Evidence map›Paper›PMID 8991100›Full record

ArticleThe Journal of cell biology1996

Quantitative analysis of cadherin-catenin-actin reorganization during development of cell-cell adhesion.

C L Adams, W J Nelson, S J Smith

Abstract read
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers.

0numbers the graph read from it
0cells of the map it votes in
107citing papers in PubMed
–field-weighted citation impact
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

107 citing papers in PubMed.

  1. Tight junction structure, assembly and (dys)function.Nature reviews. Molecular cell biology · 2026
    Review
  2. Article
  3. Structural Insights into Ordered Multicomponent Assemblies in Cell Junctions.Advances in experimental medicine and biology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. IRF6 Regulates the Delivery of E-Cadherin to the Plasma Membrane.The Journal of investigative dermatology · 2022
    Article
  11. Integrin αEβ7Cell research · 2021
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review

47 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

3 authors.

C L AdamsDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, California 94305-5426, USA.
W J Nelson
S J Smith

Funding

Topogenesis of NA/K-ATPASE in Polarized Epithelial CellsR37GM035527 · NIGMS · STANFORD UNIVERSITY · PI NELSON, W. JAMES · 2003 to 2012
$7.4M
Topogenesis of Na/K-ATPase in Polarized MDCK Epithelial CellsR01GM035527 · NIGMS · STANFORD UNIVERSITY · PI NELSON, W. JAMES · 1986 to 2015
$3.3M
CELLULAR PHYSIOLOGY OF CORTICAL DEVELOPMENTR01NS028587 · NINDS · STANFORD UNIVERSITY · PI SMITH, STEPHEN J. · 1991 to 2002
$846k
NIGMS NIH HHS GM35527NIMH NIH HHS MH48104NINDS NIH HHS NS28587
6 · The paper itself

Abstract

Epithelial cell-cell adhesion requires interactions between opposing extracellular domains of E-cadherin, and among the cytoplasmic domain of E-cadherin, catenins, and actin cytoskeleton. Little is known about how the cadherin-catenin-actin complex is assembled upon cell-cell contact, or how these complexes initiate and strengthen adhesion. We have used time-lapse differential interference contrast (DIC) imaging to observe the development of cell-cell contacts, and quantitative retrospective immunocytochemistry to measure recruitment of proteins to those contacts. We show that E-cadherin, alpha-catenin, and beta-catenin, but not plakoglobin, coassemble into Triton X-100 insoluble (TX-insoluble) structures at cell-cell contacts with kinetics similar to those for strengthening of E-cadherin-mediated cell adhesion (Angres, B., A. Barth, and W.J. Nelson. 1996. J. Cell Biol. 134:549-557). TX-insoluble E-cadherin, alpha-catenin, and beta-catenin colocalize along cell-cell contacts in spatially discrete micro-domains which we designate "puncta," and the relative amounts of each protein in each punctum increase proportionally. As the length of the contact increases, the number of puncta increases proportionally along the contact and each punctum is associated with a bundle of actin filaments. These results indicate that localized clustering of E-cadherin/catenin complexes into puncta and their association with actin is involved in initiating cell contacts. Subsequently, the spatial ordering of additional puncta along the contact may be involved in zippering membranes together, resulting in rapid strengthening of adhesion.

Indexed as

Trans-ActivatorsActinsalpha CateninAnimalsbeta CateninCadherinsCell AdhesionCell Adhesion MoleculesCell LineCytoskeletal ProteinsDesmoplakinsDogsEpithelial CellsEpitheliumFluorescent Antibody Techniquegamma CateninActinsalpha Cateninbeta CateninCadherinsCell Adhesion MoleculesCytoskeletal ProteinsDesmoplakinsgamma CateninOctoxynolTrans-Activators

Identifiers

PMID8991100
PMCPMC2133977

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.