Evidence map›Paper›PMID 11408571›Full record

ArticleMolecular biology of the cell2001

alpha-catenin-independent recruitment of ZO-1 to nectin-based cell-cell adhesion sites through afadin.

S Yokoyama, K Tachibana, H Nakanishi, Y Yamamoto, K Irie, K Mandai, A Nagafuchi, M Monden, Y Takai

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.7field-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

34 citing papers in PubMed, 92 citations in OpenAlex.

  1. Tight junction structure, assembly and (dys)function.Nature reviews. Molecular cell biology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. The desmosome as a model for lipid raft driven membrane domain organization.Biochimica et biophysica acta. Biomembranes · 2020
    Review
  8. Implications of AMPK in the Formation of Epithelial Tight Junctions.International journal of molecular sciences · 2018
    Review
  9. Review
  10. Afadin Downregulation byFrontiers in microbiology · 2018
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  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

9 authors at 2 institutions in 1 country.

S YokoyamaDepartment of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty of Medicine, Suita 565-0871, Japan.
K Tachibana
H Nakanishi
Y Yamamoto
K Irie
K Mandai
A Nagafuchi
M Monden
Y Takai
The University of Osaka · JPKyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ZO-1 is an actin filament (F-actin)-binding protein that localizes to tight junctions and connects claudin to the actin cytoskeleton in epithelial cells. In nonepithelial cells that have no tight junctions, ZO-1 localizes to adherens junctions (AJs) and may connect cadherin to the actin cytoskeleton indirectly through beta- and alpha-catenins as one of many F-actin-binding proteins. Nectin is an immunoglobulin-like adhesion molecule that localizes to AJs and is associated with the actin cytoskeleton through afadin, an F-actin-binding protein. Ponsin is an afadin- and vinculin-binding protein that also localizes to AJs. The nectin-afadin complex has a potency to recruit the E-cadherin-beta-catenin complex through alpha-catenin in a manner independent of ponsin. By the use of cadherin-deficient L cell lines stably expressing various components of the cadherin-catenin and nectin-afadin systems, and alpha-catenin-deficient F9 cell lines, we examined here whether nectin recruits ZO-1 to nectin-based cell-cell adhesion sites. Nectin showed a potency to recruit not only alpha-catenin but also ZO-1 to nectin-based cell-cell adhesion sites. This recruitment of ZO-1 was dependent on afadin but independent of alpha-catenin and ponsin. These results indicate that ZO-1 localizes to cadherin-based AJs through interactions not only with alpha-catenin but also with the nectin-afadin system.

Indexed as

alpha CateninAnimalsBinding SitesCadherinsCell AdhesionCell Adhesion MoleculesCell LineCells, CulturedChromatography, AffinityCytoskeletal ProteinsCytoskeletonGenetic VectorsHumansKinesinsMembrane ProteinsMiceafadinAFDN protein, humanAfdn protein, mousealpha CateninCadherinsCell Adhesion MoleculesCTNNA1 protein, humanCtnna1 protein, mouseCytoskeletal ProteinsKinesinsMembrane ProteinsMicrofilament ProteinsMyosinsNectinsPhosphoproteinsponsinRecombinant Fusion ProteinsTJP1 protein, humanTjp1 protein, mouseZonula Occludens-1 Protein

Identifiers

PMID11408571
PMCPMC37327
OpenAlexW2069135314

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.