Evidence map›Paper›PMID 26481195›Full record

ArticleScientific reports2015

Interaction of Cx43 with Hsc70 regulates G1/S transition through CDK inhibitor p27.

Hitoshi Hino, Ping Dai, Tatsushi Yoshida, Tomoya Hatakeyama, Yoshinori Harada, Eigo Otsuji, Tsukasa Okuda, Tetsuro Takamatsu

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Mutations of theMedicina (Kaunas, Lithuania) · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Altered translation initiation ofMolecular biology of the cell · 2018
    Article
  9. Article
  10. Article
  11. Upregulation of P27International journal of clinical and experimental pathology · 2017
    Article
  12. Article
  13. 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 at 1 institution in 1 country.

Hitoshi HinoDepartment of Pathology and Cell Regulation, Kyoto Prefectural University of Medicine, Kyoto, Japan.
Ping DaiDepartment of Pathology and Cell Regulation, Kyoto Prefectural University of Medicine, Kyoto, Japan.
Tatsushi YoshidaDepartment of Biochemistry and Molecular Biology, Kyoto Prefectural University of Medicine, Kyoto, Japan.
Tomoya HatakeyamaDepartment of Pathology and Cell Regulation, Kyoto Prefectural University of Medicine, Kyoto, Japan.
Yoshinori HaradaDepartment of Pathology and Cell Regulation, Kyoto Prefectural University of Medicine, Kyoto, Japan.
Eigo OtsujiDivision of Digestive Surgery, Department of Surgery, Kyoto Prefectural University of Medicine, Kyoto, Japan.
Tsukasa OkudaDepartment of Biochemistry and Molecular Biology, Kyoto Prefectural University of Medicine, Kyoto, Japan.
Tetsuro TakamatsuDepartment of Pathology and Cell Regulation, Kyoto Prefectural University of Medicine, Kyoto, Japan.
Kyoto Prefectural University of Medicine · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Connexin 43 (Cx43) functions as a cell growth suppressor. We have demonstrated that Cx43 interacts with heat shock cognate protein 70 (Hsc70) for regulating cell proliferation. Hsc70 interacts with CDK inhibitor p27, which regulates the assembly and subcellular localization of cyclin D1-CDK4-p27 complex. However, the involvement of p27 with Cx43-mediated cell cycle suppression is still poorly understood. Here, we report that nuclear accumulation of p27 is reduced by overexpression of Cx43, and that this reduction is restored by co-overexpression with Hsc70. We found that Cx43 competes with p27 for binding to Hsc70, and as a result, decreases the level of Hsc70 in cyclin D1-CDK4-p27 complex, leading to prevention of the nuclear translocation of the complex and the G1/S transition. Collectively, our findings suggest that, in Cx43 up-regulation, which is most likely an emergency measure, Cx43-Hsc70 interaction regulates cell cycle G1/S progression through a novel mechanism by which Cx43-Hsc70 interaction prevents the nuclear accumulation of p27 through controlling the nuclear translocation of cyclin D1-CDK4-p27 complex.

Indexed as

G1 PhaseS PhaseCell NucleusCell ProliferationConnexin 43Cyclin D1Cyclin-Dependent Kinase 4Cyclin-Dependent Kinase Inhibitor p27HSC70 Heat-Shock ProteinsHumansMultiprotein ComplexesProtein BindingProtein TransportUp-RegulationConnexin 43Cyclin D1Cyclin-Dependent Kinase 4Cyclin-Dependent Kinase Inhibitor p27HSC70 Heat-Shock ProteinsMultiprotein Complexes

Identifiers

PMID26481195
PMCPMC4612729
OpenAlexW2180447459

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.