Evidence map›Paper›PMID 30778075›Full record

ArticleNature communications2019

Morphologic determinant of tight junctions revealed by claudin-3 structures.

Shun Nakamura, Katsumasa Irie, Hiroo Tanaka, Kouki Nishikawa, Hiroshi Suzuki, Yasunori Saitoh, Atsushi Tamura, Sachiko Tsukita, Yoshinori Fujiyoshi

Abstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing 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

55 citing papers in PubMed.

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  9. "Design principles of a membrane-spanning ubiquitin ligase".bioRxiv : the preprint server for biology · 2025
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  12. Computational and structural biotechnology journal · 2025
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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

9 authors.

Shun NakamuraCellular and Structural Physiology Institute, Nagoya University, Furo-cho, Chikusa, Nagoya, 464-8601, Japan.
Katsumasa IrieCellular and Structural Physiology Institute, Nagoya University, Furo-cho, Chikusa, Nagoya, 464-8601, Japan.
Hiroo TanakaLaboratory of Biological Science, Graduate School of Frontier Biosciences and Graduate School of Medicine, Osaka University, Suita, Osaka, 565-0871, Japan.
Kouki NishikawaCellular and Structural Physiology Institute, Nagoya University, Furo-cho, Chikusa, Nagoya, 464-8601, Japan.
Hiroshi SuzukiCellular and Structural Physiology Institute, Nagoya University, Furo-cho, Chikusa, Nagoya, 464-8601, Japan.ORCID http://orcid.org/0000-0001-5371-6385
Yasunori SaitohCellular and Structural Physiology Institute, Nagoya University, Furo-cho, Chikusa, Nagoya, 464-8601, Japan.
Atsushi TamuraLaboratory of Biological Science, Graduate School of Frontier Biosciences and Graduate School of Medicine, Osaka University, Suita, Osaka, 565-0871, Japan.
Sachiko TsukitaLaboratory of Biological Science, Graduate School of Frontier Biosciences and Graduate School of Medicine, Osaka University, Suita, Osaka, 565-0871, Japan.
Yoshinori FujiyoshiCellular and Structural Physiology Institute, Nagoya University, Furo-cho, Chikusa, Nagoya, 464-8601, Japan. yoshi@cespi.nagoya-u.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tight junction is a cell adhesion apparatus functioning as barrier and/or channel in the paracellular spaces of epithelia. Claudin is the major component of tight junction and polymerizes to form tight junction strands with various morphologies that may correlate with their functions. Here we present the crystal structure of mammalian claudin-3 at 3.6 Å resolution. The third transmembrane helix of claudin-3 is clearly bent compared with that of other subtypes. Structural analysis of additional two mutants with a single mutation representing other subtypes in the third helix indicates that this helix takes a bent or straight structure depending on the residue. The presence or absence of the helix bending changes the positions of residues related to claudin-claudin interactions and affects the morphology and adhesiveness of the tight junction strands. These results evoke a model for tight junction strand formation with different morphologies - straight or curvy strands - observed in native epithelia.

Indexed as

AnimalsCell LineClaudin-3Crystallography, X-RayEnterotoxinsMiceMicroscopy, ElectronModels, MolecularMutationProtein ConformationTight JunctionsClaudin-3enterotoxin, ClostridiumEnterotoxins

Identifiers

PMID30778075
PMCPMC6379431

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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 OpenQuestion graph.