Evidence map›Paper›PMID 34445214›Full record

ArticleInternational journal of molecular sciences2021

USP48 Governs Cell Cycle Progression by Regulating the Protein Level of Aurora B.

Ainsley Mike Antao, Kamini Kaushal, Soumyadip Das, Vijai Singh, Bharathi Suresh, Kye-Seong Kim, Suresh Ramakrishna

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.0field-weighted citation impact, top 29% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Chromatin Perturbation Promotes Susceptibility to Hypomethylating Agents.bioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Review
  8. Article
  9. Dual role of deubiquitinating enzyme USP19 regulates mitotic progression and tumorigenesis by stabilizing survivin.Molecular therapy : the journal of the American Society of Gene Therapy · 2022
    Article
  10. Article
  11. Article
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 2 institutions in 2 countries.

Ainsley Mike AntaoGraduate School of Biomedical Science and Engineering, Hanyang University, Seoul 04763, Korea.
Kamini KaushalGraduate School of Biomedical Science and Engineering, Hanyang University, Seoul 04763, Korea.ORCID 0000-0002-0075-3251
Soumyadip DasGraduate School of Biomedical Science and Engineering, Hanyang University, Seoul 04763, Korea.
Vijai SinghDepartment of Biosciences, School of Science, Indrashil University, Rajpur, Ahmedabad 382740, Gujarat, India.ORCID 0000-0002-6394-4370
Bharathi SureshGraduate School of Biomedical Science and Engineering, Hanyang University, Seoul 04763, Korea.
Kye-Seong KimGraduate School of Biomedical Science and Engineering, Hanyang University, Seoul 04763, Korea.ORCID 0000-0001-5550-1660
Suresh RamakrishnaGraduate School of Biomedical Science and Engineering, Hanyang University, Seoul 04763, Korea.
Hanyang University · KRIndrashil University · IN

Funding

National Research Foundation of Korea 2017M3A9B3061830; 2017M3A9C6061361; 2017M3A9E4048172; 2021R1I1A1A01052637
6 · The paper itself

Abstract

Deubiquitinating enzymes play key roles in the precise modulation of Aurora B-an essential cell cycle regulator. The expression of Aurora B increases before the onset of mitosis and decreases during mitotic exit; an imbalance in these levels has a severe impact on the fate of the cell cycle. Dysregulation of Aurora B can lead to aberrant chromosomal segregation and accumulation of errors during mitosis, eventually resulting in cytokinesis failure. Thus, it is essential to identify the precise regulatory mechanisms that modulate Aurora B levels during the cell division cycle. Using a deubiquitinase knockout strategy, we identified USP48 as an important candidate that can regulate Aurora B protein levels during the normal cell cycle. Here, we report that USP48 interacts with and stabilizes the Aurora B protein. Furthermore, we showed that the deubiquitinating activity of USP48 helps to maintain the steady-state levels of Aurora B protein by regulating its half-life. Finally, USP48 knockout resulted in delayed progression of cell cycle due to accumulation of mitotic defects and ultimately cytokinesis failure, suggesting the role of USP48 in cell cycle regulation.

Indexed as

CytokinesisMitosisAurora Kinase BEnzyme StabilityHEK293 CellsHeLa CellsHumansUbiquitin-Specific ProteasesAURKB protein, humanAurora Kinase BUbiquitin-Specific ProteasesUSP48 protein, humanaurora kinaseCRISPR/Cas9DUBsgene knockoutmitotic regulatorpost-translational modifications

Identifiers

PMID34445214
PMCPMC8395203
OpenAlexW3187557468

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.