Evidence map›Paper›PMID 20213273›Full record

ArticleCellular and molecular life sciences : CMLS2010

Tricellulin forms homomeric and heteromeric tight junctional complexes.

Julie K Westphal, Max J Dörfel, Susanne M Krug, Jimmi D Cording, Jörg Piontek, Ingolf E Blasig, Rudolf Tauber, Michael Fromm, Otmar Huber

Abstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Dietary supplementation withAnimal nutrition (Zhongguo xu mu shou yi xue hui) · 2021
    Article
  2. Review
  3. Tight Junctions as Targets and Effectors of Mucosal Immune Homeostasis.Cellular and molecular gastroenterology and hepatology · 2020
    Review
  4. Structural Features of Tight-Junction Proteins.International journal of molecular sciences · 2019
    Review
  5. Apoptotic Fragmentation of Tricellulin.International journal of molecular sciences · 2019
    Article
  6. Article
  7. SUMOylation regulates the intracellular fate of ZO-2.Cellular and molecular life sciences : CMLS · 2017
    Article
  8. The intestinal epithelial barrier: a therapeutic target?Nature reviews. Gastroenterology & hepatology · 2017
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Regulation of intestinal epithelial permeability by tight junctions.Cellular and molecular life sciences : CMLS · 2013
    Review
  16. Article
  17. Review
  18. Review
  19. Claudins and tricellulin in fibrolamellar hepatocellular carcinoma.Virchows Archiv : an international journal of pathology · 2011
    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.

Julie K WestphalInstitute of Biochemistry II, Jena University Hospital, Nonnenplan 2, 07743, Jena, Germany.
Max J Dörfel
Susanne M Krug
Jimmi D Cording
Jörg Piontek
Ingolf E Blasig
Rudolf Tauber
Michael Fromm
Otmar Huber

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sealing of the paracellular cleft by tight junctions is of central importance for epithelia and endothelia to function as efficient barriers between the extracellular space and the inner milieu. Occludin and claudins represent the major tight junction components involved in establishing this barrier function. A special situation emerges at sites where three cells join together. Tricellulin, a recently identified tetraspan protein concentrated at tricellular contacts, was reported to organize tricellular as well as bicellular tight junctions. Here we show that in MDCK cells, the tricellulin C-terminus is important for the basolateral translocation of tricellulin, whereas the N-terminal domain appears to be involved in directing tricellulin to tricellular contacts. In this respect, identification of homomeric tricellulin-tricellulin and of heteromeric tricellulin-occludin complexes extends a previously published model and suggests that tricellulin and occludin are transported together to the edges of elongating bicellular junctions and get separated when tricellular contacts are formed.

Indexed as

Cell LineClaudinsEpitheliumExtracellular SpaceHumansMembrane ProteinsOccludinProtein TransportTetraspaninsTight JunctionsClaudinsMembrane ProteinsOccludinOCLN protein, humanTetraspaninsTSPAN32 protein, human

Identifiers

PMID20213273
PMCPMC11115662

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.