Evidence map›Paper›PMID 9660880›Full record

ArticleThe Journal of cell biology1998

Hemidesmosome formation is initiated by the beta4 integrin subunit, requires complex formation of beta4 and HD1/plectin, and involves a direct interaction between beta4 and the bullous pemphigoid antigen 180.

R Q Schaapveld, L Borradori, D Geerts, M R van Leusden, I Kuikman, M G Nievers, C M Niessen, R D Steenbergen, P J Snijders, A Sonnenberg

Open access · greenAbstract read
In one paragraph

Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
11.3field-weighted citation impact, top 1% 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

61 citing papers in PubMed, 183 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Native Autoantigen Complex Detects Pemphigoid Autoantibodies.JID innovations : skin science from molecules to population health · 2023
    Article
  6. Review
  7. Review
  8. Collagen XVII deficiency alters epidermal patterning.Laboratory investigation; a journal of technical methods and pathology · 2022
    Article
  9. Article
  10. BP180/Collagen XVII: A Molecular View.International journal of molecular sciences · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. IntegraDermatology and therapy · 2018
    Article
  19. Review
  20. Article

1 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

10 authors at 3 institutions in 2 countries.

R Q SchaapveldDivision of Cell Biology, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands.
L Borradori
D Geerts
M R van Leusden
I Kuikman
M G Nievers
C M Niessen
R D Steenbergen
P J Snijders
A Sonnenberg
University of Geneva · CHVrije Universiteit Amsterdam · NLThe Netherlands Cancer Institute · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hemidesmosomes (HDs) are stable anchoring structures that mediate the link between the intermediate filament cytoskeleton and the cell substratum. We investigated the contribution of various segments of the beta4 integrin cytoplasmic domain in the formation of HDs in transient transfection studies using immortalized keratinocytes derived from an epidermolysis bullosa patient deficient in beta4 expression. We found that the expression of wild-type beta4 restored the ability of the beta4-deficient cells to form HDs and that distinct domains in the NH2- and COOH-terminal regions of the beta4 cytoplasmic domain are required for the localization of HD1/plectin and the bullous pemphigoid antigens 180 (BP180) and 230 (BP230) in these HDs. The tyrosine activation motif located in the connecting segment (CS) of the beta4 cytoplasmic domain was dispensable for HD formation, although it may be involved in the efficient localization of BP180. Using the yeast two-hybrid system, we could demonstrate a direct interaction between beta4 and BP180 which involves sequences within the COOH-terminal part of the CS and the third fibronectin type III (FNIII) repeat. Immunoprecipitation studies using COS-7 cells transfected with cDNAs for alpha6 and beta4 and a mutant BP180 which lacks the collagenous extracellular domain confirmed the interaction of beta4 with BP180. Nevertheless, beta4 mutants which contained the BP180-binding region, but lacked sequences required for the localization of HD1/plectin, failed to localize BP180 in HDs. Additional yeast two- hybrid assays indicated that the 85 COOH-terminal residues of beta4 can interact with the first NH2-terminal pair of FNIII repeats and the CS, suggesting that the cytoplasmic domain of beta4 is folded back upon itself. Unfolding of the cytoplasmic domain may be part of a mechanism by which the interaction of beta4 with other hemidesmosomal components, e.g., BP180, is regulated.

Indexed as

AnimalsAntigens, CDAutoantigensBinding SitesCarrier ProteinsCell Line, TransformedCells, CulturedCollagen Type XVIICOS CellsCytoplasmCytoskeletal ProteinsDystoninEpidermolysis Bullosa, JunctionalHumansIntegrin alpha6Integrin beta1Antigens, CDAutoantigensCarrier ProteinsCollagen Type XVIICytoskeletal ProteinsDST protein, humanDystoninIntegrin alpha6Integrin beta1Integrin beta4Intermediate Filament ProteinsNerve Tissue ProteinsNon-Fibrillar CollagensPLEC protein, humanPlectinTyrosine

Identifiers

PMID9660880
PMCPMC2133016
OpenAlexW2081121052

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.