Evidence map›Paper›PMID 20177074›Full record

ArticleThe Journal of biological chemistry2010

Identification of Myb-binding protein 1A (MYBBP1A) as a novel substrate for aurora B kinase.

Claudia Perrera, Riccardo Colombo, Barbara Valsasina, Patrizia Carpinelli, Sonia Troiani, Michele Modugno, Laura Gianellini, Paolo Cappella, Antonella Isacchi, Jurgen Moll and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

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  11. Epigeneitc silencing of ribosomal RNA genes by Mybbp1a.Journal of biomedical science · 2012
    Article
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  17. WSTF does it all: a multifunctional protein in transcription, repair, and replication.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2011
    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

11 authors at 1 institution in 1 country.

Claudia PerreraNerviano Medical Sciences, Nerviano 20014 MI, Italy. Claudia.Perrera@nervianoms.com
Riccardo Colombo
Barbara Valsasina
Patrizia Carpinelli
Sonia Troiani
Michele Modugno
Laura Gianellini
Paolo Cappella
Antonella Isacchi
Jurgen Moll
Luisa Rusconi
Nerviano Medical Sciences · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aurora kinases are mitotic enzymes involved in centrosome maturation and separation, spindle assembly and stability, and chromosome condensation, segregation, and cytokinesis and represent well known targets for cancer therapy because their deregulation has been linked to tumorigenesis. The availability of suitable markers is of crucial importance to investigate the functions of Auroras and monitor kinase inhibition in in vivo models and in clinical trials. Extending the knowledge on Aurora substrates could help to better understand their biology and could be a source for clinical biomarkers. Using biochemical, mass spectrometric, and cellular approaches, we identified MYBBP1A as a novel Aurora B substrate and serine 1303 as the major phosphorylation site. MYBBP1A is phosphorylated in nocodazole-arrested cells and is dephosphorylated upon Aurora B silencing or by treatment with Danusertib, a small molecule inhibitor of Aurora kinases. Furthermore, we show that MYBBP1A depletion by RNA interference causes mitotic progression delay and spindle assembly defects. MYBBP1A has until now been described as a nucleolar protein, mainly involved in transcriptional regulation. The results presented herein show MYBBP1A as a novel Aurora B kinase substrate and reveal a not yet recognized link of this nucleolar protein to mitosis.

Indexed as

Amino Acid SequenceAurora Kinase BAurora KinasesBinding SitesCell LineDNA-Binding ProteinsHeLa CellsHumansNuclear ProteinsNucleocytoplasmic Transport ProteinsPhosphorylationProtein Kinase InhibitorsProtein Serine-Threonine KinasesRecombinant ProteinsRNA-Binding ProteinsRNA InterferenceAURKB protein, humanAurora Kinase BAurora KinasesDNA-Binding ProteinsMYBBP1A protein, humanNuclear ProteinsNucleocytoplasmic Transport ProteinsProtein Kinase InhibitorsProtein Serine-Threonine KinasesRecombinant ProteinsRNA-Binding ProteinsSerineTranscription Factors

Identifiers

PMID20177074
PMCPMC2852913
OpenAlexW2035762270

What OpenQuestion holds

Textmetadata
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.