Evidence map›Paper›PMID 24940650›Full record

ArticleThe Journal of investigative dermatology2014

Interaction of plectin with keratins 5 and 14: dependence on several plectin domains and keratin quaternary structure.

Jamal-Eddine Bouameur, Bertrand Favre, Lionel Fontao, Prakash Lingasamy, Nadja Begré, Luca Borradori

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in The Journal of investigative dermatology, 2014. 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
1.7field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
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  4. Galli-Galli Disease: A Comprehensive Literature Review.Dermatopathology (Basel, Switzerland) · 2024
    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

6 authors at 2 institutions in 1 country.

Jamal-Eddine BouameurDepartment of Dermatology, Inselspital Bern University Hospital, Bern, Switzerland; Department of Clinical Research, University of Bern, Bern, Switzerland; Graduate School for Cellular and Biomedical Sciences, University of Bern, Bern, Switzerland.
Bertrand FavreDepartment of Dermatology, Inselspital Bern University Hospital, Bern, Switzerland; Department of Clinical Research, University of Bern, Bern, Switzerland. Electronic address: Bertrand.Favre@insel.ch.
Lionel FontaoDepartment of Dermatology, Geneva University Hospital, Geneva, Switzerland.
Prakash LingasamyDepartment of Dermatology, Inselspital Bern University Hospital, Bern, Switzerland; Department of Clinical Research, University of Bern, Bern, Switzerland.
Nadja BegréDepartment of Dermatology, Inselspital Bern University Hospital, Bern, Switzerland; Department of Clinical Research, University of Bern, Bern, Switzerland.
Luca BorradoriDepartment of Dermatology, Inselspital Bern University Hospital, Bern, Switzerland; Department of Clinical Research, University of Bern, Bern, Switzerland.
University of Bern · CHUniversity Hospital of Geneva · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plectin, a cytolinker of the plakin family, anchors the intermediate filament (IF) network formed by keratins 5 and 14 (K5/K14) to hemidesmosomes, junctional adhesion complexes in basal keratinocytes. Genetic alterations of these proteins cause epidermolysis bullosa simplex (EBS) characterized by disturbed cytoarchitecture and cell fragility. The mechanisms through which mutations located after the documented plectin IF-binding site, composed of the plakin-repeat domain (PRD) B5 and the linker, as well as mutations in K5 or K14, lead to EBS remain unclear. We investigated the interaction of plectin C terminus, encompassing four domains, the PRD B5, the linker, the PRD C, and the C extremity, with K5/K14 using different approaches, including a rapid and sensitive fluorescent protein-binding assay, based on enhanced green fluorescent protein-tagged proteins (FluoBACE). Our results demonstrate that all four plectin C-terminal domains contribute to its association with K5/K14 and act synergistically to ensure efficient IF binding. The plectin C terminus predominantly interacted with the K5/K14 coil 1 domain and bound more extensively to K5/K14 filaments compared with monomeric keratins or IF assembly intermediates. These findings indicate a multimodular association of plectin with K5/K14 filaments and give insights into the molecular basis of EBS associated with pathogenic mutations in plectin, K5, or K14 genes.

Indexed as

Binding SitesCell Line, TumorEpidermolysis Bullosa SimplexHEK293 CellsHumansKeratin-14Keratin-5KeratinsMuscular DystrophiesMutationPlectinProtein BindingProtein MultimerizationProtein Structure, QuaternaryProtein Structure, TertiaryRecombinant ProteinsKeratin-14Keratin-5KeratinsPlectinRecombinant Proteins

Identifiers

PMID24940650
OpenAlexW1971953227

What OpenQuestion holds

Textmetadata
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.