Evidence map›Paper›PMID 29391412›Full record

ArticleScientific reports2018

The paxillin-plectin-EPLIN complex promotes apical elimination of RasV12-transformed cells by modulating HDAC6-regulated tubulin acetylation.

Nobuhiro Kasai, Ailijiang Kadeer, Mihoko Kajita, Sayaka Saitoh, Susumu Ishikawa, Takeshi Maruyama, Yasuyuki Fujita

Open 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. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Tubulin Acetylation: A Critical Regulator of Microtubule Function.Results and problems in cell differentiation · 2025
    Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. HDAC6: A unique HDAC family member as a cancer target.Cellular oncology (Dordrecht, Netherlands) · 2022
    Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. 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

7 authors at 1 institution in 1 country.

Nobuhiro KasaiDivision of Molecular Oncology, Institute for Genetic Medicine, Hokkaido University, Sapporo, 060-0815, Japan.
Ailijiang KadeerDivision of Molecular Oncology, Institute for Genetic Medicine, Hokkaido University, Sapporo, 060-0815, Japan.
Mihoko KajitaDivision of Molecular Oncology, Institute for Genetic Medicine, Hokkaido University, Sapporo, 060-0815, Japan.
Sayaka SaitohDivision of Molecular Oncology, Institute for Genetic Medicine, Hokkaido University, Sapporo, 060-0815, Japan.
Susumu IshikawaDivision of Molecular Oncology, Institute for Genetic Medicine, Hokkaido University, Sapporo, 060-0815, Japan.
Takeshi MaruyamaDivision of Molecular Oncology, Institute for Genetic Medicine, Hokkaido University, Sapporo, 060-0815, Japan. tmaru@igm.hokudai.ac.jp.
Yasuyuki FujitaDivision of Molecular Oncology, Institute for Genetic Medicine, Hokkaido University, Sapporo, 060-0815, Japan. yasu@igm.hokudai.ac.jp.
Hokkaido University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recent studies have revealed that newly emerging RasV12-transformed cells are often apically extruded from the epithelial layer. During this cancer preventive process, cytoskeletal proteins plectin and Epithelial Protein Lost In Neoplasm (EPLIN) are accumulated in RasV12 cells that are surrounded by normal cells, which positively regulate the apical elimination of transformed cells. However, the downstream regulators of the plectin-EPLIN complex remain to be identified. In this study, we have found that paxillin binds to EPLIN specifically in the mix culture of normal and RasV12-transformed cells. In addition, paxillin is accumulated in RasV12 cells surrounded by normal cells. Paxillin, plectin and EPLIN mutually influence their non-cell-autonomous accumulation, and paxillin plays a crucial role in apical extrusion of RasV12 cells. We also demonstrate that in RasV12 cells surrounded by normal cells, acetylated tubulin is accumulated. Furthermore, acetylation of tubulin is promoted by paxillin that suppresses the activity of histone deacetylase (HDAC) 6. Collectively, these results indicate that in concert with plectin and EPLIN, paxillin positively regulates apical extrusion of RasV12-transformed cells by promoting microtubule acetylation. This study shed light on the unexplored events occurring at the initial stage of carcinogenesis and would potentially lead to a novel type of cancer preventive medicine.

Indexed as

AcetylationAnimalsCell Transformation, NeoplasticCytoskeletal ProteinsDogsHistone Deacetylase 6KidneyMadin Darby Canine Kidney CellsMutationPaxillinPlectinProto-Oncogene Proteins p21(ras)TubulinTubulin ModulatorsCytoskeletal ProteinsHistone Deacetylase 6PaxillinPlectinProto-Oncogene Proteins p21(ras)TubulinTubulin Modulators

Identifiers

PMID29391412
PMCPMC5794774
OpenAlexW2805947568

What OpenQuestion holds

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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.