Evidence map›Paper›PMID 22718345›Full record

ArticleJournal of cell science2012

Cadherin-dependent mechanotransduction depends on ligand identity but not affinity.

Hamid Tabdili, Matthew Langer, Quanming Shi, Yeh-Chuin Poh, Ning Wang, Deborah Leckband

Abstract read
In one paragraph

Article in Journal of cell science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

38 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Mechanical disruption of E-cadherin complexes with epidermal growth factor receptor actuates growth factor-dependent signaling.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. Cadherin cis and trans interactions are mutually cooperative.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Characterization of the strain-rate-dependent mechanical response of single cell-cell junctions.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Article
  12. Cadherin Extracellular Domain Clustering in the Absence ofThe journal of physical chemistry letters · 2019
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  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

6 authors at 1 institution in 1 country.

Hamid TabdiliDepartment of Chemical and Biomolecular Engineering, University of Illinois, Urbana, IL 61801, USA.
Matthew Langer
Quanming Shi
Yeh-Chuin Poh
Ning Wang
Deborah Leckband
University of Illinois Urbana-Champaign · US

Funding

Bioengineering to map stress propagation in cytoskeletonR01GM072744 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI Ning Wang · 2005 to 2026
$7.6M
NIGMS NIH HHS GM072744NIGMS NIH HHS R01 GM072744
6 · The paper itself

Abstract

This study investigates the relationship between classical cadherin binding affinities and mechanotransduction through cadherin-mediated adhesions. The mechanical properties of cadherin-dependent intercellular junctions are generally attributed to differences in the binding affinities of classical cadherin subtypes that contribute to cohesive energies between cells. However, cell mechanics and mechanotransduction may also regulate intercellular contacts. We used micropipette measurements to quantify the two-dimensional affinities of cadherins at the cell surface, and two complementary mechanical measurements to assess ligand-dependent mechanotransduction through cadherin adhesions. At the cell surface, the classical cadherins investigated in this study form both homophilic and heterophilic bonds with two-dimensional affinities that differ by less than threefold. In contrast, mechanotransduction through cadherin adhesions is strongly ligand dependent such that homophilic, but not heterophilic ligation mediates mechanotransduction, independent of the cadherin binding affinity. These findings suggest that ligand-selective mechanotransduction may supersede differences in cadherin binding affinities in regulating intercellular contacts.

Indexed as

Mechanotransduction, CellularActinsAnimalsBiomechanical PhenomenaCadherinsCell AdhesionCell CountCell LineHumansKineticsLigandsNonlinear DynamicsPaxillinProtein BindingProtein Structure, TertiaryActinsCadherinsLigandsPaxillin

Identifiers

PMID22718345
PMCPMC3516441
OpenAlexW1984114593

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.