Evidence map›Paper›PMID 32678227›Full record

ArticleScientific reports2020

Cdc42 regulates cell polarization and contractile actomyosin rings during terminal differentiation of human erythroblasts.

Kumi Ubukawa, Tatsufumi Goto, Ken Asanuma, Yumi Sasaki, Yong-Mei Guo, Isuzu Kobayashi, Kenichi Sawada, Hideki Wakui, Naoto Takahashi

Abstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
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  8. Article
  9. Article
  10. Erythroblast enucleation at a glance.Journal of cell science · 2024
    Review
  11. Science advances · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
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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.

Kumi Ubukawa *Department of Hematology, Nephrology, and Rheumatology, Graduate School of Medicine, Akita University, Akita, Japan. ubukawak@med.akita-u.ac.jp.
Tatsufumi Goto *Department of Life Science, Graduate School of Engineering Science, Akita University, Akita, Japan.
Ken AsanumaDivision of Radio Isotope, Bioscience Education and Research Support Center, Akita University, Akita, Japan.
Yumi SasakiDepartment of Life Science, Graduate School of Engineering Science, Akita University, Akita, Japan.
Yong-Mei GuoDepartment of Hematology, Nephrology, and Rheumatology, Graduate School of Medicine, Akita University, Akita, Japan.
Isuzu KobayashiDepartment of Hematology, Nephrology, and Rheumatology, Graduate School of Medicine, Akita University, Akita, Japan.
Kenichi SawadaHokubukai Utsukushigaoka Hospital, Sapporo, Japan.
Hideki WakuiDepartment of Life Science, Graduate School of Engineering Science, Akita University, Akita, Japan.
Naoto TakahashiDepartment of Hematology, Nephrology, and Rheumatology, Graduate School of Medicine, Akita University, Akita, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The molecular mechanisms involved in the terminal differentiation of erythroblasts have been elucidated by comparing enucleation and cell division. Although various similarities and differences between erythroblast enucleation and cytokinesis have been reported, the mechanisms that control enucleation remain unclear. We previously reported that dynein and microtubule-organizing centers mediated the polarization of nuclei in human erythroblasts. Moreover, the accumulation of F-actin was noted during the enucleation of erythroblasts. Therefore, during enucleation, upstream effectors in the signal transduction pathway regulating dynein or actin, such as cell division control protein 42 homolog (Cdc42), may be crucial. We herein investigated the effects of the Cdc42 inhibitor, CASIN, on cytokinesis and enucleation in colony-forming units-erythroid (CFU-Es) and mature erythroblasts (day 10). CASIN blocked the proliferation of CFU-Es and their enucleation in a dose-dependent manner. Dynein adopted an island-like distribution in the cytoplasm of non-treated CFU-Es, but was concentrated near the nucleus as a dot and co-localized with γ-tubulin in CASIN-treated cells. CASIN blocked the accumulation of F-actin in CFU-Es and day 10 cells. These results demonstrated that Cdc42 plays an important role in cytokinesis, nuclear polarization and nuclear extrusion through a relationship with dynein and actin filament organization during the terminal differentiation of erythroblasts.

Indexed as

Cell DifferentiationActomyosinBiomarkerscdc42 GTP-Binding ProteinCell NucleusErythroblastsErythroid Precursor CellsErythropoiesisFluorescent Antibody TechniqueGene ExpressionHumansImmunohistochemistryActomyosinBiomarkerscdc42 GTP-Binding ProteinCDC42 protein, human

Identifiers

PMID32678227
PMCPMC7366696

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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.