Evidence map›Paper›PMID 42270729›Full record

ArticleScientific reports2026

A direct interaction of JAM-C with the tight junction scaffold protein ZO-2.

Annika Schulte, Mariel F Schwietzer, Frauke Brinkmann, Valentin Teuber, Sandra Citi, Mikio Furuse, Michel Aurrand-Lions, Klaus Ebnet

Abstract read
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In one paragraph

Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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

8 authors.

Annika SchulteInstitute-associated Research Group Cell Adhesion and Cell Polarity, Institute of Medical Biochemistry, ZMBE, University of Münster, Von- Esmarch-Str. 56, D-48149, Münster, Germany.
Mariel F SchwietzerInstitute-associated Research Group Cell Adhesion and Cell Polarity, Institute of Medical Biochemistry, ZMBE, University of Münster, Von- Esmarch-Str. 56, D-48149, Münster, Germany.
Frauke BrinkmannInstitute-associated Research Group Cell Adhesion and Cell Polarity, Institute of Medical Biochemistry, ZMBE, University of Münster, Von- Esmarch-Str. 56, D-48149, Münster, Germany.
Valentin TeuberInstitute-associated Research Group Cell Adhesion and Cell Polarity, Institute of Medical Biochemistry, ZMBE, University of Münster, Von- Esmarch-Str. 56, D-48149, Münster, Germany.
Sandra CitiDepartment of Molecular and Cellular Biology, University of Geneva, Geneva, 1205, Switzerland.
Mikio FuruseDivision of Cell Structure, National Institute for Physiological Sciences, National Institute of Natural Sciences, Okazaki, Aichi, Japan.
Michel Aurrand-LionsInstitut Paoli-Calmettes, CRCM, Equipe Labellisée Ligue 2020, Team Leuko/stromalinteractions in normal and pathological haematopoiesis, Aix Marseille University, CNRS, INSERM, Marseille, France.
Klaus EbnetInstitute-associated Research Group Cell Adhesion and Cell Polarity, Institute of Medical Biochemistry, ZMBE, University of Münster, Von- Esmarch-Str. 56, D-48149, Münster, Germany. ebnetk@uni-muenster.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tight junctions are sites of cell-cell contacts at the apical region of epithelial junctions that are involved in barrier formation, cellular signaling, and cell-cell adhesion. Tight junctions are formed by integral membrane proteins associated with cytoplasmic scaffolding and adapter proteins through which they are linked to the underlying actomyosin and microtubule cytoskeletons. Here, we have addressed the interaction of the Junctional Adhesion Molecule (JAM)-C with the zonula adherens (ZO) protein ZO-2. Using a combination of cell-based recruitment assays and biochemical in vitro experiments, we find that JAM-C and ZO-2 directly interact in a PDZ domain-dependent manner. Notably, the interaction requires PDZ domain 3 as well as the SH3 domain of ZO-2, indicating that ZO-2 forms a functional supramodule to interact with JAM-C. We also found that JAM-C is specifically localized to tight junctions in polarized epithelial cells and that JAM-A suppresses JAM-C mRNA expression in these cells. Our findings have implications for important aspects of tight junction biology, including mechanosensing and liquid-liquid phase separation.

Indexed as

Cell Adhesion MoleculesReceptors, Cell SurfaceTight JunctionsZonula Occludens-2 ProteinAnimalsDogsEpithelial CellsHumansMadin Darby Canine Kidney CellsPDZ DomainsProtein BindingCell Adhesion MoleculesF11R protein, humanReceptors, Cell SurfaceTJP2 protein, humanZonula Occludens-2 ProteinJAM-AJAM-CPDZ domainTight junctionZO-2

Identifiers

PMID42270729
PMCPMC13253849

What Socratic holds

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LicenceCC BY
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Registered trials

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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 Socratic graph.