore.
Yusuke ToyamaMechanobiology Institute, Singapore 117411, Republic of Singapore.
Benoit LadouxMechanobiology Institute, Singapore 117411, Republic of Singapore.
Rene-Marc MegeInstitut Jacques Monod, Université Paris Diderot, CNRS UMR 7592, Paris, France.
Pakorn KanchanawongMechanobiology Institute, Singapore 117411, Republic of Singapore.ORCID http://orcid.org/0000-0001-8765-3861
Centre National de la Recherche Scientifique · FRFlorida State University · USNational University of Singapore · SGTemasek Life Sciences Laboratory · SG

Funding

European Research Council 617233
6 · The paper itself

Abstract

Multicellularity in animals requires dynamic maintenance of cell-cell contacts. Intercellularly ligated cadherins recruit numerous proteins to form supramolecular complexes that connect with the actin cytoskeleton and support force transmission. However, the molecular organization within such structures remains unknown. Here we mapped protein organization in cadherin-based adhesions by super-resolution microscopy, revealing a multi-compartment nanoscale architecture, with the plasma-membrane-proximal cadherin-catenin compartment segregated from the actin cytoskeletal compartment, bridged by an interface zone containing vinculin. Vinculin position is determined by α-catenin, and following activation, vinculin can extend ∼30 nm to bridge the cadherin-catenin and actin compartments, while modulating the nanoscale positions of the actin regulators zyxin and VASP. Vinculin conformational activation requires tension and tyrosine phosphorylation, regulated by Abl kinase and PTP1B phosphatase. Such modular architecture provides a structural framework for mechanical and biochemical signal integration by vinculin, which may differentially engage cadherin-catenin complexes with the actomyosin machinery to regulate cell adhesions.

Indexed as

Actin CytoskeletonActinsalpha CateninAnimalsBiomarkersBiomechanical PhenomenaCadherinsCell AdhesionCell MembraneCytoskeletal ProteinsDogsIntercellular JunctionsInterferometryMadin Darby Canine Kidney CellsMiceMicroscopyActinsalpha CateninBiomarkersCadherinsCytoskeletal ProteinsVinculin

Identifiers

PMID27992406
PMCPMC5421576
OpenAlexW2563098669

What OpenQuestion holds

Textmetadata
LicenceTDM
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.