Evidence map›Paper›PMID 24782306›Full record

ArticleThe Journal of biological chemistry2014

Desmoglein 2 compensates for desmoglein 3 but does not control cell adhesion via regulation of p38 mitogen-activated protein kinase in keratinocytes.

Eva Hartlieb, Vera Rötzer, Mariya Radeva, Volker Spindler, Jens Waschke

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
5.1field-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

26 citing papers in PubMed, 52 citations in OpenAlex.

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  11. Dsg3 epitope-specific signalling in pemphigus.Frontiers in immunology · 2023
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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

5 authors at 1 institution in 1 country.

Eva HartliebFrom the Institute of Anatomy and Cell Biology, Department I, Ludwig-Maximilians-Universität Munich, 80336 Munich, Germany.
Vera RötzerFrom the Institute of Anatomy and Cell Biology, Department I, Ludwig-Maximilians-Universität Munich, 80336 Munich, Germany.
Mariya RadevaFrom the Institute of Anatomy and Cell Biology, Department I, Ludwig-Maximilians-Universität Munich, 80336 Munich, Germany.
Volker SpindlerFrom the Institute of Anatomy and Cell Biology, Department I, Ludwig-Maximilians-Universität Munich, 80336 Munich, Germany.
Jens WaschkeFrom the Institute of Anatomy and Cell Biology, Department I, Ludwig-Maximilians-Universität Munich, 80336 Munich, Germany jens.waschke@med.uni-muenchen.de.
Ludwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Desmosomal cadherins are transmembrane adhesion molecules that provide cell adhesion by interacting in the intercellular space of adjacent cells. In keratinocytes, several desmoglein (Dsg1-4) and desmocollin (Dsc1-3) isoforms are coexpressed. We have shown previously that Dsg2 is less important for keratinocyte cohesion compared with Dsg3 and that the latter forms a complex with p38 MAPK. In this study, we compared the involvement of Dsg2 and Dsg3 in the p38 MAPK-dependent regulation of keratinocyte cohesion. We show that loss of cell adhesion and keratin filament retraction induced by Dsg3 depletion is ameliorated by specific p38 MAPK inhibition. Furthermore, in contrast to depletion of Dsg2, siRNA-mediated silencing of Dsg3 induced p38 MAPK activation, which is in line with immunoprecipitation experiments demonstrating the interaction of activated p38 MAPK with Dsg3 but not with Dsg2. Cell fractionation into a cytoskeleton-unbound and a cytoskeleton-anchored desmosome-containing pool revealed that Dsg3, in contrast to Dsg2, is present in relevant amounts in the unbound pool in which activated p38 MAPK is predominantly detectable. Moreover, because loss of cell adhesion by Dsg3 depletion was partially rescued by p38 MAPK inhibition, we conclude that, besides its function as an adhesion molecule, Dsg3 is strengthening cell cohesion via modulation of p38 MAPK-dependent keratin filament reorganization. Nevertheless, because subsequent targeting of Dsg3 in Dsg2-depleted cells led to drastically enhanced keratinocyte dissociation and Dsg2 was enhanced at the membrane in Dsg3 knockout cells, we conclude that Dsg2 compensates for Dsg3 loss of function.

Indexed as

AnimalsCell AdhesionCell LineCytoskeletonDesmoglein 2Desmoglein 3DesmosomesHumansKeratinocytesMicep38 Mitogen-Activated Protein KinasesDesmoglein 2Desmoglein 3Dsg2 protein, mouseDsg3 protein, mousep38 Mitogen-Activated Protein KinasesCell AdhesionDesmosomeKeratinocytep38 MAPKPemphigus

Identifiers

PMID24782306
PMCPMC4059146
OpenAlexW2053073084

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.