Evidence map›Paper›PMID 30341325›Full record

ArticleScientific reports2018

AMPK-dependent phosphorylation of cingulin reversibly regulates its binding to actin filaments and microtubules.

Tomoki Yano, Takayuki Torisawa, Kazuhiro Oiwa, Sachiko Tsukita

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

20 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
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  12. The Epithelial Cell Leak Pathway.International journal of molecular sciences · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Spatial control of AMPK signaling at subcellular compartments.Critical reviews in biochemistry and molecular biology · 2020
    Review
  17. Article
  18. Review
  19. Claudin-2: Roles beyond Permeability Functions.International journal of molecular sciences · 2019
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 1 country.

Tomoki YanoLaboratory of Biological Science, Graduate School of Frontier Biosciences and Graduate School of Medicine, Osaka University, Osaka, 565-0871, Japan. t-yano@biosci.med.osaka-u.ac.jp.
Takayuki TorisawaNational Institute of Information and Communications Technology, Advanced ICT Research Institute, Kobe, Hyogo, 651-2492, Japan.
Kazuhiro OiwaNational Institute of Information and Communications Technology, Advanced ICT Research Institute, Kobe, Hyogo, 651-2492, Japan.ORCID http://orcid.org/0000-0002-1281-113X
Sachiko TsukitaLaboratory of Biological Science, Graduate School of Frontier Biosciences and Graduate School of Medicine, Osaka University, Osaka, 565-0871, Japan. atsukita@biosci.med.osaka-u.ac.jp.
The University of Osaka · JPNational Institute of Information and Communications Technology · JPThe Graduate University for Advanced Studies, SOKENDAI · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytoskeletal organization is essential for the precise morphogenesis of cells, tissues, and organs. Cytoskeletons, bound to scaffolding proteins, regulate the apical junction complex (AJC), which is composed of tight and adherens junctions, and located at the apical side of epithelial cell sheets. Cingulin is a tight junction-associated protein that binds to both actin filaments and microtubules. However, how cingulin binds to microtubules and whether cingulin can bind to actin and microtubules simultaneously are unclear. Here we examined the mechanisms behind cingulin's cytoskeleton-binding properties. First, using total internal reflection fluorescence microscopy, we detected cingulin at microtubule cross points. We then found the interdomain interactions in cingulin molecules. Notably, we found that this interaction was regulated by AMPK-dependent phosphorylation and changed cingulin's conformation and binding properties to actin filaments and microtubules. Finally, we found that the AMPK-regulated cingulin properties regulated the barrier functions of epithelial cell sheets. We propose that the cellular metabolic state, which involves AMPK, can contribute to the organization and maintenance of epithelial tissues through cingulin's tight junction/cytoskeleton regulation.

Indexed as

Protein Processing, Post-TranslationalActin CytoskeletonAMP-Activated Protein KinasesAnimalsMembrane ProteinsMiceMicroscopy, FluorescenceMicrotubulesPhosphorylationProtein BindingProtein ConformationAMP-Activated Protein KinasesCgn protein, mouseMembrane Proteins

Identifiers

PMID30341325
PMCPMC6195624
OpenAlexW2896631714

What OpenQuestion holds

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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.