Evidence map›Paper›PMID 31819079›Full record

ArticleScientific reports2019

Cdc7 kinase stimulates Aurora B kinase in M-phase.

Sayuri Ito, Hidemasa Goto, Kinue Kuniyasu, Mayumi Shindo, Masayuki Yamada, Kozo Tanaka, Gaik-Theng Toh, Masaaki Sawa, Masaki Inagaki, Jiri Bartek and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

9 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Context-Dependent Function of Long Noncoding RNAMolecular and cellular biology · 2022
    Article
  3. Review
  4. Article
  5. Article
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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

11 authors at 5 institutions in 4 countries.

Sayuri ItoDepartment of Genome Medicine, Tokyo Metropolitan Institute of Medical Science, Tokyo, 156-8506, Japan.
Hidemasa GotoDepartment of Neural Regeneration and Cell Communication, Mie University Graduate School of Medicine, Tsu, Mie, 514-8507, Japan.
Kinue KuniyasuDepartment of Molecular Oncology, Institute of Development, Aging and Cancer, Tohoku University, Sendai, 980-8575, Japan.
Mayumi ShindoLaboratory of Protein Analyses, Tokyo Metropolitan Institute of Medical Science, Tokyo, 156-8506, Japan.
Masayuki YamadaMedical Education Center, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
Kozo TanakaDepartment of Molecular Oncology, Institute of Development, Aging and Cancer, Tohoku University, Sendai, 980-8575, Japan.
Gaik-Theng TohDepartment of Genome Medicine, Tokyo Metropolitan Institute of Medical Science, Tokyo, 156-8506, Japan.
Masaaki SawaCarna Biosciences, Inc., Kobe, Japan.ORCID http://orcid.org/0000-0002-0077-2188
Masaki InagakiDepartment of Physiology, Mie University Graduate School of Medicine, Tsu, Mie, 514-8507, Japan.
Jiri BartekInstitute of Molecular and Translational Medicine, Faculty of Medicine and Dentistry, Palacky University, 77900, Olomouc, Czech Republic.
Hisao MasaiDepartment of Genome Medicine, Tokyo Metropolitan Institute of Medical Science, Tokyo, 156-8506, Japan. masai-hs@igakuken.or.jp.
Tokyo Metropolitan Institute of Medical Science · JPMie University · JPTohoku University · JPKarolinska Institutet · SEKyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The conserved serine-threonine kinase, Cdc7, plays a crucial role in initiation of DNA replication by facilitating the assembly of an initiation complex. Cdc7 is expressed at a high level and exhibits significant kinase activity not only during S-phase but also during G2/M-phases. A conserved mitotic kinase, Aurora B, is activated during M-phase by association with INCENP, forming the chromosome passenger complex with Borealin and Survivin. We show that Cdc7 phosphorylates and stimulates Aurora B kinase activity in vitro. We identified threonine-236 as a critical phosphorylation site on Aurora B that could be a target of Cdc7 or could be an autophosphorylation site stimulated by Cdc7-mediated phosphorylation elsewhere. We found that threonines at both 232 (that has been identified as an autophosphorylation site) and 236 are essential for the kinase activity of Aurora B. Cdc7 down regulation or inhibition reduced Aurora B activity in vivo and led to retarded M-phase progression. SAC imposed by paclitaxel was dramatically reversed by Cdc7 inhibition, similar to the effect of Aurora B inhibition under the similar situation. Our data show that Cdc7 contributes to M-phase progression and to spindle assembly checkpoint most likely through Aurora B activation.

Indexed as

AnimalsAurora Kinase BCell CycleCell Cycle ProteinsCell DivisionCell Line, TumorCentromereChromosomal Proteins, Non-HistoneHCT116 CellsHEK293 CellsHeLa CellsHumansInsectaMitosisMutationPhosphorylationAURKB protein, humanAurkb protein, ratAurora Kinase BBirc5 protein, ratCDC7 protein, humanCell Cycle ProteinsChromosomal Proteins, Non-HistoneProtein Serine-Threonine KinasesSurvivinThreonine

Identifiers

PMID31819079
PMCPMC6901529
OpenAlexW2994537393

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.