Evidence map›Paper›PMID 31527146›Full record

ArticleThe Journal of cell biology2019

Aurora B kinase activity is regulated by SET/TAF1 on Sgo2 at the inner centromere.

Yuichiro Asai, Koh Fukuchi, Yuji Tanno, Saki Koitabashi-Kiyozuka, Tatsuyuki Kiyozuka, Yuko Noda, Rieko Matsumura, Tetsuo Koizumi, Atsushi Watanabe, Kyosuke Nagata and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2019. 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
1.7field-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

13 citing papers in PubMed, 17 citations in OpenAlex.

  1. The next decade of SET: from an oncoprotein to beyond.Journal of molecular cell biology · 2024
    Review
  2. Article
  3. Preparation of Mitotic Cells for Fluorescence Microscopy.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. SET levels contribute to cohesion fatigue.Molecular biology of the cell · 2021
    Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. 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

12 authors at 3 institutions in 2 countries.

Yuichiro Asai *Department of Chemistry and Biochemistry, School of Advanced Science and Engineering, Waseda University, Tokyo, Japan.
Koh Fukuchi *Department of Chemistry and Biochemistry, School of Advanced Science and Engineering, Waseda University, Tokyo, Japan.
Yuji Tanno *Bioscience Department, Veritas Corporation, Tokyo, Japan.
Saki Koitabashi-KiyozukaDepartment of Chemistry and Biochemistry, School of Advanced Science and Engineering, Waseda University, Tokyo, Japan.
Tatsuyuki KiyozukaDepartment of Chemistry and Biochemistry, School of Advanced Science and Engineering, Waseda University, Tokyo, Japan.
Yuko NodaDepartment of Chemistry and Biochemistry, School of Advanced Science and Engineering, Waseda University, Tokyo, Japan.
Rieko MatsumuraDepartment of Chemistry and Biochemistry, School of Advanced Science and Engineering, Waseda University, Tokyo, Japan.
Tetsuo KoizumiDepartment of Chemistry and Biochemistry, School of Advanced Science and Engineering, Waseda University, Tokyo, Japan.
Atsushi WatanabeDepartment of Chemistry and Biochemistry, School of Advanced Science and Engineering, Waseda University, Tokyo, Japan.
Kyosuke NagataDepartment of Infection Biology, Faculty of Medicine, University of Tsukuba, Tsukuba, Japan.
Yoshinori WatanabeCell Cycle Laboratory, The Francis Crick Instiute, London, UK.
Yasuhiko TeradaDepartment of Chemistry and Biochemistry, School of Advanced Science and Engineering, Waseda University, Tokyo, Japan yterada@waseda.jp.ORCID 0000-0003-4784-5273
Waseda University · JPThe Francis Crick Institute · GBUniversity of Tsukuba · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The accurate regulation of phosphorylation at the kinetochore is essential for establishing chromosome bi-orientation. Phosphorylation of kinetochore proteins by the Aurora B kinase destabilizes improper kinetochore-microtubule attachments, whereas the phosphatase PP2A has a counteracting role. Imbalanced phosphoregulation leads to error-prone chromosome segregation and aneuploidy, a hallmark of cancer cells. However, little is known about the molecular events that control the balance of phosphorylation at the kinetochore. Here, we show that localization of SET/TAF1, an oncogene product, to centromeres maintains Aurora B kinase activity by inhibiting PP2A, thereby correcting erroneous kinetochore-microtubule attachment. SET localizes at the inner centromere by interacting directly with shugoshin 2, with SET levels declining at increased distances between kinetochore pairs, leading to establishment of chromosome bi-orientation. Moreover, SET overexpression induces chromosomal instability by disrupting kinetochore-microtubule attachment. Thus, our findings reveal the novel role of SET in fine-tuning the phosphorylation level at the kinetochore by balancing the activities of Aurora B and PP2A.

Indexed as

Aurora Kinase BCell Cycle ProteinsCells, CulturedCentromereDNA-Binding ProteinsHEK293 CellsHeLa CellsHistone AcetyltransferasesHistone ChaperonesHumansTATA-Binding Protein Associated FactorsTranscription Factor TFIIDAURKB protein, humanAurora Kinase BCell Cycle ProteinsDNA-Binding ProteinsHistone AcetyltransferasesHistone ChaperonesSET protein, humanSGO2 protein, humanTATA-binding protein associated factor 250 kDaTATA-Binding Protein Associated FactorsTranscription Factor TFIID

Identifiers

PMID31527146
PMCPMC6781429
OpenAlexW2973719930

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.