Evidence map›Paper›PMID 34269802›Full record

ArticleThe Journal of cell biology2021

Angulin-1 seals tricellular contacts independently of tricellulin and claudins.

Taichi Sugawara, Kyoko Furuse, Tetsuhisa Otani, Tomohiko Wakayama, Mikio Furuse

Open access · greenAbstract read
In one paragraph

Article in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

24 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  4. New indicator of small intestinal ageing in senescence-accelerated mice.The journal of physiological sciences : JPS · 2025
    Article
  5. Review
  6. Article
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  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. A short guide to the tight junction.Journal of cell science · 2024
    Review
  14. The epithelium takes the stage in asthma and inflammatory bowel diseases.Frontiers in cell and developmental biology · 2024
    Review
  15. Review
  16. Article
  17. Review
  18. Review
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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

5 authors at 3 institutions in 1 country.

Taichi SugawaraDivision of Cell Structure, National Institute for Physiological Sciences, National Institute of Natural Sciences, Okazaki, Aichi, Japan.
Kyoko FuruseDivision of Cell Structure, National Institute for Physiological Sciences, National Institute of Natural Sciences, Okazaki, Aichi, Japan.ORCID 0000-0003-4304-6204
Tetsuhisa OtaniDivision of Cell Structure, National Institute for Physiological Sciences, National Institute of Natural Sciences, Okazaki, Aichi, Japan.ORCID 0000-0002-2557-6722
Tomohiko WakayamaDepartment of Histology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto, Japan.
Mikio FuruseDivision of Cell Structure, National Institute for Physiological Sciences, National Institute of Natural Sciences, Okazaki, Aichi, Japan.ORCID 0000-0003-2847-8156
The Graduate University for Advanced Studies, SOKENDAI · JPKumamoto University · JPNational Institute for Physiological Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tricellular tight junctions (tTJs) are specialized tight junctions (TJs) that seal the intercellular space at tricellular contacts (TCs), where the vertices of three epithelial cells meet. Tricellulin and angulin family membrane proteins are known constituents of tTJs, but the molecular mechanism of tTJ formation remains elusive. Here, we investigated the roles of angulin-1 and tricellulin in tTJ formation in MDCK II cells by genome editing. Angulin-1-deficient cells lost the plasma membrane contact at TCs with impaired epithelial barrier function. The C terminus of angulin-1 bound to the TJ scaffold protein ZO-1, and disruption of their interaction influenced the localization of claudins at TCs, but not the tricellular sealing. Strikingly, the plasma membrane contact at TCs was formed in tricellulin- or claudin-deficient cells. These findings demonstrate that angulin-1 is responsible for the plasma membrane seal at TCs independently of tricellulin and claudins.

Indexed as

alpha CateninAnimalsBinding SitesClaudin-2DogsExtracellular SpaceGene EditingGene Expression RegulationGene Knockout TechniquesMadin Darby Canine Kidney CellsMARVEL Domain Containing 2 ProteinOccludinProtein BindingProtein Interaction Domains and MotifsReceptors, LipoproteinSignal Transductionalpha CateninClaudin-2MARVEL Domain Containing 2 ProteinOccludinReceptors, LipoproteinTranscription FactorsZonula Occludens-1 Protein

Identifiers

PMID34269802
PMCPMC8289698
OpenAlexW3181406539

What OpenQuestion holds

Textmetadata
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.