Evidence map›Paper›PMID 38177906›Full record

ArticleEMBO reports2024

TMEM25 is a Par3-binding protein that attenuates claudin assembly during tight junction development.

Sachiko Kamakura, Junya Hayase, Akira Kohda, Yuko Iwakiri, Kanako Chishiki, Tomoko Izaki, Hideki Sumimoto

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
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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

7 authors at 1 institution in 1 country.

Sachiko KamakuraDepartment of Biochemistry, Kyushu University Graduate School of Medical Sciences, Fukuoka, Japan.
Junya HayaseDepartment of Biochemistry, Kyushu University Graduate School of Medical Sciences, Fukuoka, Japan.
Akira KohdaDepartment of Biochemistry, Kyushu University Graduate School of Medical Sciences, Fukuoka, Japan.
Yuko IwakiriDepartment of Biochemistry, Kyushu University Graduate School of Medical Sciences, Fukuoka, Japan.
Kanako ChishikiDepartment of Biochemistry, Kyushu University Graduate School of Medical Sciences, Fukuoka, Japan.
Tomoko IzakiDepartment of Biochemistry, Kyushu University Graduate School of Medical Sciences, Fukuoka, Japan.
Hideki SumimotoDepartment of Biochemistry, Kyushu University Graduate School of Medical Sciences, Fukuoka, Japan. sumimoto.hideki.851@m.kyushu-u.ac.jp.ORCID http://orcid.org/0000-0003-2340-9063
Kyushu University · JP

Funding

MEXT | Japan Society for the Promotion of Science (JSPS) JP21H02698MEXT | Japan Society for the Promotion of Science (JSPS) JP21H05267MEXT | Japan Society for the Promotion of Science (JSPS) JP22K06901
6 · The paper itself

Abstract

The tight junction (TJ) in epithelial cells is formed by integral membrane proteins and cytoplasmic scaffolding proteins. The former contains the claudin family proteins with four transmembrane segments, while the latter includes Par3, a PDZ domain-containing adaptor that organizes TJ formation. Here we show the single membrane-spanning protein TMEM25 localizes to TJs in epithelial cells and binds to Par3 via a PDZ-mediated interaction with its C-terminal cytoplasmic tail. TJ development during epithelial cell polarization is accelerated by depletion of TMEM25, and delayed by overexpression of TMEM25 but not by that of a C-terminally deleted protein, indicating a regulatory role of TMEM25. TMEM25 associates via its N-terminal extracellular domain with claudin-1 and claudin-2 to suppress their cis- and trans-oligomerizations, both of which participate in TJ strand formation. Furthermore, Par3 attenuates TMEM25-claudin association via binding to TMEM25, implying its ability to affect claudin oligomerization. Thus, the TJ protein TMEM25 appears to negatively regulate claudin assembly in TJ formation, which regulation is modulated by its interaction with Par3.

Indexed as

ClaudinsTight JunctionsCarrier ProteinsClaudin-1Epithelial CellsCarrier ProteinsClaudin-1ClaudinsClaudinEpithelial Cell PolarityPar3Tight Junction

Identifiers

PMID38177906
PMCPMC10897455
OpenAlexW4390025208

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.