Evidence map›Paper›PMID 7929560›Full record

ArticleThe Journal of cell biology1994

Identification of the plakoglobin-binding domain in desmoglein and its role in plaque assembly and intermediate filament anchorage.

S M Troyanovsky, R B Troyanovsky, L G Eshkind, V A Krutovskikh, R E Leube, W W Franke

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.1field-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

36 citing papers in PubMed, 136 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Understanding the molecular basis of cardiomyopathy.American journal of physiology. Heart and circulatory physiology · 2022
    Review
  5. The desmosome as a model for lipid raft driven membrane domain organization.Biochimica et biophysica acta. Biomembranes · 2020
    Review
  6. Review
  7. Article
  8. Article
  9. Cell adhesion in epidermal development and barrier formation.Current topics in developmental biology · 2015
    Review
  10. Article
  11. Mechanistic basis of desmosome-targeted diseases.Journal of molecular biology · 2013
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. The desmosome and pemphigus.Histochemistry and cell biology · 2008
    Review
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 2 institutions in 2 countries.

S M TroyanovskyDivision of Cell Biology, Germany Cancer Research Center, Heidelberg.
R B Troyanovsky
L G Eshkind
V A Krutovskikh
R E Leube
W W Franke
German Cancer Research Center · DEWashington University in St. Louis · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The carboxyterminal cytoplasmic portions (tails) of desmosomal cadherins of both the desmoglein (Dsg) and desmocollin type are integral components of the desmosomal plaque and are involved in desmosome assembly and the anchorage of intermediate-sized filaments. When additional Dsg tails were introduced by cDNA transfection into cultured human epithelial cells, in the form of chimeras with the aminoterminal membrane insertion domain of rat connexin32 (Co32), the resulting stably transfected cells showed a dominant-negative defect specific for desmosomal junctions: despite the continual presence of all desmosomal proteins, the endogenous desmosomes disappeared and the formation of Co32-Dsg chimeric gap junctions was inhibited. Using cell transfection in combination with immunoprecipitation techniques, we have examined a series of deletion mutants of the Dsg1 tail in Co32-Dsg chimeras. We show that upon removal of the last 262 amino acids the truncated Dsg tail still effects the binding of plakoglobin but not of detectable amounts of any catenin and induces the dominant-negative phenotype. However, further truncation or excision of the next 41 amino acids, which correspond to the highly conserved carboxyterminus of the C-domain in other cadherins, abolishes plakoglobin binding and allows desmosomes to reform. Therefore, we conclude that this short segment provides a plakoglobin-binding site and is important for plaque assembly and the specific anchorage of either actin filaments in adherens junctions or IFs in desmosomes.

Indexed as

Amino Acid SequenceAnimalsBase SequenceCell AdhesionConnexinsCytoskeletal ProteinsDesmocollinsDesmoglein 1DesmogleinsDesmoplakinsDesmosomesEpithelial Cellsgamma CateninGap Junction beta-1 ProteinHumansIntermediate FilamentsConnexinsCytoskeletal ProteinsDesmocollinsDesmoglein 1DesmogleinsDesmoplakinsDSG1 protein, humangamma CateninGap Junction beta-1 ProteinRecombinant Fusion Proteins

Identifiers

PMID7929560
PMCPMC2120186
OpenAlexW1977552066

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.