Evidence map›Paper›PMID 12707304›Full record

ArticleThe Journal of cell biology2003

Defining desmosomal plakophilin-3 interactions.

Stefan Bonné, Barbara Gilbert, Mechthild Hatzfeld, Xinyu Chen, Kathleen J Green, Frans van Roy

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

77 citing papers in PubMed, 160 citations in OpenAlex.

  1. Article
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  4. Plakophilin 3 Is Involved in Basal Body Docking in Multiciliated Cells.International journal of molecular sciences · 2025
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  15. International journal of molecular sciences · 2022
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17 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

6 authors at 3 institutions in 2 countries.

Stefan BonnéMolecular Cell Biology Unit, Department for Molecular Biomedical Research, Flanders Interuniversity Institute for Biotechnology (VIB)-Ghent University, B-9000 Ghent, Belgium.
Barbara Gilbert
Mechthild Hatzfeld
Xinyu Chen
Kathleen J Green
Frans van Roy
Northwestern University · USVlaams Instituut voor Biotechnologie · BEGhent University · BE

Funding

MOLECULAR GENETICS OF PEMPHIGUS FOLIACEUS ANTIGENR01AR041836 · NIAMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Kathleen Janee Green · 1993 to 2026
$11.8M
Regulation of Cell-Cell Junction Structure and Dynamics in Oral Tumor CellP01DE012328 · NIDCR · NORTHWESTERN UNIVERSITY AT CHICAGO · PI JONES, JONATHAN C. · 1997 to 2006
$7.3M
DESMOPLAKIN FUNCTION IN EPIDERMISR01AR043380 · NIAMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Kathleen Janee Green · 1996 to 2026
$7.0M
Desmoplakin Assembly and Function in EpidermisR37AR043380 · NIAMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI GREEN, KATHLEEN JANEE · 2011 to 2020
$4.6M
NIAMS NIH HHS AR41836NIAMS NIH HHS AR43380NIAMS NIH HHS R01 AR041836NIAMS NIH HHS R01 AR043380NIAMS NIH HHS R37 AR043380NIDCR NIH HHS P01 DE012328NIDCR NIH HHS P01 DE12328
6 · The paper itself

Abstract

Plakophilin 3 (PKP3) is a recently described armadillo protein of the desmosomal plaque, which is synthesized in simple and stratified epithelia. We investigated the localization pattern of endogenous and exogenous PKP3 and fragments thereof. The desmosomal binding properties of PKP3 were determined using yeast two-hybrid, coimmunoprecipitation and colocalization experiments. To this end, novel mouse anti-PKP3 mAbs were generated. We found that PKP3 binds all three desmogleins, desmocollin (Dsc) 3a and -3b, and possibly also Dsc1a and -2a. As such, this is the first protein interaction ever observed with a Dsc-b isoform. Moreover, we determined that PKP3 interacts with plakoglobin, desmoplakin (DP) and the epithelial keratin 18. Evidence was found for the presence of at least two DP-PKP3 interaction sites. This finding might explain how lateral DP-PKP interactions are established in the upper layers of stratified epithelia, increasing the size of the desmosome and the number of anchoring points available for keratins. Together, these results show that PKP3, whose epithelial and epidermal desmosomal expression pattern and protein interaction repertoire are broader than those of PKP1 and -2, is a unique multiprotein binding element in the basic architecture of a vast majority of epithelial desmosomes.

Indexed as

AnimalsCell AdhesionCell Adhesion MoleculesCell MembraneCytoskeletal ProteinsDesmocollinsDesmogleinsDesmoplakinsDesmosomesEpithelial CellsFluorescent Antibody Techniquegamma CateninHumansKeratinsMembrane GlycoproteinsMiceCell Adhesion MoleculesCytoskeletal ProteinsDesmocollinsDesmogleinsDesmoplakinsDSC1 protein, humanDsc1 protein, mouseDSP protein, humanDsp protein, mousegamma CateninKeratinsMembrane GlycoproteinsPKP1 protein, humanPkp1 protein, mousePKP3 protein, humanPkp3 protein, mousePlakophilinsProtein Isoforms

Identifiers

PMID12707304
PMCPMC2172904
OpenAlexW2132657695

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.